Coproporphyrinogen-III oxidase, mitochondrial precursor

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P36552 (HEM6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III By similarity.
Catalytic activity	Coproporphyrinogen-III + O₂ + 2 H⁺ = protoporphyrinogen-IX + 2 CO₂ + 2 H₂O.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion intermembrane space.
Tissue specificity	Erythroid cells and non erythroid cells such as liver.
Post-translational modification	Acetylation of Lys-360 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	Belongs to the aerobic coproporphyrinogen-III oxidase family.
Sequence caution	The sequence AAH17680.2 differs from that shown. Reason: Erroneous initiation. The sequence BAA03840.1 differs from that shown. Reason: Frameshift at positions 22, 43 and 76.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	coproporphyrinogen oxidase activity Inferred from direct assay Ref.1. Source: MGI protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 98

Mitochondrion Ref.5

Chain

99 – 443

345

Coproporphyrinogen-III oxidase, mitochondrial

PRO_0000006030

Regions

Region

182 – 191

Important for dimerization By similarity

Region

249 – 251

Substrate binding By similarity

Region

381 – 417

Important for dimerization By similarity

Region

400 – 405

Substrate binding By similarity

Sites

Active site

247

Proton donor By similarity

Binding site

233

Substrate By similarity

Site

316

Important for dimerization By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.7

Modified residue

360

N6-acetyllysine Ref.6

Experimental info

Sequence conflict

R → P in BAA03840. Ref.1

Sequence conflict

101

S → T AA sequence Ref.5

Sequence conflict

116 – 117

CS → SD AA sequence Ref.5

Sequence conflict

122

S → T AA sequence Ref.5

Sequence conflict

124

V → P AA sequence Ref.5

Sequence conflict

138

K → N in BAC79229. Ref.3

Sequence conflict

275

T → R in BAA03840. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P36552 [UniParc].

Last modified June 21, 2004. Version 2.
Checksum: 9F3D5E8E420645F0
Show »

FASTA

443

49,715

        10         20         30         40         50         60 
MALRLGRLGS DPWWRAVLGD YAQLRAASPR CASARVCQLP GTAGPQPRRG LGYGPWARGG 

        70         80         90        100        110        120 
SGLGTRLAAT LAGLAGLAAA AFGHVQRAEM VPKSSGARSP SPGRREEDGD ELARRCSTFM 

       130        140        150        160        170        180 
SSPVTELREL RRRPEDMKTK MELMIMETQA QVCRALAQVD GVADFTVDRW ERKEGGGGIT 

       190        200        210        220        230        240 
CVLQDGRVFE KAGVSISVVH GNLSEEAANQ MRGRGKTLKT KDSKLPFTAM GVSSVIHPKN 

       250        260        270        280        290        300 
PYAPTMHFNY RYFEVEEADG NTHWWFGGGC DLTPTYLNQE DAVHFHRTLK EACDQHGPDI 

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

       370        380        390        400        410        420 
HCDDSYTPRD KLWQQLRRGR YVEFNLLYDR GTKFGLFTPG SRIESILMSL PLTARWEYMH 

       430        440 
SPPENSKEAE ILEVLRHPKD WVH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation." Kohno H., Furukawa T., Yoshinaga T., Tokunaga R., Taketani S. J. Biol. Chem. 268:21359-21363(1993) [PubMed: 8407975] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[3]	"Examination of mitochondrial protein targeting of haem synthetic enzymes: in vivo identification of three functional haem-responsive motifs in 5-aminolaevulinate synthase." Dailey T.A., Woodruff J.H., Dailey H.A. Biochem. J. 386:381-386(2005) [PubMed: 15482256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139.
[4]	"The long, but not the short, presequence of human coproporphyrinogen oxidase is essential for its import and sorting to mitochondria." Susa S., Daimon M., Ono H., Li S., Yoshida T., Kato T. Tohoku J. Exp. Med. 200:39-45(2003) [PubMed: 12862310] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144.
[5]	"Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase." Martasek P., Camadro J.-M., Delfau-Larue M.H., Dumas J.B., Montagne J.J., de Verneuil H., Labbe P., Grandchamp B. Proc. Natl. Acad. Sci. U.S.A. 91:3024-3028(1994) [PubMed: 8159699] [Abstract] Cited for: PROTEIN SEQUENCE OF 99-125 AND 248-258.
[6]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-360, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D16333 mRNA. Translation: BAA03840.1. Frameshift. BC017680 mRNA. Translation: AAH17680.2. Different initiation. AY382578 Genomic DNA. Translation: AAQ88103.1. AB099924 Genomic DNA. Translation: BAC79229.1.
IPI	IPI00400301.
PIR	A48049.
RefSeq	NP_031783.2. NM_007757.2.
UniGene	Mm.291519.
3D structure databases
ProteinModelPortal	P36552.
SMR	P36552. Positions 110-442.
ModBase	Search...
Protein-protein interaction databases
STRING	P36552.
PTM databases
PhosphoSite	P36552.
Proteomic databases
PRIDE	P36552.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000060077; ENSMUSP00000055455; ENSMUSG00000022742.
GeneID	12892.
KEGG	mmu:12892.
NMPDR	fig\|10090.3.peg.31449.
UCSC	uc007zoa.2. mouse.
Organism-specific databases
CTD	1371.
MGI	MGI:104841. Cpox.
Phylogenomic databases
eggNOG	roNOG06556.
HOGENOM	HBG631180.
HOVERGEN	HBG051897.
InParanoid	P36552.
OMA	VFKPWCD.
OrthoDB	EOG41VK2W.
PhylomeDB	P36552.
Gene expression databases
ArrayExpress	P36552.
Bgee	P36552.
CleanEx	MM_CPOX.
Genevestigator	P36552.
GermOnline	ENSMUSG00000022742. Mus musculus.
Family and domain databases
InterPro	IPR001260. Coprogen_oxidase_aer. IPR018375. Coprogen_oxidase_CS. [Graphical view]
Gene3D	G3DSA:3.40.1500.10. Coprogen_oxidas. 1 hit.
KO	K00228.
PANTHER	PTHR10755. Coprogen_oxidas. 1 hit.
Pfam	PF01218. Coprogen_oxidas. 1 hit. [Graphical view]
PRINTS	PR00073. COPRGNOXDASE.
SUPFAM	SSF102886. Coprogen_oxidas. 1 hit.
PROSITE	PS01021. COPROGEN_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	282498.
SOURCE	Search...

Entry information

Entry name

HEM6_MOUSE

Accession

Primary (citable) accession number: P36552
Secondary accession number(s): Q7TQ36, Q8VD08

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 21, 2004
Last modified:	November 16, 2011
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents