AGAL_HUMAN
ID AGAL_HUMAN Reviewed; 429 AA.
AC P06280; Q6LER7;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Alpha-galactosidase A {ECO:0000305};
DE EC=3.2.1.22 {ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:27211852};
DE AltName: Full=Alpha-D-galactosidase A;
DE AltName: Full=Alpha-D-galactoside galactohydrolase;
DE AltName: Full=Galactosylgalactosylglucosylceramidase GLA {ECO:0000305};
DE AltName: Full=Melibiase;
DE AltName: INN=Agalsidase;
DE Flags: Precursor;
GN Name=GLA {ECO:0000312|HGNC:HGNC:4296};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=3036505; DOI=10.1111/j.1432-1033.1987.tb11438.x;
RA Tsuji S., Martin B.M., Kaslow D.C., Migeon B.R., Choudary P.V.,
RA Stubblefield B.K., Mayor J.A., Murray G.J., Barranger J.A., Ginns E.I.;
RT "Signal sequence and DNA-mediated expression of human lysosomal alpha-
RT galactosidase A.";
RL Eur. J. Biochem. 165:275-280(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lymphoblast;
RX PubMed=2542896; DOI=10.1093/nar/17.8.3301;
RA Kornreich R., Desnick R.J., Bishop D.F.;
RT "Nucleotide sequence of the human alpha-galactosidase A gene.";
RL Nucleic Acids Res. 17:3301-3302(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7626884; DOI=10.1007/bf00364796;
RA Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W.,
RA Gibbs R.A.;
RT "Sixty-nine kilobases of contiguous human genomic sequence containing the
RT alpha-galactosidase A and Bruton's tyrosine kinase loci.";
RL Mamm. Genome 6:334-338(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-429, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lung;
RX PubMed=3014515; DOI=10.1073/pnas.83.13.4859;
RA Bishop D.F., Calhoun D.H., Bernstein H.S., Hantzopoulos P., Quinn M.,
RA Desnick R.J.;
RT "Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding
RT the mature enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4859-4863(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RX PubMed=2892762; DOI=10.1016/0378-1119(87)90374-x;
RA Quinn M., Hantzopoulos P., Fidanza V., Calhoun D.H.;
RT "A genomic clone containing the promoter for the gene encoding the human
RT lysosomal enzyme, alpha-galactosidase A.";
RL Gene 58:177-188(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RX PubMed=2836863; DOI=10.1073/pnas.85.11.3903;
RA Bishop D.F., Kornreich R., Desnick R.J.;
RT "Structural organization of the human alpha-galactosidase A gene: further
RT evidence for the absence of a 3' untranslated region.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3903-3907(1988).
RN [9]
RP RNA EDITING OF POSITION 396.
RX PubMed=7503918; DOI=10.1093/nar/23.14.2636;
RA Novo F.J., Kruszewski A., McDermot K.D., Goldspink G., Gorecki D.C.;
RT "Editing of human alpha-galactosidase RNA resulting in a pyrimidine to
RT purine conversion.";
RL Nucleic Acids Res. 23:2636-2640(1995).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=8804427; DOI=10.1016/0014-5793(96)00863-0;
RA Kase R., Bierfreund U., Klein A., Kolter T., Itoh K., Suzuki M.,
RA Hashimoto Y., Sandhoff K., Sakuraba H.;
RT "Only sphingolipid activator protein B (SAP-B or saposin B) stimulates the
RT degradation of globotriaosylceramide by recombinant human lysosomal alpha-
RT galactosidase in a detergent-free liposomal system.";
RL FEBS Lett. 393:74-76(1996).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-215.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 32-422 IN COMPLEX WITH PRODUCT,
RP HOMODIMERIZATION, AND GLYCOSYLATION AT ASN-139; ASN-192 AND ASN-215.
RX PubMed=15003450; DOI=10.1016/j.jmb.2004.01.035;
RA Garman S.C., Garboczi D.N.;
RT "The molecular defect leading to Fabry disease: structure of human alpha-
RT galactosidase.";
RL J. Mol. Biol. 337:319-335(2004).
RN [15]
RP REVIEW ON FD VARIANTS.
RX PubMed=7911050; DOI=10.1002/humu.1380030204;
RA Eng C.M., Desnick R.J.;
RT "Molecular basis of Fabry disease: mutations and polymorphisms in the human
RT alpha-galactosidase A gene.";
RL Hum. Mutat. 3:103-111(1994).
RN [16]
RP INVOLVEMENT IN FD, AND VARIANT FD SER-40.
RX PubMed=2152885; DOI=10.1016/0014-5793(90)80046-l;
RA Koide T., Ishiura M., Iwai K., Inoue M., Kaneda Y., Okada Y., Uchida T.;
RT "A case of Fabry's disease in a patient with no alpha-galactosidase A
RT activity caused by a single amino acid substitution of Pro-40 by Ser.";
RL FEBS Lett. 259:353-356(1990).
RN [17]
RP VARIANT FD VAL-296.
RX PubMed=1846223; DOI=10.1056/nejm199102073240607;
RA von Scheidt W., Eng C.M., Fitzmaurice T.F., Erdmann E., Hubner G.,
RA Olsen E.G.J., Christomanou H., Kandolf R., Bishop D.F., Desnick R.J.;
RT "An atypical variant of Fabry's disease with manifestations confined to the
RT myocardium.";
RL N. Engl. J. Med. 324:395-399(1991).
RN [18]
RP VARIANT FD GLN-301.
RX PubMed=2171331;
RA Sakuraba H., Oshima A., Fukuhara Y., Shimmoto M., Nagao Y., Bishop D.F.,
RA Desnick R.J., Suzuki Y.;
RT "Identification of point mutations in the alpha-galactosidase A gene in
RT classical and atypical hemizygotes with Fabry disease.";
RL Am. J. Hum. Genet. 47:784-789(1990).
RN [19]
RP VARIANT FD TRP-356.
RX PubMed=2539398; DOI=10.1172/jci114027;
RA Bernstein H.S., Bishop D.F., Astrin K.H., Kornreich R., Eng C.M.,
RA Sakuraba H., Desnick R.J.;
RT "Fabry disease: six gene rearrangements and an exonic point mutation in the
RT alpha-galactosidase gene.";
RL J. Clin. Invest. 83:1390-1399(1989).
RN [20]
RP VARIANTS FD GLN-66; CYS-112; GLU-279; GLN-301 AND ARG-328.
RX PubMed=1315715; DOI=10.1007/bf00207037;
RA Ishii S., Sakuraba H., Suzuki Y.;
RT "Point mutations in the upstream region of the alpha-galactosidase A gene
RT exon 6 in an atypical variant of Fabry disease.";
RL Hum. Genet. 89:29-32(1992).
RN [21]
RP VARIANTS FD SER-34; GLY-56; ARG-162; GLN-227; VAL-264; VAL-266; PHE-297;
RP TYR-313; ALA-328 AND ARG-404 DEL.
RX PubMed=7504405;
RA Eng C.M., Resnick-Silverman L.A., Niehaus D.J., Astrin K.H., Desnick R.J.;
RT "Nature and frequency of mutations in the alpha-galactosidase A gene that
RT cause Fabry disease.";
RL Am. J. Hum. Genet. 53:1186-1197(1993).
RN [22]
RP VARIANTS FD SER-34; SER-215; ALA-269; LYS-327 AND ARG-361.
RX PubMed=8395937; DOI=10.1093/hmg/2.7.1051;
RA Davies J.P., Winchester B.G., Malcolm S.;
RT "Mutation analysis in patients with the typical form of Anderson-Fabry
RT disease.";
RL Hum. Mol. Genet. 2:1051-1053(1993).
RN [23]
RP VARIANTS FD ARG-35; LEU-49; VAL-165 AND GLU-316.
RX PubMed=8069316; DOI=10.1093/hmg/3.4.667;
RA Davies J.P., Christomanou H., Winchester B.G., Malcolm S.;
RT "Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry
RT disease.";
RL Hum. Mol. Genet. 3:667-669(1994).
RN [24]
RP VARIANTS FD.
RX PubMed=7531540; DOI=10.1093/hmg/3.10.1795;
RA Eng C.M., Niehaus D.J., Enriquez A.L., Burgert T.S., Ludman M.D.,
RA Desnick R.J.;
RT "Fabry disease: twenty-three mutations including sense and antisense CpG
RT alterations and identification of a deletional hot-spot in the alpha-
RT galactosidase A gene.";
RL Hum. Mol. Genet. 3:1795-1799(1994).
RN [25]
RP VARIANTS FD GLN-66; CYS-112; VAL-156; VAL-166; ALA-260; GLU-279; ILE-296;
RP GLN-301; LYS-320; ARG-328 AND SER-373.
RX PubMed=7575533; DOI=10.1006/bbrc.1995.2416;
RA Okumiya T., Ishii S., Takenaka T., Kase R., Kamei S., Sakuraba H.,
RA Suzuki Y.;
RT "Galactose stabilizes various missense mutants of alpha-galactosidase in
RT Fabry disease.";
RL Biochem. Biophys. Res. Commun. 214:1219-1224(1995).
RN [26]
RP VARIANTS FD TYR-142; VAL-156 AND VAL-166.
RX PubMed=7759078; DOI=10.1007/bf00223869;
RA Okumiya T., Ishii S., Kase R., Kamei S., Sakuraba H., Suzuki Y.;
RT "Alpha-galactosidase gene mutations in Fabry disease: heterogeneous
RT expressions of mutant enzyme proteins.";
RL Hum. Genet. 95:557-561(1995).
RN [27]
RP VARIANTS FD PRO-32; SER-34; ASP-85; THR-156 AND GLN-301.
RX PubMed=7599642; DOI=10.1002/humu.1380050316;
RA Madsen K.M., Hasholt L., Soerensen S.A., Lagerstroem Fermer M., Dahl N.;
RT "Two novel mutations (L32P) and (G85N) among five different missense
RT mutations in six Danish families with Fabry's disease.";
RL Hum. Mutat. 5:277-278(1995).
RN [28]
RP VARIANTS FD PRO-20 AND ILE-296.
RX PubMed=7596372; DOI=10.1056/nejm199508033330504;
RA Nakao S., Takenaka T., Maeda M., Kodama C., Tanaka A., Tahara M.,
RA Yoshida A., Kuriyama M., Hayashibe H., Sakuraba H., Tanaka H.;
RT "An atypical variant of Fabry's disease in men with left ventricular
RT hypertrophy.";
RL N. Engl. J. Med. 333:288-293(1995).
RN [29]
RP VARIANT FD GLN-301.
RX PubMed=8738659;
RA Sawada K., Mizoguchi K., Hishida A., Kaneko E., Koide Y., Nishimura K.,
RA Kimura M.;
RT "Point mutation in the alpha-galactosidase A gene of atypical Fabry disease
RT with only nephropathy.";
RL Clin. Nephrol. 45:289-294(1996).
RN [30]
RP VARIANTS FD VAL-42; SER-49; TYR-56; HIS-92; GLY-93; THR-205; CYS-236;
RP GLY-287; HIS-298 AND ARG-340.
RX PubMed=8875188; DOI=10.1159/000472202;
RA Davies J.P., Eng C.M., Hill J.A., Malcolm S., MacDermot K.,
RA Winchester B.G., Desnick R.J.;
RT "Fabry disease: fourteen alpha-galactosidase A mutations in unrelated
RT families from the United Kingdom and other European countries.";
RL Eur. J. Hum. Genet. 4:219-224(1996).
RN [31]
RP VARIANT FD PHE-383 DEL.
RX PubMed=8834244; DOI=10.1007/bf02267068;
RA Cariolou M.A., Christodoulides M., Manoli P., Kokkofitou A., Tsambaos D.;
RT "Novel trinucleotide deletion in Fabry's disease.";
RL Hum. Genet. 97:468-470(1996).
RN [32]
RP VARIANTS FD ARG-52; CYS-162; ARG-265 AND 316-VAL--ASP-322 DEL.
RX PubMed=8931708; DOI=10.1007/s004390050292;
RA Germain D.P., Biasotto M., Tosi M., Meo T., Kahn A., Poenaru L.;
RT "Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of
RT the alpha-galactosidase A gene and detection of carriers in Fabry
RT disease.";
RL Hum. Genet. 98:719-726(1996).
RN [33]
RP VARIANTS FD ARG-52; GLU-128; THR-205; THR-284; LYS-298 AND GLU-358 DEL.
RX PubMed=8807334;
RX DOI=10.1002/(sici)1098-1004(1996)8:1<38::aid-humu5>3.0.co;2-l;
RA Blanch L.C., Meaney C., Morris C.P.;
RT "A sensitive mutation screening strategy for Fabry disease: detection of
RT nine mutations in the alpha-galactosidase A gene.";
RL Hum. Mutat. 8:38-43(1996).
RN [34]
RP VARIANT FD ASN-231.
RX PubMed=8863162; DOI=10.1136/jmg.33.8.682;
RA Redonnet-Vernhet I., Ploos van Amstel J.K., Jansen R.P.M., Wevers R.A.,
RA Salvayre R., Levade T.;
RT "Uneven X inactivation in a female monozygotic twin pair with Fabry disease
RT and discordant expression of a novel mutation in the alpha-galactosidase A
RT gene.";
RL J. Med. Genet. 33:682-688(1996).
RN [35]
RP VARIANTS FD PRO-20; SER-40; GLN-66; VAL-72; CYS-112; TYR-142; VAL-156;
RP VAL-166; ASN-242; ALA-260; ASP-261; GLU-279; ILE-296; GLN-301; LYS-320;
RP ARG-328; GLU-358 DEL AND SER-373.
RX PubMed=9105656; DOI=10.1016/s0387-7604(96)00486-x;
RA Takata T., Okumiya T., Hayashibe H., Shimmoto M., Kase R., Itoh K.,
RA Utsumi K., Kamei S., Sakuraba H.;
RT "Screening and detection of gene mutations in Japanese patients with Fabry
RT disease by non-radioactive single-stranded conformation polymorphism
RT analysis.";
RL Brain Dev. 19:111-116(1997).
RN [36]
RP VARIANTS FD VAL-31; 45-ARG-SER-46; ARG-46; CYS-86; PRO-89; THR-91; TYR-92;
RP TYR-94; VAL-97; THR-100; LEU-113; SER-134; ARG-138; THR-143; ARG-148;
RP VAL-163; VAL-170; TYR-202; 205-PRO--TYR-207 DEL; ASP-216; SER-263; CYS-287;
RP SER-298 AND ARG-404 DEL.
RX PubMed=9100224; DOI=10.1007/bf03401671;
RA Eng C.M., Ashley G.A., Burgert T.S., Enriquez A.L., D'Souza M.,
RA Desnick R.J.;
RT "Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in
RT patients with classic and variant phenotypes.";
RL Mol. Med. 3:174-182(1997).
RN [37]
RP VARIANT FD THR-65.
RX PubMed=9554750;
RX DOI=10.1002/(sici)1098-1004(1998)11:4<328::aid-humu11>3.0.co;2-n;
RA Chen C.-H., Shyu P.-W., Wu S.-J., Sheu S.-S., Desnick R.J., Hsiao K.-J.;
RT "Identification of a novel point mutation (S65T) in alpha-galactosidase A
RT gene in Chinese patients with Fabry disease.";
RL Hum. Mutat. 11:328-330(1998).
RN [38]
RP VARIANT FD LYS-358.
RX PubMed=9452068; DOI=10.1002/humu.1380110147;
RA Miyazaki T., Kajita M., Ohmori S., Mizutani N., Niwa T., Murata Y., Seo H.;
RT "A novel mutation (E358K) in the alpha-galactosidase A gene detected in a
RT Japanese family with Fabry disease.";
RL Hum. Mutat. Suppl. 1:S139-S140(1998).
RN [39]
RP VARIANT FD VAL-72.
RX PubMed=9452090; DOI=10.1002/humu.1380110169;
RA Okumiya T., Kawamura O., Itoh K., Kase R., Ishii S., Kamei S., Sakuraba H.;
RT "Novel missense mutation (M72V) of alpha-galactosidase gene and its
RT expression product in an atypical Fabry hemizygote.";
RL Hum. Mutat. Suppl. 1:S213-S216(1998).
RN [40]
RP VARIANTS FD SER-40; SER-215; ASP-224; TYR-313 AND TRP-THR-SER-247 INS.
RX PubMed=9452111; DOI=10.1002/humu.1380110190;
RA Guffon N., Froissart R., Chevalier-Porst F., Maire I.;
RT "Mutation analysis in 11 French patients with Fabry disease.";
RL Hum. Mutat. Suppl. 1:S288-S290(1998).
RN [41]
RP VARIANTS FD TRP-202; GLY-223; ASP-224; GLN-301 AND LYS-327.
RX PubMed=10208848; DOI=10.1006/bbrc.1999.0310;
RA Germain D.P., Poenaru L.;
RT "Fabry disease: identification of novel alpha-galactosidase A mutations and
RT molecular carrier detection by use of fluorescent chemical cleavage of
RT mismatches.";
RL Biochem. Biophys. Res. Commun. 257:708-713(1999).
RN [42]
RP VARIANT FD LYS-341.
RX PubMed=10090526; DOI=10.1016/s0009-8981(98)00133-8;
RA Beyer E.M., Karpova E.A., Udalova O.V., Ploos van Amstel J.K.,
RA van Diggelen O.P., Tsvetkova I.V.;
RT "The multiple cases of Fabry disease in a Russian family caused by an E341K
RT amino acid substitution in the alpha-galactosidase A.";
RL Clin. Chim. Acta 280:81-89(1999).
RN [43]
RP CHARACTERIZATION OF VARIANTS FD GLU-279 AND GLN-301, FUNCTION, CATALYTIC
RP ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=10838196; DOI=10.1016/s0925-4439(00)00024-7;
RA Kase R., Bierfreund U., Klein A., Kolter T., Utsumi K., Itoh K.,
RA Sandhoff K., Sakuraba H.;
RT "Characterization of two alpha-galactosidase mutants (Q279E and R301Q)
RT found in an atypical variant of Fabry disease.";
RL Biochim. Biophys. Acta 1501:227-235(2000).
RN [44]
RP VARIANTS FD VAL-42; CYS-112; ARG-142; ARG-148; VAL-165; ASP-183; SER-215;
RP CYS-235; LEU-236; HIS-244; LEU-259; ILE-267; PHE-289; GLU-321; GLU-358 DEL
RP AND TYR-378.
RX PubMed=10666480; DOI=10.1007/bf03401993;
RA Topaloglu A.K., Ashley G.A., Tong B., Shabbeer J., Astrin K.H., Eng C.M.,
RA Desnick R.J.;
RT "Twenty novel mutations in the alpha-galactosidase A gene causing Fabry
RT disease.";
RL Mol. Med. 5:806-811(1999).
RN [45]
RP VARIANT FD ASN-266.
RX PubMed=11076046; DOI=10.1034/j.1399-0004.2000.580311.x;
RA Lee J.-K., Kim G.-H., Kim J.-S., Kim K.-K., Lee M.-C., Yoo H.-W.;
RT "Identification of four novel mutations in five unrelated Korean families
RT with Fabry disease.";
RL Clin. Genet. 58:228-233(2000).
RN [46]
RP VARIANTS FD LEU-40; SER-95; CYS-112; HIS-112; ASN-148; ARG-172; VAL-187;
RP SER-224; ARG-226; GLN-227; THR-230; HIS-266; GLN-301 AND TYR-320.
RX PubMed=10916280;
RA Ashton-Prolla P., Tong B., Shabbeer J., Astrin K.H., Eng C.M.,
RA Desnick R.J.;
RT "Fabry disease: twenty-two novel mutations in the alpha-galactosidase A
RT gene and genotype/phenotype correlations in severely and mildly affected
RT hemizygotes and heterozygotes.";
RL J. Invest. Med. 48:227-235(2000).
RN [47]
RP VARIANT FD ASP-373.
RX PubMed=11295840; DOI=10.1002/humu.41;
RA Germain D.P., Salard D., Fellmann F., Azibi K., Caillaud C., Bernard M.-C.,
RA Poenaru L.;
RT "Identification of a novel de novo mutation (G373D) in the alpha-
RT galactosidase A gene (GLA) in a patient affected with Fabry disease.";
RL Hum. Mutat. 17:353-353(2001).
RN [48]
RP VARIANTS FD TYR-46; GLY-47; PRO-49; SER-94; SER-95; CYS-112; SER-113;
RP THR-143; SER-215; ARG-258; ARG-259; ILE-267; HIS-279; HIS-280; HIS-298;
RP TYR-313; HIS-363; ASP-377; ALA-409 AND THR-409.
RX PubMed=11668641; DOI=10.1002/humu.1219;
RA Blaydon D., Hill J.A., Winchester B.G.;
RT "Fabry disease: 20 novel GLA mutations in 35 families.";
RL Hum. Mutat. 18:459-459(2001).
RN [49]
RP VARIANT FD PRO-143.
RX PubMed=11889412; DOI=10.1097/00005792-200203000-00003;
RA Branton M.H., Schiffmann R., Sabnis S.G., Murray G.J., Quirk J.M.,
RA Altarescu G., Goldfarb L., Brady R.O., Balow J.E., Austin H.A. III,
RA Kopp J.B.;
RT "Natural history of Fabry renal disease: influence of alpha-galactosidase A
RT activity and genetic mutations on clinical course.";
RL Medicine (Baltimore) 81:122-138(2002).
RN [50]
RP VARIANT FD ALA-410.
RX PubMed=12694230; DOI=10.1034/j.1399-0004.2003.00050.x;
RA Yang C.-C., Lai L.-W., Whitehair O., Hwu W.-L., Chiang S.-C., Lien Y.-H.H.;
RT "Two novel mutations in the alpha-galactosidase A gene in Chinese patients
RT with Fabry disease.";
RL Clin. Genet. 63:205-209(2003).
RN [51]
RP CHARACTERIZATION OF VARIANT FD THR-65.
RX PubMed=12786754; DOI=10.1034/j.1399-0004.2003.00077.x;
RA Lai L.-W., Whitehair O., Wu M.-J., O'Meara M., Lien Y.-H.H.;
RT "Analysis of splice-site mutations of the alpha-galactosidase A gene in
RT Fabry disease.";
RL Clin. Genet. 63:476-482(2003).
RN [52]
RP VARIANT FD SER-272.
RX PubMed=15162124; DOI=10.1038/sj.ejhg.5201184;
RA Verovnik F., Benko D., Vujkovac B., Linthorst G.E.;
RT "Remarkable variability in renal disease in a large Slovenian family with
RT Fabry disease.";
RL Eur. J. Hum. Genet. 12:678-681(2004).
RN [53]
RP VARIANTS FD VAL-31; LEU-42; ARG-43; ASN-93; CYS-112; HIS-112; SER-112;
RP SER-134; VAL-135; ASP-171; PHE-201; SER-215; GLU-234; ASP-261; TYR-264;
RP VAL-264; GLY-276; PRO-285; PHE-300; ALA-328; VAL-328; LYS-338; ALA-358;
RP GLU-358 DEL; ARG-404 DEL AND SER-414.
RX PubMed=15712228; DOI=10.1002/humu.20144;
RA Shabbeer J., Robinson M., Desnick R.J.;
RT "Detection of alpha-galactosidase a mutations causing Fabry disease by
RT denaturing high performance liquid chromatography.";
RL Hum. Mutat. 25:299-305(2005).
RN [54]
RP VARIANT FD THR-143.
RX PubMed=16533976; DOI=10.1001/archneur.63.3.453;
RA Nance C.S., Klein C.J., Banikazemi M., Dikman S.H., Phelps R.G.,
RA McArthur J.C., Rodriguez M., Desnick R.J.;
RT "Later-onset Fabry disease: an adult variant presenting with the cramp-
RT fasciculation syndrome.";
RL Arch. Neurol. 63:453-457(2006).
RN [55]
RP VARIANTS FD 12-CYS--LEU-14 DEL; PRO-46; GLN-66; ASN-93; VAL-120; THR-219;
RP GLN-356 AND CYS-360, AND CHARACTERIZATION OF VARIANTS FD 12-CYS--LEU-14
RP DEL; PRO-46; GLN-66; ASN-93; VAL-120; THR-219; GLN-356 AND CYS-360.
RX PubMed=19621417; DOI=10.1002/humu.21074;
RA Hwu W.L., Chien Y.H., Lee N.C., Chiang S.C., Dobrovolny R., Huang A.C.,
RA Yeh H.Y., Chao M.C., Lin S.J., Kitagawa T., Desnick R.J., Hsu L.W.;
RT "Newborn screening for Fabry disease in Taiwan reveals a high incidence of
RT the later-onset GLA mutation c.936+919G>A (IVS4+919G>A).";
RL Hum. Mutat. 30:1397-1405(2009).
RN [56]
RP CHARACTERIZATION OF VARIANTS FD ASP-20; PRO-20; PRO-21; GLY-33; GLU-35;
RP TRP-36; SER-40; THR-42; PRO-45; ASP-48; TYR-56; LEU-60; PHE-64; ASP-80;
RP HIS-86; ASN-91; THR-91; SER-94; TYR-94; ILE-113; THR-121; LEU-164; GLY-164;
RP GLN-167; PHE-180; VAL-187; SER-196; THR-198; TYR-202; ARG-204; ARG-213;
RP LEU-214; MET-219; PRO-227; SER-228; VAL-242; PHE-243; PRO-247; LYS-249;
RP THR-253; ALA-254; ARG-259; ARG-262; GLY-269; GLY-276; VAL-309; ASN-315;
RP ALA-316; SER-317; TYR-320; ARG-323; ARG-327; LEU-327; ARG-328; ARG-330;
RP PRO-342; GLY-352; PRO-356; LYS-358; SER-360; ALA-375; SER-392; SER-399 AND
RP ARG-404 DEL, CHARACTERIZATION OF VARIANTS PRO-3; VAL-3; GLY-71; THR-154;
RP VAL-289 AND ASN-313, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=26415523; DOI=10.1002/humu.22910;
RA Lukas J., Scalia S., Eichler S., Pockrandt A.M., Dehn N., Cozma C.,
RA Giese A.K., Rolfs A.;
RT "Functional and clinical consequences of novel alpha-galactosidase A
RT mutations in Fabry disease.";
RL Hum. Mutat. 37:43-51(2016).
RN [57]
RP VARIANT FD ARG-47, CHARACTERIZATION OF VARIANTS FD ARG-47 AND GLY-47,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=27211852; DOI=10.1080/00207454.2016.1191483;
RA Ge W., Wei B., Zhu H., Miao Z., Zhang W., Leng C., Li J., Zhang D., Sun M.,
RA Xu X.;
RT "A novel mutation of alpha-galactosidase A gene causes Fabry disease
RT mimicking primary erythromelalgia in a Chinese family.";
RL Int. J. Neurosci. 2016:1-6(2016).
RN [58]
RP VARIANT FD THR-143.
RX PubMed=27142856; DOI=10.1186/s13023-016-0441-z;
RA Lenders M., Weidemann F., Kurschat C., Canaan-Kuehl S., Duning T.,
RA Stypmann J., Schmitz B., Reiermann S., Kraemer J., Blaschke D., Wanner C.,
RA Brand S.M., Brand E.;
RT "Alpha-Galactosidase A p.A143T, a non-Fabry disease-causing variant.";
RL Orphanet J. Rare Dis. 11:54-54(2016).
CC -!- FUNCTION: Catalyzes the hydrolysis of glycosphingolipids and
CC participates in their degradation in the lysosome.
CC {ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:8804427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC Evidence={ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:27211852};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside Gb3Cer (d18:1(4E)) + H2O = a beta-D-Gal-(1->4)-beta-
CC D-Glc-(1<->1)-Cer(d18:1(4E)) + D-galactose; Xref=Rhea:RHEA:21112,
CC ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:17950,
CC ChEBI:CHEBI:18313; Evidence={ECO:0000269|PubMed:10838196,
CC ECO:0000269|PubMed:8804427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21113;
CC Evidence={ECO:0000305|PubMed:10838196, ECO:0000305|PubMed:8804427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside Gb3Cer + H2O = beta-D-galactosyl-(1->4)-beta-D-
CC glucosyl-(1<->1)-ceramide + D-galactose; Xref=Rhea:RHEA:48020,
CC ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:79208,
CC ChEBI:CHEBI:88154; Evidence={ECO:0000269|PubMed:10838196,
CC ECO:0000269|PubMed:8804427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48021;
CC Evidence={ECO:0000305|PubMed:10838196, ECO:0000305|PubMed:8804427};
CC -!- ACTIVITY REGULATION: Galactosylgalactosylglucosylceramidase activity is
CC stimulated by saposin B and ammonium chloride.
CC {ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:8804427}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15003450}.
CC -!- INTERACTION:
CC P06280; Q99523: SORT1; NbExp=3; IntAct=EBI-2513305, EBI-1057058;
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- RNA EDITING: Modified_positions=396 {ECO:0000269|PubMed:7503918};
CC Note=Partially edited.;
CC -!- DISEASE: Fabry disease (FD) [MIM:301500]: Rare X-linked
CC sphingolipidosis disease where glycolipid accumulates in many tissues.
CC The disease consists of an inborn error of glycosphingolipid
CC catabolism. FD patients show systemic accumulation of
CC globotriaosylceramide (Gb3) and related glycosphingolipids in the
CC plasma and cellular lysosomes throughout the body. Clinical recognition
CC in males results from characteristic skin lesions (angiokeratomas) over
CC the lower trunk. Patients may show ocular deposits, febrile episodes,
CC and burning pain in the extremities. Death results from renal failure,
CC cardiac or cerebral complications of hypertension or other vascular
CC disease. Heterozygous females may exhibit the disorder in an attenuated
CC form, they are more likely to show corneal opacities.
CC {ECO:0000269|PubMed:10090526, ECO:0000269|PubMed:10208848,
CC ECO:0000269|PubMed:10666480, ECO:0000269|PubMed:10838196,
CC ECO:0000269|PubMed:10916280, ECO:0000269|PubMed:11076046,
CC ECO:0000269|PubMed:11295840, ECO:0000269|PubMed:11668641,
CC ECO:0000269|PubMed:11889412, ECO:0000269|PubMed:12694230,
CC ECO:0000269|PubMed:12786754, ECO:0000269|PubMed:1315715,
CC ECO:0000269|PubMed:15162124, ECO:0000269|PubMed:15712228,
CC ECO:0000269|PubMed:16533976, ECO:0000269|PubMed:1846223,
CC ECO:0000269|PubMed:19621417, ECO:0000269|PubMed:2152885,
CC ECO:0000269|PubMed:2171331, ECO:0000269|PubMed:2539398,
CC ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:27142856,
CC ECO:0000269|PubMed:27211852, ECO:0000269|PubMed:7504405,
CC ECO:0000269|PubMed:7531540, ECO:0000269|PubMed:7575533,
CC ECO:0000269|PubMed:7596372, ECO:0000269|PubMed:7599642,
CC ECO:0000269|PubMed:7759078, ECO:0000269|PubMed:8069316,
CC ECO:0000269|PubMed:8395937, ECO:0000269|PubMed:8738659,
CC ECO:0000269|PubMed:8807334, ECO:0000269|PubMed:8834244,
CC ECO:0000269|PubMed:8863162, ECO:0000269|PubMed:8875188,
CC ECO:0000269|PubMed:8931708, ECO:0000269|PubMed:9100224,
CC ECO:0000269|PubMed:9105656, ECO:0000269|PubMed:9452068,
CC ECO:0000269|PubMed:9452090, ECO:0000269|PubMed:9452111,
CC ECO:0000269|PubMed:9554750}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- PHARMACEUTICAL: Available under the names Replagal (from Shire) and
CC Fabrazyme (from Genzyme). Used as a long-term enzyme replacement
CC therapy in patients with a confirmed diagnosis of Fabry disease. The
CC differences between Replagal (also known as agalsidase alpha) and
CC Fabrazyme (also known as agalsidase beta) lies in the glycosylation
CC patterns. Agalsidase beta is produced in the hamster CHO cell line
CC while agalsidase alpha is produced in human cell lines.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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DR EMBL; X05790; CAA29232.1; -; mRNA.
DR EMBL; X14448; CAA32617.1; -; Genomic_DNA.
DR EMBL; U78027; AAB64203.1; -; Genomic_DNA.
DR EMBL; AL035422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002689; AAH02689.1; -; mRNA.
DR EMBL; M13571; AAA51676.1; -; Genomic_DNA.
DR EMBL; D00039; BAA34059.1; -; mRNA.
DR EMBL; M18242; AAA52514.1; -; Genomic_DNA.
DR EMBL; X16889; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M20317; AAA52559.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS14484.1; -.
DR PIR; S04081; GBHUA.
DR RefSeq; NP_000160.1; NM_000169.2.
DR PDB; 1R46; X-ray; 3.25 A; A/B=32-429.
DR PDB; 1R47; X-ray; 3.45 A; A/B=32-429.
DR PDB; 3GXN; X-ray; 3.01 A; A/B=32-429.
DR PDB; 3GXP; X-ray; 2.20 A; A/B=32-429.
DR PDB; 3GXT; X-ray; 2.70 A; A/B=32-429.
DR PDB; 3HG2; X-ray; 2.30 A; A/B=32-429.
DR PDB; 3HG3; X-ray; 1.90 A; A/B=32-429.
DR PDB; 3HG4; X-ray; 2.30 A; A/B=32-429.
DR PDB; 3HG5; X-ray; 2.30 A; A/B=32-429.
DR PDB; 3LX9; X-ray; 2.04 A; A/B=32-429.
DR PDB; 3LXA; X-ray; 3.04 A; A/B=32-429.
DR PDB; 3LXB; X-ray; 2.85 A; A/B=32-429.
DR PDB; 3LXC; X-ray; 2.35 A; A/B=32-429.
DR PDB; 3S5Y; X-ray; 2.10 A; A/B=32-429.
DR PDB; 3S5Z; X-ray; 2.00 A; A/B=32-429.
DR PDB; 3TV8; X-ray; 2.64 A; A/B=32-429.
DR PDB; 4NXS; X-ray; 2.55 A; A/B=32-429.
DR PDB; 6IBK; X-ray; 1.99 A; A/B=32-429.
DR PDB; 6IBM; X-ray; 2.07 A; A/B=32-429.
DR PDB; 6IBR; X-ray; 2.02 A; A/B=32-429.
DR PDB; 6IBT; X-ray; 2.04 A; A/B=32-429.
DR PDBsum; 1R46; -.
DR PDBsum; 1R47; -.
DR PDBsum; 3GXN; -.
DR PDBsum; 3GXP; -.
DR PDBsum; 3GXT; -.
DR PDBsum; 3HG2; -.
DR PDBsum; 3HG3; -.
DR PDBsum; 3HG4; -.
DR PDBsum; 3HG5; -.
DR PDBsum; 3LX9; -.
DR PDBsum; 3LXA; -.
DR PDBsum; 3LXB; -.
DR PDBsum; 3LXC; -.
DR PDBsum; 3S5Y; -.
DR PDBsum; 3S5Z; -.
DR PDBsum; 3TV8; -.
DR PDBsum; 4NXS; -.
DR PDBsum; 6IBK; -.
DR PDBsum; 6IBM; -.
DR PDBsum; 6IBR; -.
DR PDBsum; 6IBT; -.
DR AlphaFoldDB; P06280; -.
DR SMR; P06280; -.
DR BioGRID; 108981; 47.
DR IntAct; P06280; 15.
DR STRING; 9606.ENSP00000218516; -.
DR BindingDB; P06280; -.
DR ChEMBL; CHEMBL2524; -.
DR DrugBank; DB05018; Migalastat.
DR DrugCentral; P06280; -.
DR SwissLipids; SLP:000001380; -.
DR Allergome; 9621; Hom s alpha-Galactosidase.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR GlyConnect; 1005; 19 N-Linked glycans (3 sites).
DR GlyGen; P06280; 3 sites, 18 N-linked glycans (3 sites).
DR iPTMnet; P06280; -.
DR PhosphoSitePlus; P06280; -.
DR BioMuta; GLA; -.
DR EPD; P06280; -.
DR jPOST; P06280; -.
DR MassIVE; P06280; -.
DR PaxDb; P06280; -.
DR PeptideAtlas; P06280; -.
DR PRIDE; P06280; -.
DR ProteomicsDB; 51881; -.
DR Antibodypedia; 377; 439 antibodies from 34 providers.
DR DNASU; 2717; -.
DR Ensembl; ENST00000218516.4; ENSP00000218516.4; ENSG00000102393.14.
DR GeneID; 2717; -.
DR KEGG; hsa:2717; -.
DR MANE-Select; ENST00000218516.4; ENSP00000218516.4; NM_000169.3; NP_000160.1.
DR CTD; 2717; -.
DR DisGeNET; 2717; -.
DR GeneCards; GLA; -.
DR GeneReviews; GLA; -.
DR HGNC; HGNC:4296; GLA.
DR HPA; ENSG00000102393; Low tissue specificity.
DR MalaCards; GLA; -.
DR MIM; 300644; gene.
DR MIM; 301500; phenotype.
DR neXtProt; NX_P06280; -.
DR OpenTargets; ENSG00000102393; -.
DR Orphanet; 324; Fabry disease.
DR PharmGKB; PA28707; -.
DR VEuPathDB; HostDB:ENSG00000102393; -.
DR eggNOG; KOG2366; Eukaryota.
DR GeneTree; ENSGT00390000008751; -.
DR HOGENOM; CLU_013093_0_0_1; -.
DR InParanoid; P06280; -.
DR OMA; AMTPTMG; -.
DR OrthoDB; 31524at2759; -.
DR PhylomeDB; P06280; -.
DR TreeFam; TF312909; -.
DR BioCyc; MetaCyc:HS02389-MON; -.
DR BRENDA; 3.2.1.22; 2681.
DR PathwayCommons; P06280; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SABIO-RK; P06280; -.
DR SignaLink; P06280; -.
DR SIGNOR; P06280; -.
DR BioGRID-ORCS; 2717; 7 hits in 708 CRISPR screens.
DR ChiTaRS; GLA; human.
DR EvolutionaryTrace; P06280; -.
DR GeneWiki; Alpha-galactosidase; -.
DR GenomeRNAi; 2717; -.
DR Pharos; P06280; Tclin.
DR PRO; PR:P06280; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P06280; protein.
DR Bgee; ENSG00000102393; Expressed in pancreatic ductal cell and 175 other tissues.
DR ExpressionAtlas; P06280; baseline and differential.
DR Genevisible; P06280; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IMP:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IMP:UniProtKB.
DR GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0003824; F:catalytic activity; IDA:UniProtKB.
DR GO; GO:0016936; F:galactoside binding; IEA:Ensembl.
DR GO; GO:0017041; F:galactosylgalactosylglucosylceramidase activity; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; TAS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
DR GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR GO; GO:0046479; P:glycosphingolipid catabolic process; IDA:UniProtKB.
DR GO; GO:0046477; P:glycosylceramide catabolic process; ISS:UniProtKB.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISS:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:UniProtKB.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035373; Melibiase/NAGA_C.
DR PANTHER; PTHR11452; PTHR11452; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17450; Melibiase_2_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism; Lysosome;
KW Pharmaceutical; Reference proteome; RNA editing; Signal.
FT SIGNAL 1..31
FT CHAIN 32..429
FT /note="Alpha-galactosidase A"
FT /id="PRO_0000001004"
FT ACT_SITE 170
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 203..207
FT /ligand="substrate"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15003450"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15003450"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15003450,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 52..94
FT DISULFID 56..63
FT DISULFID 142..172
FT DISULFID 202..223
FT DISULFID 378..382
FT VARIANT 3
FT /note="L -> P (does not affect enzyme activity;
FT dbSNP:rs150547672)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077365"
FT VARIANT 3
FT /note="L -> V (does not affect enzyme activity;
FT dbSNP:rs869312133)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077366"
FT VARIANT 12..14
FT /note="Missing (in FD; has 4% of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:19621417"
FT /id="VAR_062550"
FT VARIANT 20
FT /note="A -> D (in FD; loss of enzyme activity;
FT dbSNP:rs869312134)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077367"
FT VARIANT 20
FT /note="A -> P (in FD; atypical; loss of enzyme activity;
FT dbSNP:rs104894847)"
FT /evidence="ECO:0000269|PubMed:26415523,
FT ECO:0000269|PubMed:7596372, ECO:0000269|PubMed:9105656"
FT /id="VAR_012362"
FT VARIANT 21
FT /note="L -> P (in FD; loss of enzyme activity;
FT dbSNP:rs869312135)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077368"
FT VARIANT 31
FT /note="A -> V (in FD; dbSNP:rs869312448)"
FT /evidence="ECO:0000269|PubMed:15712228,
FT ECO:0000269|PubMed:9100224"
FT /id="VAR_012363"
FT VARIANT 32
FT /note="L -> P (in FD; dbSNP:rs1569306168)"
FT /evidence="ECO:0000269|PubMed:7599642"
FT /id="VAR_000431"
FT VARIANT 33
FT /note="D -> G (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312136)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077369"
FT VARIANT 34
FT /note="N -> S (in FD; dbSNP:rs104894835)"
FT /evidence="ECO:0000269|PubMed:7504405,
FT ECO:0000269|PubMed:7599642, ECO:0000269|PubMed:8395937"
FT /id="VAR_000432"
FT VARIANT 35
FT /note="G -> E (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312137)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077370"
FT VARIANT 35
FT /note="G -> R (in FD)"
FT /evidence="ECO:0000269|PubMed:8069316"
FT /id="VAR_000433"
FT VARIANT 36
FT /note="L -> W (in FD; loss of enzyme activity;
FT dbSNP:rs869312138)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077371"
FT VARIANT 40
FT /note="P -> L (in FD; dbSNP:rs398123199)"
FT /evidence="ECO:0000269|PubMed:10916280"
FT /id="VAR_012364"
FT VARIANT 40
FT /note="P -> S (in FD; loss of enzyme activity;
FT dbSNP:rs104894831)"
FT /evidence="ECO:0000269|PubMed:2152885,
FT ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:9105656,
FT ECO:0000269|PubMed:9452111"
FT /id="VAR_000434"
FT VARIANT 42
FT /note="M -> L (in FD; dbSNP:rs797044613)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062551"
FT VARIANT 42
FT /note="M -> T (in FD; loss of enzyme activity;
FT dbSNP:rs398123201)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077372"
FT VARIANT 42
FT /note="M -> V (in FD; dbSNP:rs797044613)"
FT /evidence="ECO:0000269|PubMed:10666480,
FT ECO:0000269|PubMed:8875188"
FT /id="VAR_012365"
FT VARIANT 43
FT /note="G -> R (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062552"
FT VARIANT 45..46
FT /note="LH -> RS (in FD)"
FT /id="VAR_012366"
FT VARIANT 45
FT /note="L -> P (in FD; loss of enzyme activity)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077373"
FT VARIANT 46
FT /note="H -> P (in FD; has 36% of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:19621417"
FT /id="VAR_062553"
FT VARIANT 46
FT /note="H -> R (in FD; dbSNP:rs398123203)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012367"
FT VARIANT 46
FT /note="H -> Y (in FD)"
FT /evidence="ECO:0000269|PubMed:11668641"
FT /id="VAR_012368"
FT VARIANT 47
FT /note="W -> G (in FD; decreased alpha-galactosidase
FT activity)"
FT /evidence="ECO:0000269|PubMed:11668641,
FT ECO:0000269|PubMed:27211852"
FT /id="VAR_012369"
FT VARIANT 47
FT /note="W -> R (in FD; decreased alpha-galactosidase
FT activity)"
FT /evidence="ECO:0000269|PubMed:27211852"
FT /id="VAR_076478"
FT VARIANT 48
FT /note="E -> D (in FD; loss of enzyme activity;
FT dbSNP:rs869312254)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077374"
FT VARIANT 49
FT /note="R -> L (in FD)"
FT /evidence="ECO:0000269|PubMed:8069316"
FT /id="VAR_000435"
FT VARIANT 49
FT /note="R -> P (in FD; dbSNP:rs398123205)"
FT /evidence="ECO:0000269|PubMed:11668641"
FT /id="VAR_012370"
FT VARIANT 49
FT /note="R -> S (in FD)"
FT /evidence="ECO:0000269|PubMed:8875188"
FT /id="VAR_012371"
FT VARIANT 52
FT /note="C -> R (in FD; dbSNP:rs1057521047)"
FT /evidence="ECO:0000269|PubMed:8807334,
FT ECO:0000269|PubMed:8931708"
FT /id="VAR_000436"
FT VARIANT 52
FT /note="C -> S (in FD; dbSNP:rs869312256)"
FT /id="VAR_000437"
FT VARIANT 56
FT /note="C -> F (in FD; dbSNP:rs869312258)"
FT /id="VAR_000438"
FT VARIANT 56
FT /note="C -> G (in FD; dbSNP:rs104894836)"
FT /evidence="ECO:0000269|PubMed:7504405"
FT /id="VAR_000439"
FT VARIANT 56
FT /note="C -> Y (in FD; loss of enzyme activity;
FT dbSNP:rs869312258)"
FT /evidence="ECO:0000269|PubMed:26415523,
FT ECO:0000269|PubMed:8875188"
FT /id="VAR_012372"
FT VARIANT 59
FT /note="E -> K (in FD)"
FT /id="VAR_000440"
FT VARIANT 60
FT /note="P -> L (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312262)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077375"
FT VARIANT 64
FT /note="I -> F (in FD; loss of enzyme activity;
FT dbSNP:rs869312139)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077376"
FT VARIANT 65
FT /note="S -> T (in FD; does not affect enzyme function;
FT dbSNP:rs104894848)"
FT /evidence="ECO:0000269|PubMed:12786754,
FT ECO:0000269|PubMed:9554750"
FT /id="VAR_032290"
FT VARIANT 66
FT /note="E -> Q (in FD; has 52% of wild-type activity;
FT dbSNP:rs104894833)"
FT /evidence="ECO:0000269|PubMed:1315715,
FT ECO:0000269|PubMed:19621417, ECO:0000269|PubMed:7575533,
FT ECO:0000269|PubMed:9105656"
FT /id="VAR_000441"
FT VARIANT 71
FT /note="E -> G (does not affect enzyme activity;
FT dbSNP:rs781927744)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077377"
FT VARIANT 72
FT /note="M -> V (in FD; atypical)"
FT /evidence="ECO:0000269|PubMed:9105656,
FT ECO:0000269|PubMed:9452090"
FT /id="VAR_000442"
FT VARIANT 80
FT /note="G -> D (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs781838005)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077378"
FT VARIANT 85
FT /note="G -> D (in FD; dbSNP:rs1569304898)"
FT /evidence="ECO:0000269|PubMed:7599642"
FT /id="VAR_000443"
FT VARIANT 86
FT /note="Y -> C (in FD)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012373"
FT VARIANT 86
FT /note="Y -> H (in FD; loss of enzyme activity;
FT dbSNP:rs869312140)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077379"
FT VARIANT 89
FT /note="L -> P (in FD)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012374"
FT VARIANT 89
FT /note="L -> R (in FD; dbSNP:rs1569304886)"
FT /id="VAR_000444"
FT VARIANT 91
FT /note="I -> N (in FD; loss of enzyme activity;
FT dbSNP:rs869312141)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077380"
FT VARIANT 91
FT /note="I -> T (in FD; mild; loss of enzyme activity;
FT dbSNP:rs869312141)"
FT /evidence="ECO:0000269|PubMed:26415523,
FT ECO:0000269|PubMed:9100224"
FT /id="VAR_012375"
FT VARIANT 92
FT /note="D -> H (in FD)"
FT /evidence="ECO:0000269|PubMed:8875188"
FT /id="VAR_012376"
FT VARIANT 92
FT /note="D -> Y (in FD; dbSNP:rs886041315)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012377"
FT VARIANT 93
FT /note="D -> G (in FD)"
FT /evidence="ECO:0000269|PubMed:8875188"
FT /id="VAR_012378"
FT VARIANT 93
FT /note="D -> N (in FD; has no enzyme activity;
FT dbSNP:rs869312270)"
FT /evidence="ECO:0000269|PubMed:15712228,
FT ECO:0000269|PubMed:19621417"
FT /id="VAR_062554"
FT VARIANT 94
FT /note="C -> S (in FD; loss of enzyme activity)"
FT /evidence="ECO:0000269|PubMed:11668641,
FT ECO:0000269|PubMed:26415523"
FT /id="VAR_012379"
FT VARIANT 94
FT /note="C -> Y (in FD; loss of enzyme activity;
FT dbSNP:rs113173389)"
FT /evidence="ECO:0000269|PubMed:26415523,
FT ECO:0000269|PubMed:9100224"
FT /id="VAR_012380"
FT VARIANT 95
FT /note="W -> S (in FD)"
FT /evidence="ECO:0000269|PubMed:10916280,
FT ECO:0000269|PubMed:11668641"
FT /id="VAR_012381"
FT VARIANT 97
FT /note="A -> V (in FD; dbSNP:rs1569304867)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012382"
FT VARIANT 100
FT /note="R -> K (in FD; dbSNP:rs869312273)"
FT /id="VAR_000445"
FT VARIANT 100
FT /note="R -> T (in FD)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012383"
FT VARIANT 112..117
FT /note="Missing (in FD)"
FT /id="VAR_000446"
FT VARIANT 112
FT /note="R -> C (in FD; dbSNP:rs104894834)"
FT /evidence="ECO:0000269|PubMed:10666480,
FT ECO:0000269|PubMed:10916280, ECO:0000269|PubMed:11668641,
FT ECO:0000269|PubMed:1315715, ECO:0000269|PubMed:15712228,
FT ECO:0000269|PubMed:7575533, ECO:0000269|PubMed:9105656"
FT /id="VAR_000447"
FT VARIANT 112
FT /note="R -> H (in FD; mild; dbSNP:rs372966991)"
FT /evidence="ECO:0000269|PubMed:10916280,
FT ECO:0000269|PubMed:15712228"
FT /id="VAR_000448"
FT VARIANT 112
FT /note="R -> S (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062555"
FT VARIANT 113
FT /note="F -> I (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312142)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077381"
FT VARIANT 113
FT /note="F -> L (in FD; mild; dbSNP:rs869312142)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012384"
FT VARIANT 113
FT /note="F -> S (in FD)"
FT /evidence="ECO:0000269|PubMed:11668641"
FT /id="VAR_012385"
FT VARIANT 120..121
FT /note="LA -> PT (in FD)"
FT /id="VAR_000449"
FT VARIANT 120
FT /note="L -> V (in FD; has 42% of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:19621417"
FT /id="VAR_062556"
FT VARIANT 121
FT /note="A -> T (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs782197638)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077382"
FT VARIANT 128
FT /note="G -> E (in FD)"
FT /evidence="ECO:0000269|PubMed:8807334"
FT /id="VAR_000450"
FT VARIANT 131
FT /note="L -> P (in FD; dbSNP:rs869312298)"
FT /id="VAR_000451"
FT VARIANT 134
FT /note="Y -> S (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228,
FT ECO:0000269|PubMed:9100224"
FT /id="VAR_012386"
FT VARIANT 135
FT /note="A -> V (in FD; dbSNP:rs1569304221)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062557"
FT VARIANT 138
FT /note="G -> R (in FD)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012387"
FT VARIANT 142
FT /note="C -> R (in FD; dbSNP:rs886044845)"
FT /evidence="ECO:0000269|PubMed:10666480"
FT /id="VAR_012388"
FT VARIANT 142
FT /note="C -> Y (in FD)"
FT /evidence="ECO:0000269|PubMed:7759078,
FT ECO:0000269|PubMed:9105656"
FT /id="VAR_000452"
FT VARIANT 143
FT /note="A -> P (in FD; dbSNP:rs104894845)"
FT /evidence="ECO:0000269|PubMed:11889412"
FT /id="VAR_000453"
FT VARIANT 143
FT /note="A -> T (in FD; unknown pathological significance;
FT dbSNP:rs104894845)"
FT /evidence="ECO:0000269|PubMed:11668641,
FT ECO:0000269|PubMed:16533976, ECO:0000269|PubMed:27142856,
FT ECO:0000269|PubMed:9100224"
FT /id="VAR_012389"
FT VARIANT 144
FT /note="G -> V (in FD)"
FT /id="VAR_000454"
FT VARIANT 146
FT /note="P -> S (in FD; mild; dbSNP:rs104894837)"
FT /id="VAR_000455"
FT VARIANT 148
FT /note="S -> N (in FD; dbSNP:rs1555985829)"
FT /evidence="ECO:0000269|PubMed:10916280"
FT /id="VAR_012390"
FT VARIANT 148
FT /note="S -> R (in FD; dbSNP:rs1569304190)"
FT /evidence="ECO:0000269|PubMed:10666480,
FT ECO:0000269|PubMed:9100224"
FT /id="VAR_012391"
FT VARIANT 154
FT /note="I -> T (does not affect enzyme activity;
FT dbSNP:rs869312143)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077383"
FT VARIANT 156
FT /note="A -> T (in FD; dbSNP:rs28935195)"
FT /evidence="ECO:0000269|PubMed:7599642"
FT /id="VAR_000456"
FT VARIANT 156
FT /note="A -> V (in FD; dbSNP:rs869312307)"
FT /evidence="ECO:0000269|PubMed:7575533,
FT ECO:0000269|PubMed:7759078, ECO:0000269|PubMed:9105656"
FT /id="VAR_000457"
FT VARIANT 162
FT /note="W -> C (in FD; dbSNP:rs869312311)"
FT /evidence="ECO:0000269|PubMed:8931708"
FT /id="VAR_012392"
FT VARIANT 162
FT /note="W -> R (in FD; dbSNP:rs28935196)"
FT /evidence="ECO:0000269|PubMed:7504405"
FT /id="VAR_000458"
FT VARIANT 163
FT /note="G -> V (in FD)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012393"
FT VARIANT 164
FT /note="V -> G (in FD; loss of enzyme activity)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077384"
FT VARIANT 164
FT /note="V -> L (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312144)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077385"
FT VARIANT 165
FT /note="D -> V (in FD)"
FT /evidence="ECO:0000269|PubMed:10666480,
FT ECO:0000269|PubMed:8069316"
FT /id="VAR_000459"
FT VARIANT 166
FT /note="L -> V (in FD)"
FT /evidence="ECO:0000269|PubMed:7575533,
FT ECO:0000269|PubMed:7759078, ECO:0000269|PubMed:9105656"
FT /id="VAR_000460"
FT VARIANT 167
FT /note="L -> Q (in FD; loss of enzyme activity)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077386"
FT VARIANT 170
FT /note="D -> V (in FD)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012394"
FT VARIANT 171
FT /note="G -> D (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062558"
FT VARIANT 172
FT /note="C -> R (in FD)"
FT /evidence="ECO:0000269|PubMed:10916280"
FT /id="VAR_012395"
FT VARIANT 172
FT /note="C -> Y (in FD; dbSNP:rs869312318)"
FT /id="VAR_000461"
FT VARIANT 180
FT /note="L -> F (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312145)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077387"
FT VARIANT 183
FT /note="G -> D (in FD; dbSNP:rs869312320)"
FT /evidence="ECO:0000269|PubMed:10666480"
FT /id="VAR_012396"
FT VARIANT 187
FT /note="M -> I (in FD; loss of enzyme activity;
FT dbSNP:rs869312146)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077388"
FT VARIANT 187
FT /note="M -> V (in FD; decreased enzyme activity;
FT dbSNP:rs869312340)"
FT /evidence="ECO:0000269|PubMed:10916280,
FT ECO:0000269|PubMed:26415523"
FT /id="VAR_012397"
FT VARIANT 196
FT /note="R -> S (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312147)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077389"
FT VARIANT 198
FT /note="I -> T (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs727503950)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077390"
FT VARIANT 201
FT /note="S -> F (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062559"
FT VARIANT 202
FT /note="C -> W (in FD; dbSNP:rs104894838)"
FT /evidence="ECO:0000269|PubMed:10208848"
FT /id="VAR_000462"
FT VARIANT 202
FT /note="C -> Y (in FD; loss of enzyme activity;
FT dbSNP:rs869312344)"
FT /evidence="ECO:0000269|PubMed:26415523,
FT ECO:0000269|PubMed:9100224"
FT /id="VAR_012398"
FT VARIANT 204
FT /note="W -> R (in FD; loss of enzyme activity;
FT dbSNP:rs869312148)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077391"
FT VARIANT 205..207
FT /note="Missing (in FD)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012399"
FT VARIANT 205
FT /note="P -> T (in FD; dbSNP:rs397515870)"
FT /evidence="ECO:0000269|PubMed:8807334,
FT ECO:0000269|PubMed:8875188"
FT /id="VAR_000463"
FT VARIANT 213
FT /note="K -> R (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312149)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077392"
FT VARIANT 214
FT /note="P -> L (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312150)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077393"
FT VARIANT 215
FT /note="N -> S (in FD; mild; dbSNP:rs28935197)"
FT /evidence="ECO:0000269|PubMed:10666480,
FT ECO:0000269|PubMed:11668641, ECO:0000269|PubMed:15712228,
FT ECO:0000269|PubMed:8395937, ECO:0000269|PubMed:9452111"
FT /id="VAR_000464"
FT VARIANT 216
FT /note="Y -> D (in FD)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012400"
FT VARIANT 219
FT /note="I -> M (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312151)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077394"
FT VARIANT 219
FT /note="I -> N (in FD)"
FT /id="VAR_000465"
FT VARIANT 219
FT /note="I -> T (in FD; has 46% of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:19621417"
FT /id="VAR_062560"
FT VARIANT 223
FT /note="C -> G (in FD; dbSNP:rs869312381)"
FT /evidence="ECO:0000269|PubMed:10208848"
FT /id="VAR_012401"
FT VARIANT 224
FT /note="N -> D (in FD; dbSNP:rs1555985175)"
FT /evidence="ECO:0000269|PubMed:10208848,
FT ECO:0000269|PubMed:9452111"
FT /id="VAR_000466"
FT VARIANT 224
FT /note="N -> S (in FD; dbSNP:rs869312383)"
FT /evidence="ECO:0000269|PubMed:10916280"
FT /id="VAR_012402"
FT VARIANT 226
FT /note="W -> R (in FD)"
FT /evidence="ECO:0000269|PubMed:10916280"
FT /id="VAR_012403"
FT VARIANT 227
FT /note="R -> P (in FD; loss of enzyme activity;
FT dbSNP:rs104894840)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077395"
FT VARIANT 227
FT /note="R -> Q (in FD; dbSNP:rs104894840)"
FT /evidence="ECO:0000269|PubMed:10916280,
FT ECO:0000269|PubMed:7504405"
FT /id="VAR_000467"
FT VARIANT 228
FT /note="N -> S (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312152)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077396"
FT VARIANT 230
FT /note="A -> T (in FD)"
FT /evidence="ECO:0000269|PubMed:10916280"
FT /id="VAR_012404"
FT VARIANT 231
FT /note="D -> N (in FD)"
FT /evidence="ECO:0000269|PubMed:8863162"
FT /id="VAR_000468"
FT VARIANT 234
FT /note="D -> E (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062561"
FT VARIANT 235
FT /note="S -> C (in FD; dbSNP:rs797044746)"
FT /evidence="ECO:0000269|PubMed:10666480"
FT /id="VAR_012405"
FT VARIANT 236
FT /note="W -> C (in FD; dbSNP:rs869312386)"
FT /evidence="ECO:0000269|PubMed:8875188"
FT /id="VAR_012406"
FT VARIANT 236
FT /note="W -> L (in FD)"
FT /evidence="ECO:0000269|PubMed:10666480"
FT /id="VAR_012407"
FT VARIANT 242
FT /note="I -> N (in FD)"
FT /evidence="ECO:0000269|PubMed:9105656"
FT /id="VAR_012408"
FT VARIANT 242
FT /note="I -> V (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs397515873)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077397"
FT VARIANT 243
FT /note="L -> F (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs397515874)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077398"
FT VARIANT 244
FT /note="D -> H (in FD; dbSNP:rs727503948)"
FT /evidence="ECO:0000269|PubMed:10666480"
FT /id="VAR_012409"
FT VARIANT 244
FT /note="D -> N (in FD; dbSNP:rs727503948)"
FT /id="VAR_000469"
FT VARIANT 247
FT /note="S -> P (in FD; loss of enzyme activity;
FT dbSNP:rs869312393)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077399"
FT VARIANT 247
FT /note="S -> SWTS (in FD)"
FT /id="VAR_000470"
FT VARIANT 249
FT /note="N -> K (in FD; unknown pathological significance;
FT decreased enzyme activity)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077400"
FT VARIANT 253
FT /note="I -> T (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs727505292)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077401"
FT VARIANT 254
FT /note="V -> A (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312153)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077402"
FT VARIANT 258
FT /note="G -> R (in FD)"
FT /evidence="ECO:0000269|PubMed:11668641"
FT /id="VAR_012410"
FT VARIANT 259
FT /note="P -> L (in FD; dbSNP:rs869312399)"
FT /evidence="ECO:0000269|PubMed:10666480"
FT /id="VAR_012411"
FT VARIANT 259
FT /note="P -> R (in FD; decreased enzyme activity;
FT dbSNP:rs869312399)"
FT /evidence="ECO:0000269|PubMed:11668641,
FT ECO:0000269|PubMed:26415523"
FT /id="VAR_012412"
FT VARIANT 260
FT /note="G -> A (in FD)"
FT /evidence="ECO:0000269|PubMed:7575533,
FT ECO:0000269|PubMed:9105656"
FT /id="VAR_012413"
FT VARIANT 261
FT /note="G -> D (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228,
FT ECO:0000269|PubMed:9105656"
FT /id="VAR_012414"
FT VARIANT 262
FT /note="W -> R (in FD; loss of enzyme activity;
FT dbSNP:rs869312154)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077403"
FT VARIANT 263
FT /note="N -> S (in FD; dbSNP:rs869312404)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012415"
FT VARIANT 264
FT /note="D -> V (in FD; dbSNP:rs28935486)"
FT /evidence="ECO:0000269|PubMed:15712228,
FT ECO:0000269|PubMed:7504405"
FT /id="VAR_000471"
FT VARIANT 264
FT /note="D -> Y (in FD; dbSNP:rs190347120)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062562"
FT VARIANT 265
FT /note="P -> R (in FD)"
FT /evidence="ECO:0000269|PubMed:8931708"
FT /id="VAR_012416"
FT VARIANT 266
FT /note="D -> H (in FD)"
FT /evidence="ECO:0000269|PubMed:10916280"
FT /id="VAR_032291"
FT VARIANT 266
FT /note="D -> N (in FD; dbSNP:rs869312407)"
FT /evidence="ECO:0000269|PubMed:11076046"
FT /id="VAR_012418"
FT VARIANT 266
FT /note="D -> V (in FD; dbSNP:rs28935487)"
FT /evidence="ECO:0000269|PubMed:7504405"
FT /id="VAR_000472"
FT VARIANT 267
FT /note="M -> I (in FD; dbSNP:rs730880451)"
FT /evidence="ECO:0000269|PubMed:10666480,
FT ECO:0000269|PubMed:11668641"
FT /id="VAR_012419"
FT VARIANT 269
FT /note="V -> A (in FD; dbSNP:rs28935488)"
FT /evidence="ECO:0000269|PubMed:8395937"
FT /id="VAR_000473"
FT VARIANT 269
FT /note="V -> G (in FD; loss of enzyme activity;
FT dbSNP:rs28935488)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077404"
FT VARIANT 272
FT /note="N -> K (in FD)"
FT /id="VAR_000474"
FT VARIANT 272
FT /note="N -> S (in FD; dbSNP:rs28935495)"
FT /evidence="ECO:0000269|PubMed:15162124"
FT /id="VAR_032292"
FT VARIANT 276
FT /note="S -> G (in FD; loss of enzyme activity;
FT dbSNP:rs869312432)"
FT /evidence="ECO:0000269|PubMed:15712228,
FT ECO:0000269|PubMed:26415523"
FT /id="VAR_062563"
FT VARIANT 279
FT /note="Q -> E (in FD; mild; does not significantly affect
FT the enzyme activity but the mutant protein levels are
FT decreased presumably in the ER of the cells;
FT dbSNP:rs28935485)"
FT /evidence="ECO:0000269|PubMed:10838196,
FT ECO:0000269|PubMed:1315715, ECO:0000269|PubMed:7575533,
FT ECO:0000269|PubMed:9105656"
FT /id="VAR_000475"
FT VARIANT 279
FT /note="Q -> H (in FD)"
FT /evidence="ECO:0000269|PubMed:11668641"
FT /id="VAR_012420"
FT VARIANT 280
FT /note="Q -> H (in FD)"
FT /evidence="ECO:0000269|PubMed:11668641"
FT /id="VAR_012421"
FT VARIANT 284
FT /note="M -> T (in FD)"
FT /evidence="ECO:0000269|PubMed:8807334"
FT /id="VAR_000476"
FT VARIANT 285
FT /note="A -> P (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062564"
FT VARIANT 287
FT /note="W -> C (in FD; dbSNP:rs104894839)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012422"
FT VARIANT 287
FT /note="W -> G (in FD)"
FT /evidence="ECO:0000269|PubMed:8875188"
FT /id="VAR_012423"
FT VARIANT 288
FT /note="A -> D (in FD; dbSNP:rs869312437)"
FT /id="VAR_000477"
FT VARIANT 289
FT /note="I -> F (in FD; dbSNP:rs140329381)"
FT /evidence="ECO:0000269|PubMed:10666480"
FT /id="VAR_012424"
FT VARIANT 289
FT /note="I -> V (decreased enzyme activity;
FT dbSNP:rs140329381)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077405"
FT VARIANT 296
FT /note="M -> I (in FD; atypical; dbSNP:rs104894846)"
FT /evidence="ECO:0000269|PubMed:7575533,
FT ECO:0000269|PubMed:7596372, ECO:0000269|PubMed:9105656"
FT /id="VAR_012425"
FT VARIANT 296
FT /note="M -> V (in FD; mild; dbSNP:rs104894830)"
FT /evidence="ECO:0000269|PubMed:1846223"
FT /id="VAR_000478"
FT VARIANT 297
FT /note="S -> F (in FD; dbSNP:rs28935489)"
FT /evidence="ECO:0000269|PubMed:7504405"
FT /id="VAR_000479"
FT VARIANT 298
FT /note="N -> H (in FD)"
FT /evidence="ECO:0000269|PubMed:11668641,
FT ECO:0000269|PubMed:8875188"
FT /id="VAR_012426"
FT VARIANT 298
FT /note="N -> K (in FD)"
FT /evidence="ECO:0000269|PubMed:8807334"
FT /id="VAR_000480"
FT VARIANT 298
FT /note="N -> S (in FD; dbSNP:rs1569302985)"
FT /evidence="ECO:0000269|PubMed:9100224"
FT /id="VAR_012427"
FT VARIANT 300
FT /note="L -> F (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062565"
FT VARIANT 301
FT /note="R -> Q (in FD; mild; does not significantly affect
FT the enzyme activity but the mutant protein levels are
FT decreased presumably in the ER of the cells;
FT dbSNP:rs104894828)"
FT /evidence="ECO:0000269|PubMed:10208848,
FT ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:10916280,
FT ECO:0000269|PubMed:1315715, ECO:0000269|PubMed:2171331,
FT ECO:0000269|PubMed:7575533, ECO:0000269|PubMed:7599642,
FT ECO:0000269|PubMed:8738659, ECO:0000269|PubMed:9105656"
FT /id="VAR_000481"
FT VARIANT 309
FT /note="A -> V (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312155)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077406"
FT VARIANT 313
FT /note="D -> N (does not affect enzyme activity;
FT dbSNP:rs28935490)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077407"
FT VARIANT 313
FT /note="D -> Y (in FD; dbSNP:rs28935490)"
FT /evidence="ECO:0000269|PubMed:11668641,
FT ECO:0000269|PubMed:7504405, ECO:0000269|PubMed:9452111"
FT /id="VAR_000482"
FT VARIANT 315
FT /note="D -> N (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312156)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077408"
FT VARIANT 316..322
FT /note="Missing (in FD)"
FT /evidence="ECO:0000269|PubMed:8931708"
FT /id="VAR_012429"
FT VARIANT 316
FT /note="V -> A (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312157)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077409"
FT VARIANT 316
FT /note="V -> E (in FD)"
FT /evidence="ECO:0000269|PubMed:8069316"
FT /id="VAR_000483"
FT VARIANT 317
FT /note="I -> S (in FD; loss of enzyme activity;
FT dbSNP:rs869312158)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077410"
FT VARIANT 320
FT /note="N -> K (in FD)"
FT /evidence="ECO:0000269|PubMed:7575533,
FT ECO:0000269|PubMed:9105656"
FT /id="VAR_012430"
FT VARIANT 320
FT /note="N -> Y (in FD; loss of enzyme activity)"
FT /evidence="ECO:0000269|PubMed:10916280,
FT ECO:0000269|PubMed:26415523"
FT /id="VAR_012431"
FT VARIANT 321
FT /note="Q -> E (in FD; dbSNP:rs730880439)"
FT /evidence="ECO:0000269|PubMed:10666480"
FT /id="VAR_012432"
FT VARIANT 323
FT /note="P -> R (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312159)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077411"
FT VARIANT 327
FT /note="Q -> K (in FD; dbSNP:rs28935491)"
FT /evidence="ECO:0000269|PubMed:10208848,
FT ECO:0000269|PubMed:8395937"
FT /id="VAR_000484"
FT VARIANT 327
FT /note="Q -> L (in FD; loss of enzyme activity;
FT dbSNP:rs869312160)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077412"
FT VARIANT 327
FT /note="Q -> R (in FD; loss of enzyme activity;
FT dbSNP:rs869312160)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077413"
FT VARIANT 328
FT /note="G -> A (in FD; dbSNP:rs28935492)"
FT /evidence="ECO:0000269|PubMed:15712228,
FT ECO:0000269|PubMed:7504405"
FT /id="VAR_000486"
FT VARIANT 328
FT /note="G -> R (in FD; loss of enzyme activity;
FT dbSNP:rs104894832)"
FT /evidence="ECO:0000269|PubMed:1315715,
FT ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:7575533,
FT ECO:0000269|PubMed:9105656"
FT /id="VAR_000485"
FT VARIANT 328
FT /note="G -> V (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062566"
FT VARIANT 330
FT /note="Q -> R (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312161)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077414"
FT VARIANT 338
FT /note="E -> K (in FD)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062567"
FT VARIANT 340
FT /note="W -> R (in FD; dbSNP:rs1555984869)"
FT /evidence="ECO:0000269|PubMed:8875188"
FT /id="VAR_012433"
FT VARIANT 341
FT /note="E -> K (in FD; dbSNP:rs869312214)"
FT /evidence="ECO:0000269|PubMed:10090526"
FT /id="VAR_012434"
FT VARIANT 342
FT /note="R -> P (in FD; loss of enzyme activity)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077415"
FT VARIANT 342
FT /note="R -> Q (in FD; severe; dbSNP:rs28935493)"
FT /id="VAR_000487"
FT VARIANT 352
FT /note="A -> G (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312162)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077416"
FT VARIANT 356
FT /note="R -> P (in FD; loss of enzyme activity;
FT dbSNP:rs869312163)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077417"
FT VARIANT 356
FT /note="R -> Q (in FD; has 15% of wild-type activity;
FT dbSNP:rs869312163)"
FT /evidence="ECO:0000269|PubMed:19621417"
FT /id="VAR_062568"
FT VARIANT 356
FT /note="R -> W (in FD; severe; dbSNP:rs104894827)"
FT /evidence="ECO:0000269|PubMed:2539398"
FT /id="VAR_000488"
FT VARIANT 358
FT /note="E -> A (in FD; dbSNP:rs869312224)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062569"
FT VARIANT 358
FT /note="E -> K (in FD; loss of enzyme activity;
FT dbSNP:rs797044774)"
FT /evidence="ECO:0000269|PubMed:26415523,
FT ECO:0000269|PubMed:9452068"
FT /id="VAR_000489"
FT VARIANT 358
FT /note="Missing (in FD; dbSNP:rs730880453)"
FT /evidence="ECO:0000269|PubMed:10666480,
FT ECO:0000269|PubMed:15712228, ECO:0000269|PubMed:8807334,
FT ECO:0000269|PubMed:9105656"
FT /id="VAR_000490"
FT VARIANT 360
FT /note="G -> C (in FD; has 6% of wild-type activity;
FT dbSNP:rs782598150)"
FT /evidence="ECO:0000269|PubMed:19621417"
FT /id="VAR_062570"
FT VARIANT 360
FT /note="G -> S (in FD; loss of enzyme activity)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077418"
FT VARIANT 361
FT /note="G -> R (in FD; severe; dbSNP:rs28935494)"
FT /evidence="ECO:0000269|PubMed:8395937"
FT /id="VAR_000491"
FT VARIANT 363
FT /note="R -> H (in FD; dbSNP:rs111422676)"
FT /evidence="ECO:0000269|PubMed:11668641"
FT /id="VAR_012435"
FT VARIANT 373
FT /note="G -> D (in FD; dbSNP:rs869312227)"
FT /evidence="ECO:0000269|PubMed:11295840"
FT /id="VAR_012436"
FT VARIANT 373
FT /note="G -> S (in FD; dbSNP:rs727504348)"
FT /evidence="ECO:0000269|PubMed:7575533,
FT ECO:0000269|PubMed:9105656"
FT /id="VAR_012437"
FT VARIANT 375
FT /note="G -> A (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312164)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077419"
FT VARIANT 377
FT /note="A -> D (in FD)"
FT /evidence="ECO:0000269|PubMed:11668641"
FT /id="VAR_012438"
FT VARIANT 378
FT /note="C -> Y (in FD)"
FT /evidence="ECO:0000269|PubMed:10666480"
FT /id="VAR_012439"
FT VARIANT 383
FT /note="Missing (in FD; severe; with facial telangiectasias;
FT dbSNP:rs1057519609)"
FT /evidence="ECO:0000269|PubMed:8834244"
FT /id="VAR_000492"
FT VARIANT 392
FT /note="R -> S (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs869312165)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077420"
FT VARIANT 396
FT /note="F -> Y (in RNA edited version)"
FT /id="VAR_000493"
FT VARIANT 399
FT /note="W -> S (in FD; unknown pathological significance;
FT decreased enzyme activity; dbSNP:rs782449839)"
FT /evidence="ECO:0000269|PubMed:26415523"
FT /id="VAR_077421"
FT VARIANT 404
FT /note="Missing (in FD; mild; loss of enzyme activity)"
FT /evidence="ECO:0000269|PubMed:15712228,
FT ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:7504405,
FT ECO:0000269|PubMed:9100224"
FT /id="VAR_000494"
FT VARIANT 409
FT /note="P -> A (in FD; dbSNP:rs878853698)"
FT /evidence="ECO:0000269|PubMed:11668641"
FT /id="VAR_012440"
FT VARIANT 409
FT /note="P -> T (in FD)"
FT /evidence="ECO:0000269|PubMed:11668641"
FT /id="VAR_012441"
FT VARIANT 410
FT /note="T -> A (in FD; mild; dbSNP:rs104894852)"
FT /evidence="ECO:0000269|PubMed:12694230"
FT /id="VAR_032293"
FT VARIANT 414
FT /note="L -> S (in FD; dbSNP:rs869312246)"
FT /evidence="ECO:0000269|PubMed:15712228"
FT /id="VAR_062571"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:3HG3"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3HG3"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3GXT"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1R47"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3HG3"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:6IBT"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 177..193
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:3HG3"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:3HG3"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 305..311
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:3HG3"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:6IBK"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:3HG3"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 379..390
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:3HG3"
FT STRAND 412..419
FT /evidence="ECO:0007829|PDB:3HG3"
FT HELIX 420..424
FT /evidence="ECO:0007829|PDB:3HG3"
SQ SEQUENCE 429 AA; 48767 MW; 613F8BF21B107D7B CRC64;
MQLRNPELHL GCALALRFLA LVSWDIPGAR ALDNGLARTP TMGWLHWERF MCNLDCQEEP
DSCISEKLFM EMAELMVSEG WKDAGYEYLC IDDCWMAPQR DSEGRLQADP QRFPHGIRQL
ANYVHSKGLK LGIYADVGNK TCAGFPGSFG YYDIDAQTFA DWGVDLLKFD GCYCDSLENL
ADGYKHMSLA LNRTGRSIVY SCEWPLYMWP FQKPNYTEIR QYCNHWRNFA DIDDSWKSIK
SILDWTSFNQ ERIVDVAGPG GWNDPDMLVI GNFGLSWNQQ VTQMALWAIM AAPLFMSNDL
RHISPQAKAL LQDKDVIAIN QDPLGKQGYQ LRQGDNFEVW ERPLSGLAWA VAMINRQEIG
GPRSYTIAVA SLGKGVACNP ACFITQLLPV KRKLGFYEWT SRLRSHINPT GTVLLQLENT
MQMSLKDLL
