COX5A_RAT
ID COX5A_RAT Reviewed; 146 AA.
AC P11240;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cytochrome c oxidase subunit 5A, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide Va;
DE Flags: Precursor;
GN Name=Cox5a;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=2544858; DOI=10.1093/nar/17.11.4375;
RA Droste M., Schon E., Kadenbach B.;
RT "Nucleotide sequence of cDNA encoding subunit Va from rat heart cytochrome
RT c oxidase.";
RL Nucleic Acids Res. 17:4375-4375(1989).
RN [2]
RP PROTEIN SEQUENCE OF 38-47.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7601105; DOI=10.1111/j.1432-1033.1995.tb20556.x;
RA Schaegger H., Noack H., Halangk W., Brandt U., von Jagow G.;
RT "Cytochrome-c oxidase in developing rat heart. Enzymic properties and
RT amino-terminal sequences suggest identity of the fetal heart and the adult
RT liver isoform.";
RL Eur. J. Biochem. 230:235-241(1995).
RN [3]
RP PROTEIN SEQUENCE OF 94-103, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RC STRAIN=Holtzman; TISSUE=Sperm;
RX PubMed=20966424; DOI=10.2164/jandrol.110.010967;
RA Suryawanshi A.R., Khan S.A., Gajbhiye R.K., Gurav M.Y., Khole V.V.;
RT "Differential proteomics leads to identification of domain specific
RT epididymal sperm proteins.";
RL J. Androl. 32:240-259(2011).
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00427}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P00427}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A,
CC COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC are encoded in the nuclear genome. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (By similarity).
CC Interacts with AFG1L (By similarity). Interacts with RAB5IF (By
CC similarity). {ECO:0000250|UniProtKB:P00426,
CC ECO:0000250|UniProtKB:P20674}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00426}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00426}; Matrix side
CC {ECO:0000250|UniProtKB:P00426}.
CC -!- TISSUE SPECIFICITY: Expressed in the head of epididymal sperm but not
CC in testicular sperm (at protein level). {ECO:0000269|PubMed:20966424}.
CC -!- MASS SPECTROMETRY: Mass=12420; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20966424};
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5A family.
CC {ECO:0000305}.
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DR EMBL; X15030; CAA33134.1; -; mRNA.
DR PIR; S04592; S04592.
DR RefSeq; NP_665726.1; NM_145783.1.
DR AlphaFoldDB; P11240; -.
DR SMR; P11240; -.
DR BioGRID; 251679; 1.
DR CORUM; P11240; -.
DR IntAct; P11240; 2.
DR MINT; P11240; -.
DR STRING; 10116.ENSRNOP00000025525; -.
DR iPTMnet; P11240; -.
DR PhosphoSitePlus; P11240; -.
DR UCD-2DPAGE; P11240; -.
DR jPOST; P11240; -.
DR PaxDb; P11240; -.
DR PRIDE; P11240; -.
DR GeneID; 252934; -.
DR KEGG; rno:252934; -.
DR UCSC; RGD:620607; rat.
DR CTD; 9377; -.
DR RGD; 620607; Cox5a.
DR VEuPathDB; HostDB:ENSRNOG00000018816; -.
DR eggNOG; KOG4077; Eukaryota.
DR HOGENOM; CLU_099086_1_1_1; -.
DR InParanoid; P11240; -.
DR OMA; DPHHEES; -.
DR OrthoDB; 1286549at2759; -.
DR PhylomeDB; P11240; -.
DR TreeFam; TF105062; -.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR UniPathway; UPA00705; -.
DR PRO; PR:P11240; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000018816; Expressed in heart and 19 other tissues.
DR Genevisible; P11240; RN.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd00923; Cyt_c_Oxidase_Va; 1.
DR Gene3D; 1.25.40.40; -; 1.
DR InterPro; IPR003204; Cyt_c_oxidase_su5A/6.
DR InterPro; IPR036545; Cyt_c_oxidase_su5A/6_sf.
DR PANTHER; PTHR14200; PTHR14200; 1.
DR Pfam; PF02284; COX5A; 1.
DR SUPFAM; SSF48479; SSF48479; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7601105"
FT CHAIN 38..146
FT /note="Cytochrome c oxidase subunit 5A, mitochondrial"
FT /id="PRO_0000006102"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12787"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12787"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20674"
SQ SEQUENCE 146 AA; 16130 MW; 8F6AE081BDD6010F CRC64;
MLAAALRRCT AAAAARGLLH PVSAPSPAAA VCSIRCYSHG SHETDEEFDA RWVTYFNKPD
IDAWELRKGM NTLVGYDLVP EPKIIDAALR ACRRLNDFAS AVRILEVVKD KAGPHKEIYP
YVIQELRPTL NELGISTPEE LGLDKV
