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Q3B7D0 (HEM6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Short name=COX
Short name=Coprogen oxidase
Short name=Coproporphyrinogenase
EC=1.3.3.3
Gene names
Name:Cpox
Synonyms:Cpo
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX By similarity.

Catalytic activity

Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O. Ref.2

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1. Ref.2

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion intermembrane space Ref.2.

Sequence similarities

Belongs to the aerobic coproporphyrinogen-III oxidase family.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processheme biosynthetic process

Inferred from direct assay PubMed 3955059. Source: RGD

protoporphyrinogen IX biosynthetic process

Inferred from direct assay PubMed 3814086. Source: RGD

response to arsenic-containing substance

Inferred from expression pattern PubMed 2916235. Source: RGD

response to inorganic substance

Inferred from expression pattern PubMed 2289051. Source: RGD

response to insecticide

Inferred from expression pattern PubMed 6626236. Source: RGD

response to iron ion

Inferred from expression pattern PubMed 2289051. Source: RGD

response to lead ion

Inferred from expression pattern PubMed 656697. Source: RGD

response to methylmercury

Inferred from expression pattern PubMed 2916235. Source: RGD

   Cellular_componentmitochondrial inner membrane

Inferred from direct assay PubMed 31872. Source: RGD

mitochondrial intermembrane space

Inferred from direct assay PubMed 31872. Source: RGD

mitochondrion

Inferred from direct assay PubMed 3996415. Source: RGD

   Molecular_functioncoproporphyrinogen oxidase activity

Inferred from direct assay PubMed 11079369. Source: RGD

identical protein binding

Inferred from direct assay PubMed 11079369. Source: RGD

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

structural constituent of eye lens

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 9898Mitochondrion By similarity UniProtKB P36552
Chain99 – 443345Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial UniProtKB P36552
PRO_0000293624

Regions

Region182 – 19110Important for dimerization By similarity
Region249 – 2513Substrate binding By similarity
Region381 – 41737Important for dimerization By similarity
Region400 – 4056Substrate binding By similarity

Sites

Active site2471Proton donor By similarity
Binding site2331Substrate By similarity
Site3161Important for dimerization By similarity

Amino acid modifications

Modified residue3931N6-acetyllysine; alternate By similarity
Modified residue3931N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3B7D0 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: C599A521060628A4

FASTA44349,278
        10         20         30         40         50         60 
MALRLGQLGS GPWWRAVRGD YAQLRAPSPR SASACVCRLP GTAGTQPRRG LGHGSSAGGG 

        70         80         90        100        110        120 
SRLGTGLAAA LAGMAGLAAA VLGHVQRAEM VPKSSGARSP SPGRLEEDGD ELARRCSTFM 

       130        140        150        160        170        180 
SSPVTELREL GRRPDDMKTK MELMIMETQA QVCRALAQVD GVADFSVDRW ERKEGGGGIT 

       190        200        210        220        230        240 
CVLQDGRVFE KAGVNISVVH GNLSEEAANQ MRSRGKALKK KDGKLPFTAM GISSVIHPKN 

       250        260        270        280        290        300 
PYAPTMHFNY RYFEVEEADG KMHWWFGGGC DLTPTYLNRE DAVHFHRTLK EACDQHGPDI 

       310        320        330        340        350        360 
YPKFKKWCDD YFFIAHRGER RGIGGIFFDD LDSPSKEEAF RFVKTCAEAV VPSYVPIVKK 

       370        380        390        400        410        420 
HCDDSYTPQD KLWQQLRRGR YVEFNLVYDR GTKFGLFTPG SRIESILMSL PLTARWEYMH 

       430        440 
SPPENSKEAE ILEVLRHPKD WVH 

« Hide

References

« Hide 'large scale' references
[1]"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].
Tissue: Prostate.
[2]"Evidence that the coproporphyrinogen oxidase activity of rat liver is situated in the intermembrane space of mitochondria."
Elder G.H., Evans J.O.
Biochem. J. 172:345-347(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, PATHWAY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC107664 mRNA. Translation: AAI07665.1.
RefSeqNP_001032172.1. NM_001037095.1.
UniGeneRn.19581.

3D structure databases

ProteinModelPortalQ3B7D0.
SMRQ3B7D0. Positions 110-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000002257.

PTM databases

PhosphoSiteQ3B7D0.

Proteomic databases

PaxDbQ3B7D0.
PRIDEQ3B7D0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000002257; ENSRNOP00000002257; ENSRNOG00000001654.
GeneID304024.
KEGGrno:304024.
UCSCRGD:1311817. rat.

Organism-specific databases

CTD1371.
RGD1311817. Cpox.

Phylogenomic databases

eggNOGCOG0408.
GeneTreeENSGT00390000017311.
HOGENOMHOG000262768.
HOVERGENHBG051897.
InParanoidQ3B7D0.
KOK00228.
OMARYFETAN.
OrthoDBEOG7BZVSG.
PhylomeDBQ3B7D0.
TreeFamTF300703.

Enzyme and pathway databases

UniPathwayUPA00251; UER00322.

Gene expression databases

GenevestigatorQ3B7D0.

Family and domain databases

Gene3D3.40.1500.10. 1 hit.
InterProIPR001260. Coprogen_oxidase_aer.
IPR018375. Coprogen_oxidase_CS.
[Graphical view]
PANTHERPTHR10755. PTHR10755. 1 hit.
PfamPF01218. Coprogen_oxidas. 1 hit.
[Graphical view]
PRINTSPR00073. COPRGNOXDASE.
SUPFAMSSF102886. SSF102886. 1 hit.
PROSITEPS01021. COPROGEN_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio652479.
PROQ3B7D0.

Entry information

Entry nameHEM6_RAT
AccessionPrimary (citable) accession number: Q3B7D0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: November 22, 2005
Last modified: May 14, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways