FUCO_HUMAN
ID FUCO_HUMAN Reviewed; 466 AA.
AC P04066; B2RBG3; Q14334; Q14335; Q3LID0; Q8NAC2;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 4.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Tissue alpha-L-fucosidase {ECO:0000305};
DE EC=3.2.1.51 {ECO:0000305|PubMed:9741689};
DE AltName: Full=Alpha-L-fucosidase I;
DE AltName: Full=Alpha-L-fucoside fucohydrolase 1;
DE Short=Alpha-L-fucosidase 1;
DE Flags: Precursor;
GN Name=FUCA1 {ECO:0000312|HGNC:HGNC:4006}; ORFNames=Nbla10230;
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 [GENOMIC DNA], VARIANT FUCA1D ASP-65, AND VARIANT
RP ARG-286.
RX PubMed=8504303; DOI=10.1093/hmg/2.4.423;
RA Seo H.-C., Willems P.J., Kretz K.A., Martin B.M., O'Brien J.S.;
RT "Fucosidosis: four new mutations and a new polymorphism.";
RL Hum. Mol. Genet. 2:423-429(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-286.
RC TISSUE=Spleen, and Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 2-466, AND VARIANT SER-269.
RX PubMed=2803312; DOI=10.1016/0006-291x(89)91739-7;
RA Occhiodoro T., Beckmann K.R., Morris C.P., Hopwood J.J.;
RT "Human alpha-L-fucosidase: complete coding sequence from cDNA clones.";
RL Biochem. Biophys. Res. Commun. 164:439-445(1989).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-92.
RC TISSUE=Placenta;
RX PubMed=2174090; DOI=10.1007/bf01799583;
RA Fukushima H., Nishimoto J., Okada S.;
RT "Sequencing and expression of a full-length cDNA for human alpha-L-
RT fucosidase.";
RL J. Inherit. Metab. Dis. 13:761-765(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-427.
RX PubMed=2983333; DOI=10.1073/pnas.82.4.1262;
RA Fukushima H., de Wet J.R., O'Brien J.S.;
RT "Molecular cloning of a cDNA for human alpha-L-fucosidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1262-1265(1985).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-426.
RX PubMed=6096099; DOI=10.1089/dna.1.1984.3.437;
RA de Wet J.R., Fukushima H., Dewji N.N., Wilcox E., O'Brien J.S.,
RA Helinski D.R.;
RT "Chromogenic immunodetection of human serum albumin and alpha-L-fucosidase
RT clones in a human hepatoma cDNA expression library.";
RL DNA 3:437-447(1984).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-426, AND VARIANT SER-269.
RX PubMed=2894306; DOI=10.1159/000469189;
RA O'Brien J.S., Willems P.J., Fukushima H., de Wet J.R., Darby J.K.,
RA Dicioccio R.A., Fowler M.L., Shows T.B.;
RT "Molecular biology of the alpha-6L-fucosidase gene and fucosidosis.";
RL Enzyme 38:45-53(1987).
RN [11]
RP STRUCTURE OF CARBOHYDRATES.
RA Beem E.P., Lisman J.J.W., van Steijn G.J., van der Wal C.J.,
RA Trippelvitz L.A.W., Overdijk B., van Halbeek H., Mutsaers J.H.G.M.,
RA Vliegenthart J.F.G.;
RT "Structural analysis of the carbohydrate moieties of alpha-L-fucosidase
RT from human liver.";
RL Glycoconj. J. 4:33-42(1987).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=9741689;
RA Asfaw B., Schindler D., Ledvinova J., Cerny B., Smid F., Conzelmann E.;
RT "Degradation of blood group A glycolipid A-6-2 by normal and mutant human
RT skin fibroblasts.";
RL J. Lipid Res. 39:1768-1780(1998).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-241 AND ASN-382.
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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
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 [18]
RP VARIANT ARG-286.
RX PubMed=8399358; DOI=10.1016/0925-4439(93)90065-9;
RA Yang M., Allen H., Dicioccio R.A.;
RT "Pedigree analysis of alpha-L-fucosidase gene mutations in a fucosidosis
RT family.";
RL Biochim. Biophys. Acta 1182:245-249(1993).
RN [19]
RP VARIANT FUCA1D LEU-68.
RX PubMed=7874128;
RA Seo H.-C., Yang M., Tonlorenzi R., Willems P.J., Kim A.H., Filocamo M.,
RA Gatti R., Dicioccio R.A., O'Brien J.S.;
RT "A missense mutation (S63L) in alpha-L-fucosidase is responsible for
RT fucosidosis in an Italian patient.";
RL Hum. Mol. Genet. 3:2065-2066(1994).
RN [20]
RP VARIANT ARG-286.
RX PubMed=7815431; DOI=10.1136/jmg.31.8.659-a;
RA Cragg H., Winchester B., Seo H.-C., O'Brien J.S., Swallow D.;
RT "Molecular basis of the common electrophoretic polymorphism (Fu1/Fu2) in
RT human alpha-L-fucosidase.";
RL J. Med. Genet. 31:659-660(1994).
RN [21]
RP VARIANT FUCA1D ARG-410.
RX PubMed=9762612; DOI=10.1023/a:1005405222252;
RA Fleming C.J., Sinclair D.U., White E.J., Winchester B., Whiteford M.L.,
RA Connor J.M.;
RT "A fucosidosis patient with relative longevity and a missense mutation in
RT exon 7 of the alpha-fucosidase gene.";
RL J. Inherit. Metab. Dis. 21:688-689(1998).
RN [22]
RP REVIEW ON VARIANTS.
RX PubMed=10094192; DOI=10.1038/sj.ejhg.5200272;
RA Willems P.J., Seo H.-C., Coucke P., Tonlorenzi R., O'Brien J.S.;
RT "Spectrum of mutations in fucosidosis.";
RL Eur. J. Hum. Genet. 7:60-67(1999).
RN [23]
RP VARIANTS SER-269 AND ARG-286.
RX PubMed=12408193; DOI=10.1023/a:1020116220624;
RA Ip P., Goh W., Chan K.W., Cheung P.T.;
RT "A novel FUCA1 mutation causing fucosidosis in a Chinese boy.";
RL J. Inherit. Metab. Dis. 25:415-416(2002).
CC -!- FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC 1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC carbohydrate moieties of glycoproteins. {ECO:0000269|PubMed:9741689}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-L-fucoside + H2O = an alcohol + L-fucose;
CC Xref=Rhea:RHEA:12288, ChEBI:CHEBI:2181, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28349, ChEBI:CHEBI:30879; EC=3.2.1.51;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10054};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12289;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + H2O = a
CC neolactoside nLc4Cer(d18:1(4E)) + L-fucose; Xref=Rhea:RHEA:48224,
CC ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:17006,
CC ChEBI:CHEBI:28691; Evidence={ECO:0000269|PubMed:9741689};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48225;
CC Evidence={ECO:0000269|PubMed:9741689};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:0) + H2O = a
CC neolactoside nLc4Cer(d18:0) + L-fucose; Xref=Rhea:RHEA:49308,
CC ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:91119,
CC ChEBI:CHEBI:91121; Evidence={ECO:0000269|PubMed:9741689};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49309;
CC Evidence={ECO:0000269|PubMed:9741689};
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P04066; Q99828: CIB1; NbExp=3; IntAct=EBI-2512153, EBI-372594;
CC P04066; Q9BTT4: MED10; NbExp=3; IntAct=EBI-2512153, EBI-394354;
CC P04066; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-2512153, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9741689}.
CC -!- POLYMORPHISM: There are two common alleles of FUCA1; FUCA1*1; also
CC known as Fu1; has Arg-281 and FUCA1*2; also known as Fu2; has Gln-281.
CC -!- DISEASE: Fucosidosis (FUCA1D) [MIM:230000]: An autosomal recessive
CC lysosomal storage disease characterized by accumulation of fucose-
CC containing glycolipids and glycoproteins in various tissues. Clinical
CC signs include facial dysmorphism, dysostosis multiplex, moderate
CC hepatomegaly, severe intellectual deficit, deafness, and according to
CC age, angiokeratomas. {ECO:0000269|PubMed:7874128,
CC ECO:0000269|PubMed:8504303, ECO:0000269|PubMed:9762612}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35519.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA52481.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH17338.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG37210.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA25646.1; Type=Miscellaneous discrepancy; Note=Translation of X01390 sequence produces a larger peptide than that shown in CAA25646.1.; Evidence={ECO:0000305};
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DR EMBL; M80815; AAA52481.1; ALT_INIT; Genomic_DNA.
DR EMBL; M80809; AAA52481.1; JOINED; Genomic_DNA.
DR EMBL; M80810; AAA52481.1; JOINED; Genomic_DNA.
DR EMBL; M80811; AAA52481.1; JOINED; Genomic_DNA.
DR EMBL; M80812; AAA52481.1; JOINED; Genomic_DNA.
DR EMBL; M80813; AAA52481.1; JOINED; Genomic_DNA.
DR EMBL; M80814; AAA52481.1; JOINED; Genomic_DNA.
DR EMBL; AB074175; BAE45738.1; -; mRNA.
DR EMBL; AK092914; BAC04002.1; -; mRNA.
DR EMBL; AK314649; BAG37210.1; ALT_INIT; mRNA.
DR EMBL; AL590728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017338; AAH17338.1; ALT_INIT; mRNA.
DR EMBL; M29877; AAA35519.1; ALT_INIT; mRNA.
DR EMBL; M10355; AAA52482.1; -; mRNA.
DR EMBL; X01390; CAA25646.1; ALT_SEQ; mRNA.
DR CCDS; CCDS244.2; -.
DR PIR; A33427; HWHUFA.
DR RefSeq; NP_000138.2; NM_000147.4.
DR AlphaFoldDB; P04066; -.
DR SMR; P04066; -.
DR BioGRID; 108793; 32.
DR IntAct; P04066; 17.
DR MINT; P04066; -.
DR STRING; 9606.ENSP00000363603; -.
DR BindingDB; P04066; -.
DR ChEMBL; CHEMBL4176; -.
DR SwissLipids; SLP:000001407; -.
DR CAZy; GH29; Glycoside Hydrolase Family 29.
DR GlyConnect; 1810; 6 N-Linked glycans (2 sites).
DR GlyGen; P04066; 4 sites, 6 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P04066; -.
DR MetOSite; P04066; -.
DR PhosphoSitePlus; P04066; -.
DR BioMuta; FUCA1; -.
DR DMDM; 156631012; -.
DR CPTAC; CPTAC-2215; -.
DR EPD; P04066; -.
DR jPOST; P04066; -.
DR MassIVE; P04066; -.
DR MaxQB; P04066; -.
DR PaxDb; P04066; -.
DR PeptideAtlas; P04066; -.
DR PRIDE; P04066; -.
DR ProteomicsDB; 51645; -.
DR Antibodypedia; 30233; 306 antibodies from 29 providers.
DR DNASU; 2517; -.
DR Ensembl; ENST00000374479.4; ENSP00000363603.3; ENSG00000179163.12.
DR GeneID; 2517; -.
DR KEGG; hsa:2517; -.
DR MANE-Select; ENST00000374479.4; ENSP00000363603.3; NM_000147.5; NP_000138.2.
DR UCSC; uc001bie.5; human.
DR CTD; 2517; -.
DR DisGeNET; 2517; -.
DR GeneCards; FUCA1; -.
DR HGNC; HGNC:4006; FUCA1.
DR HPA; ENSG00000179163; Low tissue specificity.
DR MalaCards; FUCA1; -.
DR MIM; 230000; phenotype.
DR MIM; 612280; gene.
DR neXtProt; NX_P04066; -.
DR OpenTargets; ENSG00000179163; -.
DR Orphanet; 349; Fucosidosis.
DR PharmGKB; PA28422; -.
DR VEuPathDB; HostDB:ENSG00000179163; -.
DR eggNOG; KOG3340; Eukaryota.
DR GeneTree; ENSGT00440000035378; -.
DR HOGENOM; CLU_002934_1_1_1; -.
DR InParanoid; P04066; -.
DR OMA; LPEHKWE; -.
DR OrthoDB; 929780at2759; -.
DR PhylomeDB; P04066; -.
DR TreeFam; TF313034; -.
DR BRENDA; 3.2.1.51; 2681.
DR PathwayCommons; P04066; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR SABIO-RK; P04066; -.
DR SignaLink; P04066; -.
DR BioGRID-ORCS; 2517; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; FUCA1; human.
DR GeneWiki; Fucosidase; -.
DR GenomeRNAi; 2517; -.
DR Pharos; P04066; Tchem.
DR PRO; PR:P04066; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P04066; protein.
DR Bgee; ENSG00000179163; Expressed in mucosa of sigmoid colon and 203 other tissues.
DR Genevisible; P04066; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IDA:UniProtKB.
DR GO; GO:0006004; P:fucose metabolic process; IDA:UniProtKB.
DR GO; GO:0019377; P:glycolipid catabolic process; ISS:BHF-UCL.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; NAS:UniProtKB.
DR GO; GO:0016139; P:glycoside catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR028755; FUCA1.
DR InterPro; IPR031919; Fucosidase_C.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR018526; Glyco_hydro_29_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10030; PTHR10030; 1.
DR PANTHER; PTHR10030:SF2; PTHR10030:SF2; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF16757; Fucosidase_C; 1.
DR PIRSF; PIRSF001092; Alpha-L-fucosidase; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
PE 1: Evidence at protein level;
KW Disease variant; Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism;
KW Lysosome; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..466
FT /note="Tissue alpha-L-fucosidase"
FT /id="PRO_0000010308"
FT SITE 296
FT /note="May be important for catalysis"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VARIANT 2
FT /note="R -> W (in dbSNP:rs2070955)"
FT /id="VAR_049106"
FT VARIANT 10
FT /note="P -> R (in dbSNP:rs2070956)"
FT /id="VAR_016233"
FT VARIANT 65
FT /note="G -> D (in FUCA1D; loss of activity;
FT dbSNP:rs1353778985)"
FT /evidence="ECO:0000269|PubMed:8504303"
FT /id="VAR_002442"
FT VARIANT 68
FT /note="S -> L (in FUCA1D)"
FT /evidence="ECO:0000269|PubMed:7874128"
FT /id="VAR_002443"
FT VARIANT 146
FT /note="P -> L (in dbSNP:rs2228424)"
FT /id="VAR_049107"
FT VARIANT 260
FT /note="V -> I (in dbSNP:rs665)"
FT /id="VAR_049108"
FT VARIANT 269
FT /note="C -> S (in dbSNP:rs1126512)"
FT /evidence="ECO:0000269|PubMed:12408193,
FT ECO:0000269|PubMed:2803312, ECO:0000269|PubMed:2894306"
FT /id="VAR_016234"
FT VARIANT 286
FT /note="Q -> R (in allele FUCA1*2; dbSNP:rs13551)"
FT /evidence="ECO:0000269|PubMed:12408193,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:7815431,
FT ECO:0000269|PubMed:8399358, ECO:0000269|PubMed:8504303"
FT /id="VAR_002444"
FT VARIANT 410
FT /note="L -> R (in FUCA1D; less than 1% of residual
FT activity; dbSNP:rs80358199)"
FT /evidence="ECO:0000269|PubMed:9762612"
FT /id="VAR_016235"
FT CONFLICT 54..56
FT /note="DEA -> NEV (in Ref. 3; BAC04002)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="S -> T (in Ref. 7; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 76..77
FT /note="WF -> FL (in Ref. 8; AAA52482 and 9; CAA25646)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..114
FT /note="Missing (in Ref. 3; BAC04002)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="A -> T (in Ref. 3; BAC04002)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="A -> G (in Ref. 3; BAC04002)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="N -> D (in Ref. 3; BAC04002)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="Q -> P (in Ref. 8; AAA52482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 53689 MW; D9A38ECC7BADCBBB CRC64;
MRAPGMRSRP AGPALLLLLL FLGAAESVRR AQPPRRYTPD WPSLDSRPLP AWFDEAKFGV
FIHWGVFSVP AWGSEWFWWH WQGEGRPQYQ RFMRDNYPPG FSYADFGPQF TARFFHPEEW
ADLFQAAGAK YVVLTTKHHE GFTNWPSPVS WNWNSKDVGP HRDLVGELGT ALRKRNIRYG
LYHSLLEWFH PLYLLDKKNG FKTQHFVSAK TMPELYDLVN SYKPDLIWSD GEWECPDTYW
NSTNFLSWLY NDSPVKDEVV VNDRWGQNCS CHHGGYYNCE DKFKPQSLPD HKWEMCTSID
KFSWGYRRDM ALSDVTEESE IISELVQTVS LGGNYLLNIG PTKDGLIVPI FQERLLAVGK
WLSINGEAIY ASKPWRVQWE KNTTSVWYTS KGSAVYAIFL HWPENGVLNL ESPITTSTTK
ITMLGIQGDL KWSTDPDKGL FISLPQLPPS AVPAEFAWTI KLTGVK
