COX5A_CAEEL
ID COX5A_CAEEL Reviewed; 174 AA.
AC P55954; Q9XWV8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cytochrome c oxidase subunit 5A, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide Va;
DE Flags: Precursor;
GN Name=cox-5A {ECO:0000312|WormBase:Y37D8A.14};
GN Synonyms=cco-2 {ECO:0000312|WormBase:Y37D8A.14};
GN ORFNames=Y37D8A.14 {ECO:0000312|WormBase:Y37D8A.14};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP PROTEIN SEQUENCE OF 30-41.
RC STRAIN=Bristol N2;
RX PubMed=9150941; DOI=10.1002/elps.1150180337;
RA Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R.;
RT "Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates
RT and identification of protein spots by microsequencing.";
RL Electrophoresis 18:557-562(1997).
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 a catalytic core of 3 subunits and
CC several supernumerary subunits. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00427}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00427}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00427}; Matrix side
CC {ECO:0000250|UniProtKB:P00427}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5A family.
CC {ECO:0000305}.
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DR EMBL; BX284603; CAA21532.1; -; Genomic_DNA.
DR PIR; T26631; T26631.
DR RefSeq; NP_499681.1; NM_067280.5.
DR AlphaFoldDB; P55954; -.
DR SMR; P55954; -.
DR BioGRID; 41880; 47.
DR DIP; DIP-27022N; -.
DR STRING; 6239.Y37D8A.14; -.
DR EPD; P55954; -.
DR PaxDb; P55954; -.
DR PeptideAtlas; P55954; -.
DR EnsemblMetazoa; Y37D8A.14.1; Y37D8A.14.1; WBGene00012553.
DR GeneID; 176707; -.
DR KEGG; cel:CELE_Y37D8A.14; -.
DR UCSC; Y37D8A.14.1; c. elegans.
DR CTD; 176707; -.
DR WormBase; Y37D8A.14; CE20218; WBGene00012553; cox-5A.
DR eggNOG; KOG4077; Eukaryota.
DR GeneTree; ENSGT00390000001424; -.
DR HOGENOM; CLU_099086_1_0_1; -.
DR InParanoid; P55954; -.
DR OMA; DKHFIDY; -.
DR OrthoDB; 1286549at2759; -.
DR PhylomeDB; P55954; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:P55954; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012553; Expressed in larva and 4 other tissues.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IMP:WormBase.
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 Direct protein sequencing; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:9150941"
FT CHAIN 30..174
FT /note="Cytochrome c oxidase subunit 5A, mitochondrial"
FT /id="PRO_0000006103"
FT CONFLICT 30
FT /note="G -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 20111 MW; DAB897567143BF1C CRC64;
MASLTRAVTR LAIAGRQAVR TIATTTPVSG HGDDIMEKWP ADKFDNHFIN YLNRPEIDGW
EVRKALSELH DYDVIPDPKV VEAALRACRR VNDFALAVRF LEAIKIKCGA QKNRDTVYAY
IVKQVEPVLK ELGIDTPEQL GYGEPEFFVP EPEYWWEKKW YKDYGYDKHP NIQI
