COX5A_BOVIN
ID COX5A_BOVIN Reviewed; 152 AA.
AC P00426; Q32LF6; Q6QRN2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cytochrome c oxidase subunit 5A, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide Va;
DE Flags: Precursor;
GN Name=COX5A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shin M.L., Cui X.S., Park S.Y., Kim E.Y., Park S.P., Lee W.J., Hwang K.C.,
RA Kim N.H.;
RT "Analysis of gene expression in the bovine blastocyst or hatched blastocyst
RT in vitro using ACP method.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 44-152.
RC TISSUE=Heart;
RX PubMed=220224; DOI=10.1016/s0021-9258(18)50669-4;
RA Tanaka M., Haniu M., Yasunobu K.T., Yu C.-A., Yu L., Wei Y.-H., King T.E.;
RT "Amino acid sequence of subunit V of bovine heart cytochrome oxidase, the
RT heme alpha-containing subunit.";
RL J. Biol. Chem. 254:3879-3885(1979).
RN [4]
RP PROTEIN SEQUENCE OF 44-77.
RC TISSUE=Liver;
RX PubMed=2844245; DOI=10.1021/bi00413a048;
RA Yanamura W., Zhang Y.-Z., Takamiya S., Capaldi R.A.;
RT "Tissue-specific differences between heart and liver cytochrome c
RT oxidase.";
RL Biochemistry 27:4909-4914(1988).
RN [5]
RP SUBUNIT.
RX PubMed=26698328; DOI=10.1074/jbc.m115.680553;
RA Shinzawa-Itoh K., Shimomura H., Yanagisawa S., Shimada S., Takahashi R.,
RA Oosaki M., Ogura T., Tsukihara T.;
RT "Purification of active respiratory supercomplex from bovine heart
RT mitochondria enables functional studies.";
RL J. Biol. Chem. 291:4178-4184(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-152.
RX PubMed=8638158; DOI=10.1126/science.272.5265.1136;
RA Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H.,
RA Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8
RT A.";
RL Science 272:1136-1144(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-152.
RC TISSUE=Heart;
RX PubMed=10089392; DOI=10.1107/s0907444998006362;
RA Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T.,
RA Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT "Structure analysis of bovine heart cytochrome c oxidase at 2.8 A
RT resolution.";
RL Acta Crystallogr. D 55:31-45(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 44-152.
RC TISSUE=Heart;
RX PubMed=10771420; DOI=10.1107/s0907444900002213;
RA Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T.,
RA Shinzawa-Itoh K., Nakashima R., Yoshikawa S.;
RT "X-ray structure of azide-bound fully oxidized cytochrome c oxidase from
RT bovine heart at 2.9 A resolution.";
RL Acta Crystallogr. D 56:529-535(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RX PubMed=20385840; DOI=10.1073/pnas.0910410107;
RA Muramoto K., Ohta K., Shinzawa-Itoh K., Kanda K., Taniguchi M.,
RA Nabekura H., Yamashita E., Tsukihara T., Yoshikawa S.;
RT "Bovine cytochrome c oxidase structures enable O2 reduction with
RT minimization of reactive oxygens and provide a proton-pumping gate.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7740-7745(2010).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS).
RX PubMed=27830641; DOI=10.7554/elife.21290;
RA Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT "Functional asymmetry and electron flow in the bovine respirasome.";
RL Elife 5:0-0(2016).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RX PubMed=27605664; DOI=10.1074/jbc.m115.711770;
RA Yano N., Muramoto K., Shimada A., Takemura S., Baba J., Fujisawa H.,
RA Mochizuki M., Shinzawa-Itoh K., Yamashita E., Tsukihara T., Yoshikawa S.;
RT "The Mg2+-containing water cluster of mammalian cytochrome c oxidase
RT collects four pumping proton equivalents in each catalytic cycle.";
RL J. Biol. Chem. 291:23882-23894(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=31533957; DOI=10.1073/pnas.1907183116;
RA Shinzawa-Itoh K., Sugimura T., Misaki T., Tadehara Y., Yamamoto S.,
RA Hanada M., Yano N., Nakagawa T., Uene S., Yamada T., Aoyama H.,
RA Yamashita E., Tsukihara T., Yoshikawa S., Muramoto K.;
RT "Monomeric structure of an active form of bovine cytochrome c oxidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:19945-19951(2019).
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 COX4I1 (or
CC COX4I2), COX5A, COX5B, COX6A2 (or COX6A1), COX6B1 (or COX6B2), COX6C,
CC COX7A1 (or COX7A2), COX7B, COX7C, COX8B and NDUFA4, which are encoded
CC in the nuclear genome (PubMed:8638158). The complex exists as a monomer
CC or a 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)) (PubMed:26698328,
CC PubMed:27830641). Interacts with AFG1L (By similarity). Interacts with
CC RAB5IF (By similarity). {ECO:0000250|UniProtKB:P20674,
CC ECO:0000269|PubMed:26698328, ECO:0000269|PubMed:27830641,
CC ECO:0000269|PubMed:8638158}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Peripheral
CC membrane protein {ECO:0000269|PubMed:27605664,
CC ECO:0000269|PubMed:31533957}; Matrix side {ECO:0000269|PubMed:27605664,
CC ECO:0000269|PubMed:31533957}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5A family.
CC {ECO:0000305}.
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DR EMBL; AY528254; AAS20602.1; -; mRNA.
DR EMBL; BC109608; AAI09609.1; -; mRNA.
DR PIR; A00493; CABO.
DR RefSeq; NP_001002891.1; NM_001002891.1.
DR RefSeq; XP_005221971.1; XM_005221914.2.
DR PDB; 1OCC; X-ray; 2.80 A; E/R=44-152.
DR PDB; 1OCO; X-ray; 2.80 A; E/R=44-152.
DR PDB; 1OCR; X-ray; 2.35 A; E/R=44-152.
DR PDB; 1OCZ; X-ray; 2.90 A; E/R=44-152.
DR PDB; 1V54; X-ray; 1.80 A; E/R=44-152.
DR PDB; 1V55; X-ray; 1.90 A; E/R=44-152.
DR PDB; 2DYR; X-ray; 1.80 A; E/R=44-152.
DR PDB; 2DYS; X-ray; 2.20 A; E/R=44-152.
DR PDB; 2EIJ; X-ray; 1.90 A; E/R=44-152.
DR PDB; 2EIK; X-ray; 2.10 A; E/R=44-152.
DR PDB; 2EIL; X-ray; 2.10 A; E/R=44-152.
DR PDB; 2EIM; X-ray; 2.60 A; E/R=44-152.
DR PDB; 2EIN; X-ray; 2.70 A; E/R=44-152.
DR PDB; 2OCC; X-ray; 2.30 A; E/R=44-152.
DR PDB; 2Y69; X-ray; 1.95 A; E/R=1-152.
DR PDB; 2YBB; EM; 19.00 A; P=44-152.
DR PDB; 2ZXW; X-ray; 2.50 A; E/R=44-152.
DR PDB; 3ABK; X-ray; 2.00 A; E/R=44-152.
DR PDB; 3ABL; X-ray; 2.10 A; E/R=44-152.
DR PDB; 3ABM; X-ray; 1.95 A; E/R=44-152.
DR PDB; 3AG1; X-ray; 2.20 A; E/R=44-152.
DR PDB; 3AG2; X-ray; 1.80 A; E/R=44-152.
DR PDB; 3AG3; X-ray; 1.80 A; E/R=44-152.
DR PDB; 3AG4; X-ray; 2.05 A; E/R=44-152.
DR PDB; 3ASN; X-ray; 3.00 A; E/R=44-152.
DR PDB; 3ASO; X-ray; 2.30 A; E/R=44-152.
DR PDB; 3WG7; X-ray; 1.90 A; E/R=44-152.
DR PDB; 3X2Q; X-ray; 2.00 A; E/R=44-152.
DR PDB; 5B1A; X-ray; 1.50 A; E/R=44-152.
DR PDB; 5B1B; X-ray; 1.60 A; E/R=44-152.
DR PDB; 5B3S; X-ray; 1.68 A; E/R=44-152.
DR PDB; 5GPN; EM; 5.40 A; 2=44-152.
DR PDB; 5IY5; X-ray; 2.00 A; E/R=48-152.
DR PDB; 5LUF; EM; 9.10 A; 2=44-152.
DR PDB; 5W97; X-ray; 2.30 A; E/e=44-152.
DR PDB; 5WAU; X-ray; 1.95 A; E/e=44-152.
DR PDB; 5X19; X-ray; 2.20 A; E/R=44-152.
DR PDB; 5X1B; X-ray; 2.40 A; E/R=44-152.
DR PDB; 5X1F; X-ray; 2.20 A; E/R=44-152.
DR PDB; 5XDQ; X-ray; 1.77 A; E/R=44-152.
DR PDB; 5XDX; X-ray; 1.99 A; E/R=44-152.
DR PDB; 5XTH; EM; 3.90 A; 1=44-152.
DR PDB; 5XTI; EM; 17.40 A; 1/B1=44-152.
DR PDB; 5Z84; X-ray; 1.85 A; E/R=44-152.
DR PDB; 5Z85; X-ray; 1.85 A; E/R=44-152.
DR PDB; 5Z86; X-ray; 1.85 A; E/R=44-152.
DR PDB; 5ZCO; X-ray; 1.90 A; E/R=44-152.
DR PDB; 5ZCP; X-ray; 1.65 A; E/R=44-152.
DR PDB; 5ZCQ; X-ray; 1.65 A; E/R=44-152.
DR PDB; 6J8M; X-ray; 1.90 A; E/R=44-152.
DR PDB; 6JUW; X-ray; 1.80 A; E/R=48-152.
DR PDB; 6JY3; X-ray; 1.85 A; E=44-152.
DR PDB; 6JY4; X-ray; 1.95 A; E=44-152.
DR PDB; 6NKN; X-ray; 2.50 A; E/R=44-152.
DR PDB; 6NMF; X-ray; 2.80 A; E/R=44-152.
DR PDB; 6NMP; X-ray; 2.90 A; E/R=44-152.
DR PDB; 7COH; X-ray; 1.30 A; E/R=44-152.
DR PDB; 7CP5; X-ray; 1.76 A; E/R=48-152.
DR PDB; 7D5W; X-ray; 1.84 A; E/R=48-152.
DR PDB; 7D5X; X-ray; 1.74 A; E/R=48-152.
DR PDB; 7EV7; X-ray; 1.70 A; E/R=44-152.
DR PDB; 7THU; X-ray; 1.93 A; EEE/RRR=44-152.
DR PDB; 7TIE; X-ray; 1.90 A; EEE/RRR=44-152.
DR PDB; 7TIH; X-ray; 2.35 A; EEE/RRR=44-152.
DR PDB; 7TII; X-ray; 2.45 A; EEE/RRR=44-152.
DR PDBsum; 1OCC; -.
DR PDBsum; 1OCO; -.
DR PDBsum; 1OCR; -.
DR PDBsum; 1OCZ; -.
DR PDBsum; 1V54; -.
DR PDBsum; 1V55; -.
DR PDBsum; 2DYR; -.
DR PDBsum; 2DYS; -.
DR PDBsum; 2EIJ; -.
DR PDBsum; 2EIK; -.
DR PDBsum; 2EIL; -.
DR PDBsum; 2EIM; -.
DR PDBsum; 2EIN; -.
DR PDBsum; 2OCC; -.
DR PDBsum; 2Y69; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 2ZXW; -.
DR PDBsum; 3ABK; -.
DR PDBsum; 3ABL; -.
DR PDBsum; 3ABM; -.
DR PDBsum; 3AG1; -.
DR PDBsum; 3AG2; -.
DR PDBsum; 3AG3; -.
DR PDBsum; 3AG4; -.
DR PDBsum; 3ASN; -.
DR PDBsum; 3ASO; -.
DR PDBsum; 3WG7; -.
DR PDBsum; 3X2Q; -.
DR PDBsum; 5B1A; -.
DR PDBsum; 5B1B; -.
DR PDBsum; 5B3S; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5IY5; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5W97; -.
DR PDBsum; 5WAU; -.
DR PDBsum; 5X19; -.
DR PDBsum; 5X1B; -.
DR PDBsum; 5X1F; -.
DR PDBsum; 5XDQ; -.
DR PDBsum; 5XDX; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR PDBsum; 5Z84; -.
DR PDBsum; 5Z85; -.
DR PDBsum; 5Z86; -.
DR PDBsum; 5ZCO; -.
DR PDBsum; 5ZCP; -.
DR PDBsum; 5ZCQ; -.
DR PDBsum; 6J8M; -.
DR PDBsum; 6JUW; -.
DR PDBsum; 6JY3; -.
DR PDBsum; 6JY4; -.
DR PDBsum; 6NKN; -.
DR PDBsum; 6NMF; -.
DR PDBsum; 6NMP; -.
DR PDBsum; 7COH; -.
DR PDBsum; 7CP5; -.
DR PDBsum; 7D5W; -.
DR PDBsum; 7D5X; -.
DR PDBsum; 7EV7; -.
DR PDBsum; 7THU; -.
DR PDBsum; 7TIE; -.
DR PDBsum; 7TIH; -.
DR PDBsum; 7TII; -.
DR AlphaFoldDB; P00426; -.
DR SMR; P00426; -.
DR CORUM; P00426; -.
DR DIP; DIP-38982N; -.
DR IntAct; P00426; 3.
DR STRING; 9913.ENSBTAP00000022949; -.
DR iPTMnet; P00426; -.
DR UCD-2DPAGE; P00426; -.
DR PaxDb; P00426; -.
DR PeptideAtlas; P00426; -.
DR PRIDE; P00426; -.
DR Ensembl; ENSBTAT00000022949; ENSBTAP00000022949; ENSBTAG00000017267.
DR GeneID; 444878; -.
DR KEGG; bta:444878; -.
DR CTD; 9377; -.
DR VEuPathDB; HostDB:ENSBTAG00000017267; -.
DR VGNC; VGNC:27636; COX5A.
DR eggNOG; KOG4077; Eukaryota.
DR GeneTree; ENSGT00390000001424; -.
DR HOGENOM; CLU_099086_1_1_1; -.
DR InParanoid; P00426; -.
DR OMA; DPHHEES; -.
DR OrthoDB; 1286549at2759; -.
DR TreeFam; TF105062; -.
DR BRENDA; 7.1.1.9; 908.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-9707564; Cytoprotection by HMOX1.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; P00426; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000017267; Expressed in corpus luteum and 105 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; ISS:AgBase.
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 3D-structure; Acetylation; Direct protein sequencing; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:220224,
FT ECO:0000269|PubMed:2844245"
FT CHAIN 44..152
FT /note="Cytochrome c oxidase subunit 5A, mitochondrial"
FT /id="PRO_0000006099"
FT MOD_RES 89
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12787"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12787"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20674"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 144..150
FT /evidence="ECO:0007829|PDB:7COH"
SQ SEQUENCE 152 AA; 16735 MW; CE8FA765A8ABBA02 CRC64;
MLGAAVRRCS VAAAAVARAS PRGLLHPTPA PGQAAAVQSL RCYSHGSHET DEEFDARWVT
YFNKPDIDAW ELRKGMNTLV GYDLVPEPKI IDAALRACRR LNDFASAVRI LEVVKDKAGP
HKEIYPYVIQ ELRPTLNELG ISTPEELGLD KV
