DCUP_MOUSE
ID DCUP_MOUSE Reviewed; 367 AA.
AC P70697; Q91VW4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000305};
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37 {ECO:0000250|UniProtKB:P06132};
GN Name=Urod {ECO:0000312|MGI:MGI:98916};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C57BL/6 X CBA;
RX PubMed=8661721; DOI=10.1007/s003359900101;
RA Wu C., Xu W., Kozak C.A., Desnick R.J.;
RT "Mouse uroporphyrinogen decarboxylase: cDNA cloning, expression, and
RT mapping.";
RL Mamm. Genome 7:349-352(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND CATALYTIC ACTIVITY.
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP PROTEIN SEQUENCE OF 51-74; 105-116; 121-142; 232-238; 251-263 AND 298-359,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Isomer
CC I or isomer III of uroporphyrinogen may serve as substrate, but only
CC coproporphyrinogen III can ultimately be converted to heme (By
CC similarity). In vitro also decarboxylates pentacarboxylate
CC porphyrinogen I (PubMed:8661721). {ECO:0000250|UniProtKB:P06132,
CC ECO:0000269|PubMed:8661721}.
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:0000250|UniProtKB:P06132};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19866;
CC Evidence={ECO:0000250|UniProtKB:P06132};
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:0000250|UniProtKB:P06132};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31240;
CC Evidence={ECO:0000250|UniProtKB:P06132};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC {ECO:0000250|UniProtKB:P06132}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U34691; AAB18294.1; -; mRNA.
DR EMBL; AK172426; BAE43002.1; -; mRNA.
DR EMBL; AL671671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008109; AAH08109.1; -; mRNA.
DR CCDS; CCDS18521.1; -.
DR PIR; T10088; T10088.
DR RefSeq; NP_033504.2; NM_009478.4.
DR AlphaFoldDB; P70697; -.
DR SMR; P70697; -.
DR BioGRID; 204461; 4.
DR IntAct; P70697; 1.
DR STRING; 10090.ENSMUSP00000030446; -.
DR iPTMnet; P70697; -.
DR PhosphoSitePlus; P70697; -.
DR SwissPalm; P70697; -.
DR EPD; P70697; -.
DR jPOST; P70697; -.
DR MaxQB; P70697; -.
DR PaxDb; P70697; -.
DR PeptideAtlas; P70697; -.
DR PRIDE; P70697; -.
DR ProteomicsDB; 279607; -.
DR Antibodypedia; 18538; 246 antibodies from 32 providers.
DR DNASU; 22275; -.
DR Ensembl; ENSMUST00000030446; ENSMUSP00000030446; ENSMUSG00000028684.
DR GeneID; 22275; -.
DR KEGG; mmu:22275; -.
DR UCSC; uc008uhr.1; mouse.
DR CTD; 7389; -.
DR MGI; MGI:98916; Urod.
DR VEuPathDB; HostDB:ENSMUSG00000028684; -.
DR eggNOG; KOG2872; Eukaryota.
DR GeneTree; ENSGT00390000018302; -.
DR HOGENOM; CLU_040933_0_0_1; -.
DR InParanoid; P70697; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1114675at2759; -.
DR PhylomeDB; P70697; -.
DR TreeFam; TF300744; -.
DR BioCyc; MetaCyc:MON-14921; -.
DR Reactome; R-MMU-189451; Heme biosynthesis.
DR UniPathway; UPA00251; UER00321.
DR BioGRID-ORCS; 22275; 27 hits in 73 CRISPR screens.
DR ChiTaRS; Urod; mouse.
DR PRO; PR:P70697; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P70697; protein.
DR Bgee; ENSMUSG00000028684; Expressed in fetal liver hematopoietic progenitor cell and 268 other tissues.
DR ExpressionAtlas; P70697; baseline and differential.
DR Genevisible; P70697; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008198; F:ferrous iron binding; ISO:MGI.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IDA:MGI.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:MGI.
DR GO; GO:0042168; P:heme metabolic process; IMP:MGI.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISO:MGI.
DR GO; GO:0006787; P:porphyrin-containing compound catabolic process; ISS:UniProtKB.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; ISO:MGI.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046502; P:uroporphyrinogen III metabolic process; ISO:MGI.
DR CDD; cd00717; URO-D; 1.
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 Acetylation; Cytoplasm; Decarboxylase; Direct protein sequencing;
KW Heme biosynthesis; Lyase; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..367
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187570"
FT BINDING 37..41
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 86
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P06132"
FT CONFLICT 96
FT /note="M -> I (in Ref. 1; AAB18294)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="Y -> S (in Ref. 1; AAB18294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40692 MW; EDDFD66C3BFA2D84 CRC64;
MEANGFGLQN FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR
SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREERDLER
LRDPAAAASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGS SSTMAQAKRW
LYQRPQASHK LLGILTDVLV PYLIGQVAAG AQALQLFESH AGHLGTELFS KFALPYIRDV
AKRVKAGLQK AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARERVGKAVT
LQGNLDPCAL YASEEEIGRL VQQMLDDFGP QRYIANLGHG LYPDMDPERV GAFVDAVHKH
SRLLRQN
