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uroporphyrinogen decarboxylase [Homo sapiens]

NCBI Reference Sequence: NP_000365.3

Identical Proteins FASTA Graphics 

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
//
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