DCUP_HUMAN
ID DCUP_HUMAN Reviewed; 367 AA.
AC P06132; A8K762; Q16863; Q16883; Q53YB8; Q53ZP6; Q6IB28; Q9BUZ0;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000305};
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37 {ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:14633982, ECO:0000269|PubMed:21668429};
GN Name=UROD {ECO:0000312|HGNC:HGNC:12591};
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], AND PROTEIN SEQUENCE OF 2-21; 37-65; 101-123;
RP 175-251; 259-322; 325-344 AND 346-367.
RX PubMed=3015909; DOI=10.1016/s0021-9258(18)67589-1;
RA Romeo P.-H., Raich N., Dubart A., Beaupain D., Pryor M., Kushner J.P.,
RA Cohen-Solal M., Goossens M.;
RT "Molecular cloning and nucleotide sequence of a complete human
RT uroporphyrinogen decarboxylase cDNA.";
RL J. Biol. Chem. 261:9825-9831(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HEP LEU-62; LEU-77; GLU-281
RP AND CYS-311.
RX PubMed=8644733;
RA Moran-Jimenez M.J., Ged C., Romana M., de Salamanca R.E., Taieb A.,
RA Topi G., D'Alessandro L., de Verneuil H.;
RT "Uroporphyrinogen decarboxylase: complete human gene sequence and molecular
RT study of three families with hepatoerythropoietic porphyria.";
RL Am. J. Hum. Genet. 58:712-721(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mendez M.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-77.
RA Martinez di Montemuros F., Fiorelli G., Cappellini M.D.;
RT "Uroporphyrinogen decarboxylase (UROD) cDNA sequence from Italian
RT population.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-77.
RA Martinez di Montemuros F., Cappellini M.D.;
RT "Molecular characterization of UROD gene in Italian patients with familial
RT porphyria cutanea tarda (f-PCT).";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-303.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [10]
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-303.
RC TISSUE=Lymph;
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 [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=3658695; DOI=10.1093/nar/15.18.7343;
RA Romana M., Dubart A., Beaupain D., Chabret C., Goossens M., Romeo P.-H.;
RT "Structure of the gene for human uroporphyrinogen decarboxylase.";
RL Nucleic Acids Res. 15:7343-7356(1987).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-258, AND INVOLVEMENT IN FPCT.
RX PubMed=2243121; DOI=10.1172/jci114856;
RA Garey J.R., Harrison L.M., Franklin K.F., Metcalf K.M., Radisky E.S.,
RA Kushner J.P.;
RT "Uroporphyrinogen decarboxylase: a splice site mutation causes the deletion
RT of exon 6 in multiple families with porphyria cutanea tarda.";
RL J. Clin. Invest. 86:1416-1422(1990).
RN [15]
RP CRYSTALLIZATION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=9194196; DOI=10.1002/pro.5560060624;
RA Phillips J.D., Whitby F.G., Kushner J.P., Hill C.P.;
RT "Characterization and crystallization of human uroporphyrinogen
RT decarboxylase.";
RL Protein Sci. 6:1343-1346(1997).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT.
RX PubMed=9564029; DOI=10.1093/emboj/17.9.2463;
RA Whitby F.G., Phillips J.D., Kushner J.P., Hill C.P.;
RT "Crystal structure of human uroporphyrinogen decarboxylase.";
RL EMBO J. 17:2463-2471(1998).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANTS FPCT ASP-156; LEU-232 AND
RP THR-260, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, VARIANTS FPCT GLU-25;
RP SER-80; GLN-134; ASP-156; ARG-165; LYS-167; PRO-193; LEU-232; GLN-253 AND
RP THR-260, AND CHARACTERIZATION OF VARIANTS FPCT GLU-25; SER-80; GLN-134;
RP ASP-156; ARG-165; LYS-167; PRO-193; LEU-232; GLN-253 AND THR-260.
RX PubMed=11719352; DOI=10.1182/blood.v98.12.3179;
RA Phillips J.D., Parker T.L., Schubert H.L., Whitby F.G., Hill C.P.,
RA Kushner J.P.;
RT "Functional consequences of naturally occurring mutations in human
RT uroporphyrinogen decarboxylase.";
RL Blood 98:3179-3185(2001).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF WILD-TYPE AND MUTANTS ASN-86;
RP GLU-86; GLY-86 AND PHE-164 IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF ASP-86 AND TYR-164, AND
RP REACTION MECHANISM.
RX PubMed=14633982; DOI=10.1093/emboj/cdg606;
RA Phillips J.D., Whitby F.G., Kushner J.P., Hill C.P.;
RT "Structural basis for tetrapyrrole coordination by uroporphyrinogen
RT decarboxylase.";
RL EMBO J. 22:6225-6233(2003).
RN [23]
RP VARIANT HEP GLU-281.
RX PubMed=3775362; DOI=10.1126/science.3775362;
RA de Verneuil H., Grandchamp B., Beaumont C., Picat C., Nordmann Y.;
RT "Uroporphyrinogen decarboxylase structural mutant (Gly-281-->Glu) in a case
RT of porphyria.";
RL Science 234:732-734(1986).
RN [24]
RP VARIANT FPCT VAL-281.
RX PubMed=2920211;
RA Garey J.R., Hansen J.L., Harrison L.M., Kennedy J.B., Kushner J.P.;
RT "A point mutation in the coding region of uroporphyrinogen decarboxylase
RT associated with familial porphyria cutanea tarda.";
RL Blood 73:892-895(1989).
RN [25]
RP VARIANT HEP LYS-167.
RX PubMed=1905636; DOI=10.1111/j.1365-2362.1991.tb01814.x;
RA Romana M., Grandchamp B., Dubart A., Amselem S., Chabret C., Nordmann Y.,
RA Goossens M., Romeo P.-H.;
RT "Identification of a new mutation responsible for hepatoerythropoietic
RT porphyria.";
RL Eur. J. Clin. Invest. 21:225-229(1991).
RN [26]
RP VARIANT HEP GLY-292.
RX PubMed=1634232; DOI=10.1007/bf00219182;
RA de Verneuil H., Bourgeois F., de Rooij F.W.M., Siersema P.D.,
RA Wilson J.H.P., Grandchamp B., Nordmann Y.;
RT "Characterization of a new mutation (R292G) and a deletion at the human
RT uroporphyrinogen decarboxylase locus in two patients with
RT hepatoerythropoietic porphyria.";
RL Hum. Genet. 89:548-552(1992).
RN [27]
RP VARIANTS HEP GLN-134 AND PRO-220.
RX PubMed=8176248; DOI=10.1111/1523-1747.ep12374134;
RA Meguro K., Fujita H., Ishida N., Akagi R., Kurihara T., Galbraith R.A.,
RA Kappas A., Zabriskie J.B., Toback A.C., Harber L.C., Sassa S.;
RT "Molecular defects of uroporphyrinogen decarboxylase in a patient with mild
RT hepatoerythropoietic porphyria.";
RL J. Invest. Dermatol. 102:681-685(1994).
RN [28]
RP VARIANT FPCT GLU-281.
RX PubMed=7706766; DOI=10.1111/1523-1747.ep12605953;
RA Roberts A.G., Elder G.H., de Salamanca R.E., Herrero C., Lecha M.,
RA Mascaro J.M.;
RT "A mutation 'G281E' of the human uroporphyrinogen decarboxylase gene causes
RT both hepatoerythropoietic porphyria and overt familial porphyria cutanea
RT tarda: biochemical and genetic studies on Spanish patients.";
RL J. Invest. Dermatol. 104:500-502(1995).
RN [29]
RP VARIANT HEP GLY-80, AND VARIANTS FPCT GLN-253; ARG-318 AND THR-334.
RX PubMed=8896428;
RA McManus J.F., Begley C.G., Sassa S., Ratnaike S.;
RT "Five new mutations in the uroporphyrinogen decarboxylase gene identified
RT in families with cutaneous porphyria.";
RL Blood 88:3589-3600(1996).
RN [30]
RP VARIANTS FPCT ARG-165; PHE-195; LYS-304 AND HIS-332.
RX PubMed=9792863; DOI=10.1086/302119;
RA Mendez M., Sorkin L., Rossetti M.V., Astrin K.H., Batlle A.M.C.,
RA Parera V.E., Aizencang G.I., Desnick R.J.;
RT "Familial porphyria cutanea tarda: characterization of seven novel
RT uroporphyrinogen decarboxylase mutations and frequency of common
RT hemochromatosis alleles.";
RL Am. J. Hum. Genet. 63:1363-1375(1998).
RN [31]
RP VARIANT FPCT GLN-134.
RX PubMed=10338097;
RX DOI=10.1002/(sici)1098-1004(1999)13:5<412::aid-humu13>3.0.co;2-n;
RA McManus J.F., Begley C.G., Sassa S., Ratnaike S.;
RT "Three new mutations in the uroporphyrinogen decarboxylase gene in familial
RT porphyria cutanea tarda.";
RL Hum. Mutat. 13:412-412(1999).
RN [32]
RP VARIANTS FPCT LEU-229 AND THR-324.
RX PubMed=10477430;
RX DOI=10.1002/(sici)1098-1004(1999)14:3<222::aid-humu5>3.0.co;2-v;
RA Christiansen L., Ged C., Hombrados I., Broens-Poulsen J., Fontanellas A.,
RA de Verneuil H., Hoerder M., Petersen N.E.;
RT "Screening for mutations in the uroporphyrinogen decarboxylase gene using
RT denaturing gradient gel electrophoresis. Identification and
RT characterization of six novel mutations associated with familial PCT.";
RL Hum. Mutat. 14:222-232(1999).
RN [33]
RP VARIANTS FPCT SER-80; GLN-134; PRO-144; GLN-216; LYS-218; VAL-281; ARG-282;
RP SER-303 AND ARG-318, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP CHARACTERIZATION OF VARIANTS FPCT PRO-144 AND LYS-218.
RX PubMed=11069625; DOI=10.1046/j.1523-1747.2000.00148.x;
RA Brady J.J., Jackson H.A., Roberts A.G., Morgan R.R., Whatley S.D.,
RA Rowlands G.L., Darby C., Shudell E., Watson R., Paiker J., Worwood M.W.,
RA Elder G.H.;
RT "Co-inheritance of mutations in the uroporphyrinogen decarboxylase and
RT hemochromatosis genes accelerates the onset of porphyria cutanea tarda.";
RL J. Invest. Dermatol. 115:868-874(2000).
RN [34]
RP VARIANTS FPCT GLN-142; GLN-161; PHE-219 AND SER-235.
RX PubMed=11295834; DOI=10.1002/humu.35;
RA Cappellini M.D., Martinez Di Montemuros F., Tavazzi D., Fargion S.,
RA Pizzuti A., Comino A., Cainelli T., Fiorelli G.;
RT "Seven novel point mutations in the uroporphyrinogen decarboxylase (UROD)
RT gene in patients with familial porphyria cutanea tarda (f-PCT).";
RL Hum. Mutat. 17:350-350(2001).
RN [35]
RP VARIANT HEP LEU-46, FUNCTION, AND CHARACTERIZATION OF VARIANT HEP LEU-46.
RX PubMed=12071824; DOI=10.1001/archderm.138.7.957;
RA Ged C., Ozalla D., Herrero C., Lecha M., Mendez M., de Verneuil H.,
RA Mascaro J.M.;
RT "Description of a new mutation in hepatoerythropoietic porphyria and
RT prenatal exclusion of a homozygous fetus.";
RL Arch. Dermatol. 138:957-960(2002).
RN [36]
RP VARIANT HEP LEU-46.
RX PubMed=15491440; DOI=10.1111/j.1365-2133.2004.06101.x;
RA Armstrong D.K.B., Sharpe P.C., Chambers C.R., Whatley S.D., Roberts A.G.,
RA Elder G.H.;
RT "Hepatoerythropoietic porphyria: a missense mutation in the UROD gene is
RT associated with mild disease and an unusual porphyrin excretion pattern.";
RL Br. J. Dermatol. 151:920-923(2004).
RN [37]
RP VARIANT HEP ARG-168, AND CHARACTERIZATION OF VARIANT HEP ARG-168.
RX PubMed=17240319; DOI=10.1016/j.trsl.2006.08.006;
RA Phillips J.D., Whitby F.G., Stadtmueller B.M., Edwards C.Q., Hill C.P.,
RA Kushner J.P.;
RT "Two novel uroporphyrinogen decarboxylase (URO-D) mutations causing
RT hepatoerythropoietic porphyria (HEP).";
RL Transl. Res. 149:85-91(2007).
RN [38]
RP VARIANT HEP ASP-170, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP CHARACTERIZATION OF VARIANT HEP ASP-170.
RX PubMed=21668429; DOI=10.1111/j.1365-2133.2011.10453.x;
RA To-Figueras J., Phillips J., Gonzalez-Lopez J.M., Badenas C., Madrigal I.,
RA Gonzalez-Romaris E.M., Ramos C., Aguirre J.M., Herrero C.;
RT "Hepatoerythropoietic porphyria due to a novel mutation in the
RT uroporphyrinogen decarboxylase gene.";
RL Br. J. Dermatol. 165:499-505(2011).
CC -!- FUNCTION: Catalyzes the sequential decarboxylation of the four acetate
CC side chains of uroporphyrinogen to form coproporphyrinogen and
CC participates in the fifth step in the heme biosynthetic pathway
CC (PubMed:14633982, PubMed:11069625, PubMed:21668429, PubMed:11719352).
CC Isomer I or isomer III of uroporphyrinogen may serve as substrate, but
CC only coproporphyrinogen III can ultimately be converted to heme
CC (PubMed:14633982, PubMed:11069625, PubMed:21668429, PubMed:11719352).
CC In vitro also decarboxylates pentacarboxylate porphyrinogen I
CC (PubMed:12071824). {ECO:0000269|PubMed:11069625,
CC ECO:0000269|PubMed:11719352, ECO:0000269|PubMed:12071824,
CC ECO:0000269|PubMed:14633982, ECO:0000269|PubMed:21668429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen
CC III; Xref=Rhea:RHEA:19865, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57308, ChEBI:CHEBI:57309; EC=4.1.1.37;
CC Evidence={ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:14633982,
CC ECO:0000269|PubMed:21668429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19866;
CC Evidence={ECO:0000305|PubMed:11069625, ECO:0000305|PubMed:14633982,
CC ECO:0000305|PubMed:21668429};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 H(+) + uroporphyrinogen I = 4 CO2 + coproporphyrinogen I;
CC Xref=Rhea:RHEA:31239, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:62626, ChEBI:CHEBI:62631;
CC Evidence={ECO:0000269|PubMed:11719352, ECO:0000269|PubMed:14633982,
CC ECO:0000269|PubMed:21668429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31240;
CC Evidence={ECO:0000305|PubMed:11719352, ECO:0000305|PubMed:14633982,
CC ECO:0000305|PubMed:21668429};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC {ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:11719352,
CC ECO:0000269|PubMed:14633982, ECO:0000269|PubMed:21668429}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14633982,
CC ECO:0000269|PubMed:9194196, ECO:0000269|PubMed:9564029}.
CC -!- INTERACTION:
CC P06132; Q96KN1: LRATD2; NbExp=7; IntAct=EBI-2871776, EBI-9057780;
CC P06132; P46019: PHKA2; NbExp=3; IntAct=EBI-2871776, EBI-1642846;
CC P06132; C9JJ79: PILRA; NbExp=5; IntAct=EBI-2871776, EBI-12117156;
CC P06132; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-2871776, EBI-3918381;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISEASE: Familial porphyria cutanea tarda (FPCT) [MIM:176100]: A form
CC of porphyria. Porphyrias are inherited defects in the biosynthesis of
CC heme, resulting in the accumulation and increased excretion of
CC porphyrins or porphyrin precursors. They are classified as
CC erythropoietic or hepatic, depending on whether the enzyme deficiency
CC occurs in red blood cells or in the liver. Familial porphyria cutanea
CC tarda is an autosomal dominant disorder characterized by light-
CC sensitive dermatitis, with onset in later life. It is associated with
CC the excretion of large amounts of uroporphyrin in the urine. Iron
CC overload is often present in association with varying degrees of liver
CC damage. {ECO:0000269|PubMed:10338097, ECO:0000269|PubMed:10477430,
CC ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:11295834,
CC ECO:0000269|PubMed:11719352, ECO:0000269|PubMed:2243121,
CC ECO:0000269|PubMed:2920211, ECO:0000269|PubMed:7706766,
CC ECO:0000269|PubMed:8896428, ECO:0000269|PubMed:9792863}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Hepatoerythropoietic porphyria (HEP) [MIM:176100]: A form of
CC porphyria. Porphyrias are inherited defects in the biosynthesis of
CC heme, resulting in the accumulation and increased excretion of
CC porphyrins or porphyrin precursors. They are classified as
CC erythropoietic or hepatic, depending on whether the enzyme deficiency
CC occurs in red blood cells or in the liver. HEP is a cutaneous porphyria
CC that presents in infancy. It is characterized biochemically by
CC excessive excretion of acetate-substituted porphyrins and accumulation
CC of protoporphyrin in erythrocytes. Uroporphyrinogen decarboxylase
CC levels are very low in erythrocytes and cultured skin fibroblasts.
CC {ECO:0000269|PubMed:12071824, ECO:0000269|PubMed:15491440,
CC ECO:0000269|PubMed:1634232, ECO:0000269|PubMed:17240319,
CC ECO:0000269|PubMed:1905636, ECO:0000269|PubMed:21668429,
CC ECO:0000269|PubMed:3775362, ECO:0000269|PubMed:8176248,
CC ECO:0000269|PubMed:8644733, ECO:0000269|PubMed:8896428}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Uroporphyrinogen III decarboxylase
CC entry;
CC URL="https://en.wikipedia.org/wiki/Uroporphyrinogen_III_decarboxylase";
CC ---------------------------------------------------------------------------
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DR EMBL; M14016; AAA61258.1; -; mRNA.
DR EMBL; X89267; CAA61540.1; -; Genomic_DNA.
DR EMBL; AF047383; AAC03563.1; -; Genomic_DNA.
DR EMBL; AF104421; AAD04571.1; -; mRNA.
DR EMBL; AF104422; AAD04572.1; -; mRNA.
DR EMBL; AF104423; AAD04573.1; -; mRNA.
DR EMBL; AF104424; AAD04574.1; -; mRNA.
DR EMBL; AF104425; AAD04575.1; -; mRNA.
DR EMBL; AF104426; AAD04576.1; -; mRNA.
DR EMBL; AF104427; AAD04577.1; -; mRNA.
DR EMBL; AF104428; AAD04578.1; -; mRNA.
DR EMBL; AF104429; AAD04579.1; -; mRNA.
DR EMBL; AF104430; AAD04580.1; -; mRNA.
DR EMBL; AF104431; AAD04581.1; -; mRNA.
DR EMBL; AF104432; AAD04582.1; -; mRNA.
DR EMBL; AF104433; AAD04583.1; -; mRNA.
DR EMBL; AF104434; AAD04584.1; -; mRNA.
DR EMBL; AF104435; AAD04585.1; -; mRNA.
DR EMBL; AF104436; AAD04586.1; -; mRNA.
DR EMBL; AF104437; AAD04587.1; -; mRNA.
DR EMBL; AF104438; AAD04588.1; -; mRNA.
DR EMBL; AF104439; AAD04589.1; -; mRNA.
DR EMBL; AF104440; AAD04590.1; -; mRNA.
DR EMBL; AY292986; AAP44118.1; -; Genomic_DNA.
DR EMBL; BT006737; AAP35383.1; -; mRNA.
DR EMBL; CR456976; CAG33257.1; -; mRNA.
DR EMBL; CR542057; CAG46854.1; -; mRNA.
DR EMBL; AK291877; BAF84566.1; -; mRNA.
DR EMBL; AL359473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07007.1; -; Genomic_DNA.
DR EMBL; BC001778; AAH01778.1; -; mRNA.
DR EMBL; U30787; AAC50482.1; -; Genomic_DNA.
DR EMBL; M60891; AAB59456.1; -; Genomic_DNA.
DR CCDS; CCDS518.1; -.
DR PIR; A24411; A24411.
DR PIR; G02786; G02786.
DR RefSeq; NP_000365.3; NM_000374.4.
DR PDB; 1JPH; X-ray; 2.10 A; A=1-367.
DR PDB; 1JPI; X-ray; 2.30 A; A=1-367.
DR PDB; 1JPK; X-ray; 2.20 A; A=1-367.
DR PDB; 1R3Q; X-ray; 1.70 A; A=1-367.
DR PDB; 1R3R; X-ray; 1.85 A; A=1-367.
DR PDB; 1R3S; X-ray; 1.65 A; A=1-367.
DR PDB; 1R3T; X-ray; 1.70 A; A=1-367.
DR PDB; 1R3V; X-ray; 1.90 A; A=1-367.
DR PDB; 1R3W; X-ray; 1.70 A; A=1-367.
DR PDB; 1R3Y; X-ray; 1.75 A; A=1-367.
DR PDB; 1URO; X-ray; 1.80 A; A=1-367.
DR PDB; 2Q6Z; X-ray; 2.00 A; A=11-366.
DR PDB; 2Q71; X-ray; 1.90 A; A=11-366.
DR PDB; 3GVQ; X-ray; 2.10 A; A=1-367.
DR PDB; 3GVR; X-ray; 2.20 A; A=1-367.
DR PDB; 3GVV; X-ray; 2.80 A; A=1-367.
DR PDB; 3GVW; X-ray; 2.80 A; A=1-367.
DR PDB; 3GW0; X-ray; 2.00 A; A=1-367.
DR PDB; 3GW3; X-ray; 1.70 A; A=1-367.
DR PDBsum; 1JPH; -.
DR PDBsum; 1JPI; -.
DR PDBsum; 1JPK; -.
DR PDBsum; 1R3Q; -.
DR PDBsum; 1R3R; -.
DR PDBsum; 1R3S; -.
DR PDBsum; 1R3T; -.
DR PDBsum; 1R3V; -.
DR PDBsum; 1R3W; -.
DR PDBsum; 1R3Y; -.
DR PDBsum; 1URO; -.
DR PDBsum; 2Q6Z; -.
DR PDBsum; 2Q71; -.
DR PDBsum; 3GVQ; -.
DR PDBsum; 3GVR; -.
DR PDBsum; 3GVV; -.
DR PDBsum; 3GVW; -.
DR PDBsum; 3GW0; -.
DR PDBsum; 3GW3; -.
DR AlphaFoldDB; P06132; -.
DR SMR; P06132; -.
DR BioGRID; 113235; 34.
DR IntAct; P06132; 15.
DR MINT; P06132; -.
DR STRING; 9606.ENSP00000246337; -.
DR ChEMBL; CHEMBL1681619; -.
DR DrugBank; DB03727; Coproporphyrin I.
DR DrugBank; DB04461; Coproporphyrinogen III.
DR GlyGen; P06132; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P06132; -.
DR MetOSite; P06132; -.
DR PhosphoSitePlus; P06132; -.
DR BioMuta; UROD; -.
DR DMDM; 2507533; -.
DR OGP; P06132; -.
DR EPD; P06132; -.
DR jPOST; P06132; -.
DR MassIVE; P06132; -.
DR MaxQB; P06132; -.
DR PaxDb; P06132; -.
DR PeptideAtlas; P06132; -.
DR PRIDE; P06132; -.
DR ProteomicsDB; 51870; -.
DR TopDownProteomics; P06132; -.
DR Antibodypedia; 18538; 246 antibodies from 32 providers.
DR DNASU; 7389; -.
DR Ensembl; ENST00000246337.9; ENSP00000246337.4; ENSG00000126088.14.
DR GeneID; 7389; -.
DR KEGG; hsa:7389; -.
DR MANE-Select; ENST00000246337.9; ENSP00000246337.4; NM_000374.5; NP_000365.3.
DR UCSC; uc001cna.3; human.
DR CTD; 7389; -.
DR DisGeNET; 7389; -.
DR GeneCards; UROD; -.
DR GeneReviews; UROD; -.
DR HGNC; HGNC:12591; UROD.
DR HPA; ENSG00000126088; Low tissue specificity.
DR MalaCards; UROD; -.
DR MIM; 176100; phenotype.
DR MIM; 613521; gene.
DR neXtProt; NX_P06132; -.
DR OpenTargets; ENSG00000126088; -.
DR Orphanet; 443062; Familial porphyria cutanea tarda.
DR Orphanet; 95159; Hepatoerythropoietic porphyria.
DR PharmGKB; PA37221; -.
DR VEuPathDB; HostDB:ENSG00000126088; -.
DR eggNOG; KOG2872; Eukaryota.
DR GeneTree; ENSGT00390000018302; -.
DR HOGENOM; CLU_040933_0_0_1; -.
DR InParanoid; P06132; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1114675at2759; -.
DR PhylomeDB; P06132; -.
DR TreeFam; TF300744; -.
DR BioCyc; MetaCyc:HS04993-MON; -.
DR BRENDA; 4.1.1.37; 2681.
DR PathwayCommons; P06132; -.
DR Reactome; R-HSA-189451; Heme biosynthesis.
DR SignaLink; P06132; -.
DR UniPathway; UPA00251; UER00321.
DR BioGRID-ORCS; 7389; 516 hits in 1084 CRISPR screens.
DR ChiTaRS; UROD; human.
DR EvolutionaryTrace; P06132; -.
DR GeneWiki; Uroporphyrinogen_III_decarboxylase; -.
DR GenomeRNAi; 7389; -.
DR Pharos; P06132; Tbio.
DR PRO; PR:P06132; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P06132; protein.
DR Bgee; ENSG00000126088; Expressed in trabecular bone tissue and 204 other tissues.
DR ExpressionAtlas; P06132; baseline and differential.
DR Genevisible; P06132; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0006787; P:porphyrin-containing compound catabolic process; IDA:UniProtKB.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; IDA:UniProtKB.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00717; URO-D; 1.
DR DisProt; DP00308; -.
DR Gene3D; 3.20.20.210; -; 1.
DR HAMAP; MF_00218; URO_D; 1.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR InterPro; IPR006361; Uroporphyrinogen_deCO2ase_HemE.
DR InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR Pfam; PF01208; URO-D; 1.
DR SUPFAM; SSF51726; SSF51726; 1.
DR TIGRFAMs; TIGR01464; hemE; 1.
DR PROSITE; PS00906; UROD_1; 1.
DR PROSITE; PS00907; UROD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Decarboxylase;
KW Direct protein sequencing; Disease variant; Heme biosynthesis; Lyase;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..367
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187569"
FT BINDING 37..41
FT /ligand="substrate"
FT BINDING 55
FT /ligand="substrate"
FT BINDING 85
FT /ligand="substrate"
FT BINDING 86
FT /ligand="substrate"
FT BINDING 164
FT /ligand="substrate"
FT BINDING 219
FT /ligand="substrate"
FT BINDING 339
FT /ligand="substrate"
FT SITE 86
FT /note="Transition state stabilizer"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT VARIANT 15
FT /note="K -> E (in dbSNP:rs11541959)"
FT /id="VAR_060683"
FT VARIANT 25
FT /note="G -> E (in FPCT; insoluble protein;
FT dbSNP:rs764268015)"
FT /evidence="ECO:0000269|PubMed:11719352"
FT /id="VAR_022567"
FT VARIANT 46
FT /note="F -> L (in HEP; mild phenotype; strong decrease of
FT activity; dbSNP:rs769378741)"
FT /evidence="ECO:0000269|PubMed:12071824,
FT ECO:0000269|PubMed:15491440"
FT /id="VAR_022568"
FT VARIANT 62
FT /note="P -> L (in HEP; dbSNP:rs121918060)"
FT /evidence="ECO:0000269|PubMed:8644733"
FT /id="VAR_009103"
FT VARIANT 77
FT /note="P -> L (in dbSNP:rs1131147)"
FT /evidence="ECO:0000269|PubMed:8644733, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5"
FT /id="VAR_067457"
FT VARIANT 80
FT /note="A -> G (in HEP; dbSNP:rs776907084)"
FT /evidence="ECO:0000269|PubMed:8896428"
FT /id="VAR_007910"
FT VARIANT 80
FT /note="A -> S (in FPCT; decrease of activity;
FT dbSNP:rs376921379)"
FT /evidence="ECO:0000269|PubMed:11069625,
FT ECO:0000269|PubMed:11719352"
FT /id="VAR_022569"
FT VARIANT 106
FT /note="P -> L (in dbSNP:rs11541962)"
FT /id="VAR_060684"
FT VARIANT 113
FT /note="R -> T (in dbSNP:rs11541963)"
FT /id="VAR_060685"
FT VARIANT 134
FT /note="V -> Q (in FPCT and HEP; requires 2 nucleotide
FT substitutions; nearly normal activity)"
FT /evidence="ECO:0000269|PubMed:10338097,
FT ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:11719352,
FT ECO:0000269|PubMed:8176248"
FT /id="VAR_009104"
FT VARIANT 142
FT /note="R -> Q (in FPCT; dbSNP:rs1182234844)"
FT /evidence="ECO:0000269|PubMed:11295834"
FT /id="VAR_010985"
FT VARIANT 144
FT /note="R -> P (in FPCT; decrease of activity)"
FT /evidence="ECO:0000269|PubMed:11069625"
FT /id="VAR_022570"
FT VARIANT 156
FT /note="G -> D (in FPCT; decrease of activity;
FT dbSNP:rs762617943)"
FT /evidence="ECO:0000269|PubMed:11719352"
FT /id="VAR_022571"
FT VARIANT 161
FT /note="L -> Q (in FPCT)"
FT /evidence="ECO:0000269|PubMed:11295834"
FT /id="VAR_010986"
FT VARIANT 165
FT /note="M -> R (in FPCT; activity < 2%; dbSNP:rs121918063)"
FT /evidence="ECO:0000269|PubMed:11719352,
FT ECO:0000269|PubMed:9792863"
FT /id="VAR_007911"
FT VARIANT 167
FT /note="E -> K (in HEP and FPCT; nearly normal activity;
FT dbSNP:rs121918058)"
FT /evidence="ECO:0000269|PubMed:11719352,
FT ECO:0000269|PubMed:1905636"
FT /id="VAR_007714"
FT VARIANT 168
FT /note="G -> R (in HEP; relative activity of 65% of wild-
FT type towards uroporphyrinogen III)"
FT /evidence="ECO:0000269|PubMed:17240319"
FT /id="VAR_065558"
FT VARIANT 170
FT /note="G -> D (in HEP; relative activity of 17% and 60% of
FT wild-type towards uroporphyrinogen I and III respectively)"
FT /evidence="ECO:0000269|PubMed:21668429"
FT /id="VAR_065559"
FT VARIANT 193
FT /note="R -> P (in FPCT; insoluble protein;
FT dbSNP:rs143823335)"
FT /evidence="ECO:0000269|PubMed:11719352"
FT /id="VAR_022572"
FT VARIANT 195
FT /note="L -> F (in FPCT; dbSNP:rs121918064)"
FT /evidence="ECO:0000269|PubMed:9792863"
FT /id="VAR_007912"
FT VARIANT 216
FT /note="L -> Q (in FPCT)"
FT /evidence="ECO:0000269|PubMed:11069625"
FT /id="VAR_022573"
FT VARIANT 218
FT /note="E -> K (in FPCT; significant decrease of activity)"
FT /evidence="ECO:0000269|PubMed:11069625"
FT /id="VAR_022574"
FT VARIANT 219
FT /note="S -> F (in FPCT; dbSNP:rs982293378)"
FT /evidence="ECO:0000269|PubMed:11295834"
FT /id="VAR_010987"
FT VARIANT 220
FT /note="H -> P (in HEP; mild form)"
FT /evidence="ECO:0000269|PubMed:8176248"
FT /id="VAR_009105"
FT VARIANT 229
FT /note="F -> L (in FPCT)"
FT /evidence="ECO:0000269|PubMed:10477430"
FT /id="VAR_009106"
FT VARIANT 232
FT /note="F -> L (in FPCT; decrease of activity)"
FT /evidence="ECO:0000269|PubMed:11719352"
FT /id="VAR_022575"
FT VARIANT 235
FT /note="P -> S (in FPCT; dbSNP:rs141312224)"
FT /evidence="ECO:0000269|PubMed:11295834"
FT /id="VAR_010988"
FT VARIANT 253
FT /note="L -> Q (in FPCT; decrease of activity;
FT dbSNP:rs36033115)"
FT /evidence="ECO:0000269|PubMed:11719352,
FT ECO:0000269|PubMed:8896428"
FT /id="VAR_007913"
FT VARIANT 260
FT /note="I -> T (in FPCT; decrease of activity;
FT dbSNP:rs1483459837)"
FT /evidence="ECO:0000269|PubMed:11719352"
FT /id="VAR_022576"
FT VARIANT 281
FT /note="G -> E (in FPCT and HEP; dbSNP:rs121918057)"
FT /evidence="ECO:0000269|PubMed:3775362,
FT ECO:0000269|PubMed:7706766, ECO:0000269|PubMed:8644733"
FT /id="VAR_007715"
FT VARIANT 281
FT /note="G -> V (in FPCT; dbSNP:rs121918057)"
FT /evidence="ECO:0000269|PubMed:11069625,
FT ECO:0000269|PubMed:2920211"
FT /id="VAR_007716"
FT VARIANT 282
FT /note="L -> R (in FPCT)"
FT /evidence="ECO:0000269|PubMed:11069625"
FT /id="VAR_022577"
FT VARIANT 292
FT /note="R -> G (in HEP; dbSNP:rs121918059)"
FT /evidence="ECO:0000269|PubMed:1634232"
FT /id="VAR_007717"
FT VARIANT 303
FT /note="G -> S (in FPCT; dbSNP:rs964670864)"
FT /evidence="ECO:0000269|PubMed:11069625"
FT /id="VAR_022578"
FT VARIANT 303
FT /note="G -> V (in dbSNP:rs17849533)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6"
FT /id="VAR_060686"
FT VARIANT 304
FT /note="N -> K (in FPCT; dbSNP:rs121918065)"
FT /evidence="ECO:0000269|PubMed:9792863"
FT /id="VAR_007914"
FT VARIANT 311
FT /note="Y -> C (in HEP; dbSNP:rs121918061)"
FT /evidence="ECO:0000269|PubMed:8644733"
FT /id="VAR_009107"
FT VARIANT 318
FT /note="G -> R (in FPCT; dbSNP:rs116233118)"
FT /evidence="ECO:0000269|PubMed:11069625,
FT ECO:0000269|PubMed:8896428"
FT /id="VAR_007915"
FT VARIANT 324
FT /note="M -> T (in FPCT; dbSNP:rs763746230)"
FT /evidence="ECO:0000269|PubMed:10477430"
FT /id="VAR_009108"
FT VARIANT 332
FT /note="R -> H (in FPCT; dbSNP:rs121918066)"
FT /evidence="ECO:0000269|PubMed:9792863"
FT /id="VAR_007916"
FT VARIANT 334
FT /note="I -> T (in FPCT)"
FT /evidence="ECO:0000269|PubMed:8896428"
FT /id="VAR_007917"
FT MUTAGEN 86
FT /note="D->E: 5-10% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:14633982"
FT MUTAGEN 86
FT /note="D->G: Very low activity. Binds substrate with
FT similar geometry as wild-type."
FT /evidence="ECO:0000269|PubMed:14633982"
FT MUTAGEN 86
FT /note="D->N: No activity. Unable to bind substrate."
FT /evidence="ECO:0000269|PubMed:14633982"
FT MUTAGEN 164
FT /note="Y->F: 25-30% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:14633982"
FT CONFLICT 103
FT /note="G -> S (in Ref. 1; AAA61258 and 14; AAB59456)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="R -> A (in Ref. 1; AAA61258 and 14; AAB59456)"
FT /evidence="ECO:0000305"
FT CONFLICT 212..214
FT /note="Missing (in Ref. 14; AAB59456)"
FT /evidence="ECO:0000305"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:1R3S"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:1R3S"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1R3S"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1R3S"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:1R3S"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 185..208
FT /evidence="ECO:0007829|PDB:1R3S"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 234..250
FT /evidence="ECO:0007829|PDB:1R3S"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:1R3S"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:3GVV"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:1R3S"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 314..328
FT /evidence="ECO:0007829|PDB:1R3S"
FT STRAND 330..339
FT /evidence="ECO:0007829|PDB:1R3S"
FT HELIX 347..365
FT /evidence="ECO:0007829|PDB:1R3S"
SQ SEQUENCE 367 AA; 40787 MW; 840510B36CFC3856 CRC64;
MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR
SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER
LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW
LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV
AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT
LQGNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH
SRLLRQN
