CPLM-006652

Genbank Nucleotide ID

Coproporphyrinogen-III oxidase, mitochondrial

Protein Synonyms/Alias

COX; Coprogen oxidase; Coproporphyrinogenase

Mus musculus (Mouse)

Position	Peptide	Type	References
303	HGPDIYPKFKKWCDD	acetylation	[1]
344	EEAFRFVKTCAEAVV	acetylation	[2]
360	SYVPIVKKHCDDSYT	acetylation	[2, 3]
371	DSYTPRDKLWQQLRR	acetylation	[1, 4, 5]
371	DSYTPRDKLWQQLRR	succinylation	[4]
393	LLYDRGTKFGLFTPG	acetylation	[1, 2, 4, 5, 6]
393	LLYDRGTKFGLFTPG	succinylation	[4]

[1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[3] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[6] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]

Functional Description

Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III (By similarity).

REGION 182 191 Important for dimerization (By
REGION 249 251 Substrate binding (By similarity).
REGION 381 417 Important for dimerization (By
REGION 400 405 Substrate binding (By similarity).
ACT_SITE 247 247 Proton donor (By similarity).
BINDING 233 233 Substrate (By similarity).
MOD_RES 99 99 Phosphoserine.
MOD_RES 360 360 N6-acetyllysine.

Acetylation; Complete proteome; Direct protein sequencing; Heme biosynthesis; Mitochondrion; Oxidoreductase; Phosphoprotein; Porphyrin biosynthesis; Reference proteome; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IDA:MGI.
GO:0004109; F:coproporphyrinogen oxidase activity; IDA:MGI.
GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO:0006783; P:heme biosynthetic process; IDA:MGI.
GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
GO:0046685; P:response to arsenic-containing substance; IEA:Compara.
GO:0017085; P:response to insecticide; IEA:Compara.
GO:0010039; P:response to iron ion; IEA:Compara.
GO:0010288; P:response to lead ion; IEA:Compara.
GO:0051597; P:response to methylmercury; IEA:Compara.

IPR001260; Coprogen_oxidase_aer.
IPR018375; Coprogen_oxidase_CS.

PF01218; Coprogen_oxidas

PS01021; COPROGEN_OXIDASE

PR00073; COPRGNOXDASE.