HEM6_RAT
ID HEM6_RAT Reviewed; 443 AA.
AC Q3B7D0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial;
DE Short=COX;
DE Short=Coprogen oxidase;
DE Short=Coproporphyrinogenase;
DE EC=1.3.3.3 {ECO:0000269|PubMed:666752};
DE Flags: Precursor;
GN Name=Cpox {ECO:0000312|EMBL:AAI07665.1}; Synonyms=Cpo;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAI07665.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate {ECO:0000312|EMBL:AAI07665.1};
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 [2] {ECO:0000305}
RP ENZYME ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=666752; DOI=10.1042/bj1720345;
RA Elder G.H., Evans J.O.;
RT "Evidence that the coproporphyrinogen oxidase activity of rat liver is
RT situated in the intermembrane space of mitochondria.";
RL Biochem. J. 172:345-347(1978).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic
CC oxidative decarboxylation of propionate groups of rings A and B of
CC coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-
CC IX (By similarity). {ECO:0000250|UniProtKB:P36551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O +
CC protoporphyrinogen IX; Xref=Rhea:RHEA:18257, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57307, ChEBI:CHEBI:57309; EC=1.3.3.3;
CC Evidence={ECO:0000269|PubMed:666752};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18258;
CC Evidence={ECO:0000305|PubMed:666752};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2
CC route): step 1/1. {ECO:0000269|PubMed:666752}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:666752}.
CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000305}.
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DR EMBL; BC107664; AAI07665.1; -; mRNA.
DR RefSeq; NP_001032172.1; NM_001037095.1.
DR AlphaFoldDB; Q3B7D0; -.
DR SMR; Q3B7D0; -.
DR IntAct; Q3B7D0; 2.
DR STRING; 10116.ENSRNOP00000002257; -.
DR iPTMnet; Q3B7D0; -.
DR PhosphoSitePlus; Q3B7D0; -.
DR jPOST; Q3B7D0; -.
DR PaxDb; Q3B7D0; -.
DR PRIDE; Q3B7D0; -.
DR GeneID; 304024; -.
DR KEGG; rno:304024; -.
DR UCSC; RGD:1311817; rat.
DR CTD; 1371; -.
DR RGD; 1311817; Cpox.
DR VEuPathDB; HostDB:ENSRNOG00000001654; -.
DR eggNOG; KOG1518; Eukaryota.
DR HOGENOM; CLU_026169_1_1_1; -.
DR InParanoid; Q3B7D0; -.
DR OMA; HDKGTLF; -.
DR OrthoDB; 1080991at2759; -.
DR PhylomeDB; Q3B7D0; -.
DR TreeFam; TF300703; -.
DR Reactome; R-RNO-189451; Heme biosynthesis.
DR UniPathway; UPA00251; UER00322.
DR PRO; PR:Q3B7D0; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001654; Expressed in stomach and 19 other tissues.
DR Genevisible; Q3B7D0; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; ISO:RGD.
DR GO; GO:0006783; P:heme biosynthetic process; IDA:RGD.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IDA:RGD.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0017085; P:response to insecticide; IEP:RGD.
DR GO; GO:0010039; P:response to iron ion; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0051597; P:response to methylmercury; IEP:RGD.
DR Gene3D; 3.40.1500.10; -; 1.
DR InterPro; IPR001260; Coprogen_oxidase_aer.
DR InterPro; IPR036406; Coprogen_oxidase_aer_sf.
DR InterPro; IPR018375; Coprogen_oxidase_CS.
DR PANTHER; PTHR10755; PTHR10755; 1.
DR Pfam; PF01218; Coprogen_oxidas; 1.
DR PRINTS; PR00073; COPRGNOXDASE.
DR SUPFAM; SSF102886; SSF102886; 1.
DR PROSITE; PS01021; COPROGEN_OXIDASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Heme biosynthesis; Mitochondrion; Oxidoreductase;
KW Phosphoprotein; Porphyrin biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..98
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P36552"
FT CHAIN 99..443
FT /note="Oxygen-dependent coproporphyrinogen-III oxidase,
FT mitochondrial"
FT /id="PRO_0000293624"
FT REGION 90..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..191
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT REGION 381..417
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT ACT_SITE 247
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249..251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 400..405
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 316
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 393
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P36552"
FT MOD_RES 393
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P36552"
SQ SEQUENCE 443 AA; 49278 MW; C599A521060628A4 CRC64;
MALRLGQLGS GPWWRAVRGD YAQLRAPSPR SASACVCRLP GTAGTQPRRG LGHGSSAGGG
SRLGTGLAAA LAGMAGLAAA VLGHVQRAEM VPKSSGARSP SPGRLEEDGD ELARRCSTFM
SSPVTELREL GRRPDDMKTK MELMIMETQA QVCRALAQVD GVADFSVDRW ERKEGGGGIT
CVLQDGRVFE KAGVNISVVH GNLSEEAANQ MRSRGKALKK KDGKLPFTAM GISSVIHPKN
PYAPTMHFNY RYFEVEEADG KMHWWFGGGC DLTPTYLNRE DAVHFHRTLK EACDQHGPDI
YPKFKKWCDD YFFIAHRGER RGIGGIFFDD LDSPSKEEAF RFVKTCAEAV VPSYVPIVKK
HCDDSYTPQD KLWQQLRRGR YVEFNLVYDR GTKFGLFTPG SRIESILMSL PLTARWEYMH
SPPENSKEAE ILEVLRHPKD WVH
