LOCUS NP_000365 367 aa linear PRI 04-OCT-2024
DEFINITION uroporphyrinogen decarboxylase [Homo sapiens].
ACCESSION NP_000365
VERSION NP_000365.3
DBSOURCE REFSEQ: accession NM_000374.5
KEYWORDS RefSeq; MANE Select.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 367)
AUTHORS Cunha,L., Kuti,M., Bishop,D.F., Mezei,M., Zeng,L., Zhou,M.M. and
Desnick,R.J.
TITLE Human uroporphyrinogen III synthase: NMR-based mapping of the
active site
JOURNAL Proteins 71 (2), 855-873 (2008)
PUBMED 18004775
REFERENCE 2 (residues 1 to 367)
AUTHORS Whitby,F.G., Phillips,J.D., Kushner,J.P. and Hill,C.P.
TITLE Crystal structure of human uroporphyrinogen decarboxylase
JOURNAL EMBO J 17 (9), 2463-2471 (1998)
PUBMED 9564029
REFERENCE 3 (residues 1 to 367)
AUTHORS Rudnick,S., Phillips,J. and Bonkovsky,H.
CONSRTM Porphyrias Consortium of the Rare Diseases Clinical Research
Network
TITLE Hepatoerythropoietic Porphyria
JOURNAL (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
Amemiya A (Eds.);
GENEREVIEWS(R);
(1993)
PUBMED 24175354
REFERENCE 4 (residues 1 to 367)
AUTHORS Rudnick,S., Phillips,J. and Bonkovsky,H.
CONSRTM Porphyrias Consortium of the Rare Diseases Clinical Research
Network
TITLE Familial Porphyria Cutanea Tarda
JOURNAL (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
Amemiya A (Eds.);
GENEREVIEWS(R);
(1993)
PUBMED 23741761
REFERENCE 5 (residues 1 to 367)
AUTHORS de Verneuil,H., Bourgeois,F., de Rooij,F., Siersema,P.D.,
Wilson,J.H., Grandchamp,B. and Nordmann,Y.
TITLE Characterization of a new mutation (R292G) and a deletion at the
human uroporphyrinogen decarboxylase locus in two patients with
hepatoerythropoietic porphyria
JOURNAL Hum Genet 89 (5), 548-552 (1992)
PUBMED 1634232
REFERENCE 6 (residues 1 to 367)
AUTHORS Garey,J.R., Hansen,J.L., Harrison,L.M., Kennedy,J.B. and
Kushner,J.P.
TITLE A point mutation in the coding region of uroporphyrinogen
decarboxylase associated with familial porphyria cutanea tarda
JOURNAL Blood 73 (4), 892-895 (1989)
PUBMED 2920211
REFERENCE 7 (residues 1 to 367)
AUTHORS Romana,M., Dubart,A., Beaupain,D., Chabret,C., Goossens,M. and
Romeo,P.H.
TITLE Structure of the gene for human uroporphyrinogen decarboxylase
JOURNAL Nucleic Acids Res 15 (18), 7343-7356 (1987)
PUBMED 3658695
REFERENCE 8 (residues 1 to 367)
AUTHORS Romeo,P.H., Raich,N., Dubart,A., Beaupain,D., Pryor,M., Kushner,J.,
Cohen-Solal,M. and Goossens,M.
TITLE Molecular cloning and nucleotide sequence of a complete human
uroporphyrinogen decarboxylase cDNA
JOURNAL J Biol Chem 261 (21), 9825-9831 (1986)
PUBMED 3015909
REFERENCE 9 (residues 1 to 367)
AUTHORS Dubart,A., Mattei,M.G., Raich,N., Beaupain,D., Romeo,P.H.,
Mattei,J.F. and Goossens,M.
TITLE Assignment of human uroporphyrinogen decarboxylase (URO-D) to the
p34 band of chromosome 1
JOURNAL Hum Genet 73 (3), 277-279 (1986)
PUBMED 3460962
REFERENCE 10 (residues 1 to 367)
AUTHORS Elder,G.H., Lee,G.B. and Tovey,J.A.
TITLE Decreased activity of hepatic uroporphyrinogen decarboxylase in
sporadic porphyria cutanea tarda
JOURNAL N Engl J Med 299 (6), 274-278 (1978)
PUBMED 661926
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AK291877.1 and AL359473.22.
This sequence is a reference standard in the RefSeqGene project.
On Jul 21, 2005 this sequence version replaced NP_000365.2.
Summary: This gene encodes an enzyme in the heme biosynthetic
pathway. This enzyme is responsible for catalyzing the conversion
of uroporphyrinogen to coproporphyrinogen through the removal of
four carboxymethyl side chains. Mutations and deficiency in this
enzyme are known to cause familial porphyria cutanea tarda and
hepatoerythropoetic porphyria.[provided by RefSeq, Aug 2010].
Transcript Variant: This variant (1) represents the shortest
transcript and encodes the functional protein.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: SRR5189655.6910.1,
SRR5189658.54891.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA1965299, SAMEA1966682
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000246337.9/ ENSP00000246337.4
RefSeq Select criteria :: based on conservation, expression,
longest protein
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..367
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="1"
/map="1p34.1"
Protein 1..367
/product="uroporphyrinogen decarboxylase"
/EC_number="4.1.1.37"
/note="uroporphyrinogen III decarboxylase"
/calculated_mol_wt=40656
Site 1
/site_type="acetylation"
/note="N-acetylmethionine.
/evidence=ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
propagated from UniProtKB/Swiss-Prot (P06132.2)"
Region 20..359
/region_name="URO-D"
/note="Uroporphyrinogen decarboxylase (URO-D) is a dimeric
cytosolic enzyme that decarboxylates the four acetate side
chains of uroporphyrinogen III (uro-III) to create
coproporphyrinogen III, without requiring any prosthetic
groups or cofactors. This reaction...; cd00717"
/db_xref="CDD:238368"
Site order(36..41,46,50,55,82..88,100,105,154,164,170,217,
219..220,261,339)
/site_type="other"
/note="substrate binding site [chemical binding]"
/db_xref="CDD:238368"
Site order(37,41,86,164,219,339)
/site_type="active"
/db_xref="CDD:238368"
Site 86
/site_type="other"
/note="Transition state stabilizer; propagated from
UniProtKB/Swiss-Prot (P06132.2)"
CDS 1..367
/gene="UROD"
/gene_synonym="PCT; UPD"
/coded_by="NM_000374.5:13..1116"
/db_xref="CCDS:CCDS518.1"
/db_xref="GeneID:7389"
/db_xref="HGNC:HGNC:12591"
/db_xref="MIM:613521"
ORIGIN
1 meanglgpqg fpelkndtfl raawgeetdy tpvwcmrqag rylpefretr aaqdffstcr
61 speacceltl qplrrfplda aiifsdilvv pqalgmevtm vpgkgpsfpe plreeqdler
121 lrdpevvase lgyvfqaitl trqrlagrvp ligfagapwt lmtymveggg sstmaqakrw
181 lyqrpqashq llriltdalv pylvgqvvag aqalqlfesh aghlgpqlfn kfalpyirdv
241 akqvkarlre aglapvpmii fakdghfale elaqagyevv gldwtvapkk arecvgktvt
301 lqgnldpcal yaseeeigql vkqmlddfgp hryianlghg lypdmdpehv gafvdavhkh
361 srllrqn
//