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Protein

Uroporphyrinogen decarboxylase

Gene

Urod

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.By similarity

Catalytic activityi

Uroporphyrinogen III = coproporphyrinogen + 4 CO2.

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (Alad)
  2. Porphobilinogen deaminase (Hmbs)
  3. Uroporphyrinogen-III synthase (Uros)
  4. Uroporphyrinogen decarboxylase (Urod)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551SubstrateBy similarity
Binding sitei85 – 851SubstrateBy similarity
Binding sitei86 – 861SubstrateBy similarity
Sitei86 – 861Transition state stabilizerBy similarity
Binding sitei164 – 1641SubstrateBy similarity
Binding sitei219 – 2191SubstrateBy similarity
Binding sitei339 – 3391SubstrateBy similarity

GO - Molecular functioni

  • ferrous iron binding Source: Ensembl
  • uroporphyrinogen decarboxylase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14921.
ReactomeiR-MMU-189451. Heme biosynthesis.
UniPathwayiUPA00251; UER00321.

Names & Taxonomyi

Protein namesi
Recommended name:
Uroporphyrinogen decarboxylase (EC:4.1.1.37)
Short name:
UPD
Short name:
URO-D
Gene namesi
Name:Urod
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:98916. Urod.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Uroporphyrinogen decarboxylasePRO_0000187570Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP70697.
MaxQBiP70697.
PaxDbiP70697.
PeptideAtlasiP70697.
PRIDEiP70697.

PTM databases

iPTMnetiP70697.
PhosphoSiteiP70697.

Expressioni

Gene expression databases

BgeeiP70697.
CleanExiMM_UROD.
ExpressionAtlasiP70697. baseline and differential.
GenevisibleiP70697. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiP70697. 2 interactions.
MINTiMINT-4092930.
STRINGi10090.ENSMUSP00000030446.

Structurei

3D structure databases

ProteinModelPortaliP70697.
SMRiP70697. Positions 11-366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 415Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2872. Eukaryota.
COG0407. LUCA.
GeneTreeiENSGT00390000018302.
HOGENOMiHOG000253896.
HOVERGENiHBG000229.
InParanoidiP70697.
KOiK01599.
OMAiLGHGMHP.
OrthoDBiEOG7FNC85.
PhylomeDBiP70697.
TreeFamiTF300744.

Family and domain databases

HAMAPiMF_00218. URO_D.
InterProiIPR006361. Uroporphyrinogen_deCO2ase_HemE.
IPR000257. Uroporphyrinogen_deCOase.
[Graphical view]
PfamiPF01208. URO-D. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01464. hemE. 1 hit.
PROSITEiPS00906. UROD_1. 1 hit.
PS00907. UROD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P70697-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEANGFGLQN FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR
60 70 80 90 100
AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM
110 120 130 140 150
VPGKGPSFPE PLREERDLER LRDPAAAASE LGYVFQAITL TRQRLAGRVP
160 170 180 190 200
LIGFAGAPWT LMTYMVEGGS SSTMAQAKRW LYQRPQASHK LLGILTDVLV
210 220 230 240 250
PYLIGQVAAG AQALQLFESH AGHLGTELFS KFALPYIRDV AKRVKAGLQK
260 270 280 290 300
AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARERVGKAVT
310 320 330 340 350
LQGNLDPCAL YASEEEIGRL VQQMLDDFGP QRYIANLGHG LYPDMDPERV
360
GAFVDAVHKH SRLLRQN
Length:367
Mass (Da):40,692
Last modified:March 6, 2007 - v2
Checksum:iEDDFD66C3BFA2D84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961M → I in AAB18294 (PubMed:8661721).Curated
Sequence conflicti333 – 3331Y → S in AAB18294 (PubMed:8661721).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34691 mRNA. Translation: AAB18294.1.
AK172426 mRNA. Translation: BAE43002.1.
AL671671 Genomic DNA. Translation: CAM23809.1.
BC008109 mRNA. Translation: AAH08109.1.
CCDSiCCDS18521.1.
PIRiT10088.
RefSeqiNP_033504.2. NM_009478.4.
UniGeneiMm.46484.

Genome annotation databases

EnsembliENSMUST00000030446; ENSMUSP00000030446; ENSMUSG00000028684.
GeneIDi22275.
KEGGimmu:22275.
UCSCiuc008uhr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34691 mRNA. Translation: AAB18294.1.
AK172426 mRNA. Translation: BAE43002.1.
AL671671 Genomic DNA. Translation: CAM23809.1.
BC008109 mRNA. Translation: AAH08109.1.
CCDSiCCDS18521.1.
PIRiT10088.
RefSeqiNP_033504.2. NM_009478.4.
UniGeneiMm.46484.

3D structure databases

ProteinModelPortaliP70697.
SMRiP70697. Positions 11-366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP70697. 2 interactions.
MINTiMINT-4092930.
STRINGi10090.ENSMUSP00000030446.

PTM databases

iPTMnetiP70697.
PhosphoSiteiP70697.

Proteomic databases

EPDiP70697.
MaxQBiP70697.
PaxDbiP70697.
PeptideAtlasiP70697.
PRIDEiP70697.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030446; ENSMUSP00000030446; ENSMUSG00000028684.
GeneIDi22275.
KEGGimmu:22275.
UCSCiuc008uhr.1. mouse.

Organism-specific databases

CTDi7389.
MGIiMGI:98916. Urod.

Phylogenomic databases

eggNOGiKOG2872. Eukaryota.
COG0407. LUCA.
GeneTreeiENSGT00390000018302.
HOGENOMiHOG000253896.
HOVERGENiHBG000229.
InParanoidiP70697.
KOiK01599.
OMAiLGHGMHP.
OrthoDBiEOG7FNC85.
PhylomeDBiP70697.
TreeFamiTF300744.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00321.
BioCyciMetaCyc:MONOMER-14921.
ReactomeiR-MMU-189451. Heme biosynthesis.

Miscellaneous databases

ChiTaRSiUrod. mouse.
PROiP70697.
SOURCEiSearch...

Gene expression databases

BgeeiP70697.
CleanExiMM_UROD.
ExpressionAtlasiP70697. baseline and differential.
GenevisibleiP70697. MM.

Family and domain databases

HAMAPiMF_00218. URO_D.
InterProiIPR006361. Uroporphyrinogen_deCO2ase_HemE.
IPR000257. Uroporphyrinogen_deCOase.
[Graphical view]
PfamiPF01208. URO-D. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01464. hemE. 1 hit.
PROSITEiPS00906. UROD_1. 1 hit.
PS00907. UROD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse uroporphyrinogen decarboxylase: cDNA cloning, expression, and mapping."
    Wu C., Xu W., Kozak C.A., Desnick R.J.
    Mamm. Genome 7:349-352(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Spleen.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 51-74; 105-116; 121-142; 232-238; 251-263 AND 298-359, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiDCUP_MOUSE
AccessioniPrimary (citable) accession number: P70697
Secondary accession number(s): Q91VW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 6, 2007
Last modified: July 6, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.