ID   COX7B_BOVIN             Reviewed;          80 AA.
AC   P13183; Q3SZ39;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 3.
DT   04-NOV-2026, entry version 178.
DE   RecName: Full=Cytochrome c oxidase subunit 7B, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide VIIb;
DE   AltName: Full=IHQ;
DE   Flags: Precursor;
GN   Name=COX7B;
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].
RX   PubMed=2550462; DOI=10.1016/s0021-9258(19)84785-3;
RA   Lightowlers R.N., Takamiya S., Wessling R., Lindorfer M., Capaldi R.A.;
RT   "Cloning and sequencing of the cDNA for a 13th different subunit (IHQ) of
RT   beef heart cytochrome c oxidase.";
RL   J. Biol. Chem. 264:16858-16861(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 25-46.
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   [4]
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   [5]
RP   X-RAY CRYSTALLOGRAPHY.
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   [6]
RP   X-RAY CRYSTALLOGRAPHY.
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   [7]
RP   X-RAY CRYSTALLOGRAPHY.
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   [8]
RP   X-RAY CRYSTALLOGRAPHY.
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   [9]
RP   STRUCTURE BY ELECTRON MICROSCOPY.
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   [10]
RP   X-RAY CRYSTALLOGRAPHY.
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   [11]
RP   X-RAY CRYSTALLOGRAPHY.
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 (PubMed:27605664). Plays a role
CC       in proper central nervous system (CNS) development in vertebrates (By
CC       similarity). {ECO:0000250|UniProtKB:P24311,
CC       ECO:0000269|PubMed:27605664}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000305|PubMed:27605664}.
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 COXFA4, 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). {ECO:0000269|PubMed:26698328,
CC       ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:8638158}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:27605664,
CC       ECO:0000269|PubMed:31533957}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase VIIb family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA30489.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI03175.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; J05058; AAA30489.1; ALT_INIT; mRNA.
DR   EMBL; BC103174; AAI03175.1; ALT_INIT; mRNA.
DR   PIR; A34410; OSBO7B.
DR   RefSeq; NP_786989.3; NM_175795.3.
DR   PDB; 1OCC; X-ray; 2.80 A; K/X=25-80.
DR   PDB; 1OCO; X-ray; 2.80 A; K/X=25-80.
DR   PDB; 1OCR; X-ray; 2.35 A; K/X=25-80.
DR   PDB; 1OCZ; X-ray; 2.90 A; K/X=25-80.
DR   PDB; 1V54; X-ray; 1.80 A; K/X=25-80.
DR   PDB; 1V55; X-ray; 1.90 A; K/X=25-80.
DR   PDB; 2DYR; X-ray; 1.80 A; K/X=25-80.
DR   PDB; 2DYS; X-ray; 2.20 A; K/X=25-80.
DR   PDB; 2EIJ; X-ray; 1.90 A; K/X=25-80.
DR   PDB; 2EIK; X-ray; 2.10 A; K/X=25-80.
DR   PDB; 2EIL; X-ray; 2.10 A; K/X=25-80.
DR   PDB; 2EIM; X-ray; 2.60 A; K/X=25-80.
DR   PDB; 2EIN; X-ray; 2.70 A; K/X=25-80.
DR   PDB; 2OCC; X-ray; 2.30 A; K/X=25-80.
DR   PDB; 2Y69; X-ray; 1.95 A; K/X=1-80.
DR   PDB; 2YBB; EM; 19.00 A; V=25-80.
DR   PDB; 2ZXW; X-ray; 2.50 A; K/X=25-80.
DR   PDB; 3ABK; X-ray; 2.00 A; K/X=25-80.
DR   PDB; 3ABL; X-ray; 2.10 A; K/X=25-80.
DR   PDB; 3ABM; X-ray; 1.95 A; K/X=25-80.
DR   PDB; 3AG1; X-ray; 2.20 A; K/X=25-80.
DR   PDB; 3AG2; X-ray; 1.80 A; K/X=25-80.
DR   PDB; 3AG3; X-ray; 1.80 A; K/X=25-80.
DR   PDB; 3AG4; X-ray; 2.05 A; K/X=25-80.
DR   PDB; 3ASN; X-ray; 3.00 A; K/X=25-80.
DR   PDB; 3ASO; X-ray; 2.30 A; K/X=25-80.
DR   PDB; 3WG7; X-ray; 1.90 A; K/X=25-80.
DR   PDB; 3X2Q; X-ray; 2.00 A; K/X=25-80.
DR   PDB; 5B1A; X-ray; 1.50 A; K/X=25-80.
DR   PDB; 5B1B; X-ray; 1.60 A; K/X=30-78.
DR   PDB; 5B3S; X-ray; 1.68 A; K/X=30-78.
DR   PDB; 5GPN; EM; 5.40 A; 8=25-80.
DR   PDB; 5IY5; X-ray; 2.00 A; K/X=30-78.
DR   PDB; 5LUF; EM; 9.10 A; 8=25-80.
DR   PDB; 5W97; X-ray; 2.30 A; K/k=25-80.
DR   PDB; 5WAU; X-ray; 1.95 A; K/k=25-80.
DR   PDB; 5X19; X-ray; 2.20 A; K/X=25-80.
DR   PDB; 5X1B; X-ray; 2.40 A; K/X=25-80.
DR   PDB; 5X1F; X-ray; 2.20 A; K/X=25-80.
DR   PDB; 5XDQ; X-ray; 1.77 A; K/X=25-80.
DR   PDB; 5XDX; X-ray; 1.99 A; K/X=25-80.
DR   PDB; 5XTH; EM; 3.90 A; 7=30-78.
DR   PDB; 5XTI; EM; 17.40 A; 7/B7=30-78.
DR   PDB; 5Z84; X-ray; 1.85 A; K/X=25-80.
DR   PDB; 5Z85; X-ray; 1.85 A; K/X=25-80.
DR   PDB; 5Z86; X-ray; 1.85 A; K/X=25-80.
DR   PDB; 5ZCO; X-ray; 1.90 A; K/X=25-80.
DR   PDB; 5ZCP; X-ray; 1.65 A; K/X=25-80.
DR   PDB; 5ZCQ; X-ray; 1.65 A; K/X=25-80.
DR   PDB; 6J8M; X-ray; 1.90 A; K/X=25-80.
DR   PDB; 6JUW; X-ray; 1.80 A; K/X=30-78.
DR   PDB; 6JY3; X-ray; 1.85 A; K=25-80.
DR   PDB; 6JY4; X-ray; 1.95 A; K=25-80.
DR   PDB; 6NKN; X-ray; 2.50 A; K/X=25-80.
DR   PDB; 6NMF; X-ray; 2.80 A; K/X=25-80.
DR   PDB; 6NMP; X-ray; 2.90 A; K/X=25-80.
DR   PDB; 7COH; X-ray; 1.30 A; K/X=25-80.
DR   PDB; 7CP5; X-ray; 1.76 A; K/X=30-78.
DR   PDB; 7D5W; X-ray; 1.84 A; K/X=30-78.
DR   PDB; 7D5X; X-ray; 1.74 A; K/X=30-78.
DR   PDB; 7DGQ; EM; 5.00 A; B3=1-80.
DR   PDB; 7DGR; EM; 4.60 A; B0=1-80.
DR   PDB; 7DGS; EM; 7.80 A; B0=1-80.
DR   PDB; 7DKF; EM; 8.30 A; K3=1-80.
DR   PDB; 7EV7; X-ray; 1.70 A; K/X=25-80.
DR   PDB; 7THU; X-ray; 1.93 A; K/X=25-80.
DR   PDB; 7TIE; X-ray; 1.90 A; K/X=25-80.
DR   PDB; 7TIH; X-ray; 2.35 A; K/X=25-80.
DR   PDB; 7TII; X-ray; 2.45 A; K/X=25-80.
DR   PDB; 7VUW; X-ray; 1.60 A; K/X=30-78.
DR   PDB; 7VVR; X-ray; 1.65 A; K/X=30-78.
DR   PDB; 7W3E; X-ray; 1.45 A; K/X=30-78.
DR   PDB; 7XMA; X-ray; 2.20 A; K/X=25-80.
DR   PDB; 7XMB; X-ray; 2.20 A; K/X=25-80.
DR   PDB; 7Y44; X-ray; 1.90 A; K/X=25-80.
DR   PDB; 7YPY; X-ray; 1.50 A; K/X=25-80.
DR   PDB; 8D4T; EM; 3.10 A; X=32-78.
DR   PDB; 8GBT; X-ray; 2.80 A; K/X=25-80.
DR   PDB; 8GCQ; X-ray; 2.38 A; K/X=25-80.
DR   PDB; 8GVM; X-ray; 1.85 A; K/X=25-80.
DR   PDB; 8H8R; X-ray; 1.70 A; K/X=25-80.
DR   PDB; 8H8S; X-ray; 1.70 A; K/X=25-80.
DR   PDB; 8IJN; X-ray; 1.80 A; K/X=25-80.
DR   PDB; 9IKF; X-ray; 1.75 A; K/X=25-80.
DR   PDB; 9IKG; X-ray; 1.85 A; K/X=25-80.
DR   PDB; 9IKH; X-ray; 1.75 A; K/X=25-80.
DR   PDB; 9IKI; X-ray; 1.75 A; K/X=25-80.
DR   PDB; 9KUK; X-ray; 1.80 A; K/X=25-80.
DR   PDB; 9KUL; X-ray; 1.80 A; K/X=25-80.
DR   PDB; 9KUM; X-ray; 1.80 A; K/X=25-80.
DR   PDB; 9M56; X-ray; 1.60 A; K/X=25-80.
DR   PDB; 9W2Z; EM; 2.61 A; K=30-78.
DR   AlphaFoldDB; P13183; -.
DR   EMDB; EMD-27196; -.
DR   EMDB; EMD-30673; -.
DR   EMDB; EMD-30674; -.
DR   EMDB; EMD-30675; -.
DR   EMDB; EMD-30706; -.
DR   EMDB; EMD-4107; -.
DR   EMDB; EMD-65585; -.
DR   EMDB; EMD-9534; -.
DR   SMR; P13183; -.
DR   CORUM; P13183; -.
DR   DIP; DIP-60939N; -.
DR   FunCoup; P13183; 316.
DR   IntAct; P13183; 1.
DR   STRING; 9913.ENSBTAP00000041017; -.
DR   PaxDb; 9913-ENSBTAP00000041017; -.
DR   GeneID; 100300550; -.
DR   KEGG; bta:100300550; -.
DR   CTD; 1349; -.
DR   eggNOG; ENOG502S9DG; Eukaryota.
DR   HOGENOM; CLU_172656_0_0_1; -.
DR   InParanoid; P13183; -.
DR   OMA; AMWTYVA; -.
DR   OrthoDB; 9937520at2759; -.
DR   BRENDA; 7.1.1.9; 908.
DR   UniPathway; UPA00705; -.
DR   EvolutionaryTrace; P13183; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; EXP:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR   CDD; cd01403; Cyt_c_Oxidase_VIIb; 1.
DR   DisProt; DP00828; -.
DR   FunFam; 4.10.51.10:FF:000001; Cytochrome c oxidase subunit 7B, mitochondrial; 1.
DR   Gene3D; 4.10.51.10; Cytochrome C Oxidase, chain K; 1.
DR   InterPro; IPR008433; Cyt_c_oxidase_suVIIB.
DR   InterPro; IPR023272; Cyt_c_oxidase_suVIIB_dom_sf.
DR   PANTHER; PTHR16716; CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR16716:SF0; CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL; 1.
DR   Pfam; PF05392; COX7B; 1.
DR   SUPFAM; SSF81423; Mitochondrial cytochrome c oxidase subunit VIIb; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2844245"
FT   CHAIN           25..80
FT                   /note="Cytochrome c oxidase subunit 7B, mitochondrial"
FT                   /id="PRO_0000006157"
FT   TOPO_DOM        25..32
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TRANSMEM        33..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   TOPO_DOM        60..80
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:27605664"
FT   CONFLICT        21
FT                   /note="V -> VQAV (in Ref. 1; AAA30489)"
FT                   /evidence="ECO:0000305"
FT   HELIX           33..59
FT                   /evidence="ECO:0007829|PDB:7COH"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:7COH"
SQ   SEQUENCE   80 AA;  9065 MW;  D8EB7080C1CAEB16 CRC64;
     MFPLAKNALS RLRVQSIQQA VARQIHQKRA PDFHDKYGNA VLASGATFCV AVWVYMATQI
     GIEWNPSPVG RVTPKEWREQ
//