CX6B2_RAT
ID CX6B2_RAT Reviewed; 88 AA.
AC Q6YFQ1;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cytochrome c oxidase subunit 6B2;
DE AltName: Full=Cytochrome c oxidase subunit VIb isoform 2;
DE Short=COX VIb-2;
DE AltName: Full=Cytochrome c oxidase subunit VIb, testis-specific isoform;
GN Name=Cox6b2;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12874793; DOI=10.1002/mrd.10327;
RA Huttemann M., Jaradat S., Grossman L.I.;
RT "Cytochrome c oxidase of mammals contains a testes-specific isoform of
RT subunit VIb -- the counterpart to testes-specific cytochrome c?";
RL Mol. Reprod. Dev. 66:8-16(2003).
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:Q01519}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:Q01519}.
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)).
CC {ECO:0000250|UniProtKB:P00429}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00429}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00429}; Intermembrane side
CC {ECO:0000250|UniProtKB:P00429}.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12874793}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC {ECO:0000305}.
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DR EMBL; AY152399; AAN46752.1; -; mRNA.
DR RefSeq; NP_001034174.1; NM_001039085.1.
DR AlphaFoldDB; Q6YFQ1; -.
DR SMR; Q6YFQ1; -.
DR STRING; 10116.ENSRNOP00000035591; -.
DR PaxDb; Q6YFQ1; -.
DR GeneID; 654441; -.
DR KEGG; rno:654441; -.
DR UCSC; RGD:1591896; rat.
DR CTD; 125965; -.
DR RGD; 1591896; Cox6b2.
DR eggNOG; KOG3057; Eukaryota.
DR HOGENOM; CLU_133964_3_1_1; -.
DR InParanoid; Q6YFQ1; -.
DR OMA; VQRWNQQ; -.
DR OrthoDB; 1586678at2759; -.
DR PhylomeDB; Q6YFQ1; -.
DR TreeFam; TF105065; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:Q6YFQ1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000038616; Expressed in testis and 20 other tissues.
DR Genevisible; Q6YFQ1; RN.
DR GO; GO:0030061; C:mitochondrial crista; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd00926; Cyt_c_Oxidase_VIb; 1.
DR Gene3D; 1.10.10.140; -; 1.
DR InterPro; IPR003213; Cyt_c_oxidase_su6B.
DR InterPro; IPR036549; Cyt_c_oxidase_su6B_sf.
DR PANTHER; PTHR11387; PTHR11387; 1.
DR Pfam; PF02297; COX6B; 1.
DR PIRSF; PIRSF000278; Cyt_c_oxidase_6B; 1.
DR SUPFAM; SSF47694; SSF47694; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome.
FT CHAIN 1..88
FT /note="Cytochrome c oxidase subunit 6B2"
FT /id="PRO_0000194923"
FT DOMAIN 29..75
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..42
FT /note="Cx9C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 56..67
FT /note="Cx10C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 32..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 42..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 88 AA; 10472 MW; E20F30D1486EA1B7 CRC64;
MLGVQAQMPA PGQWTTPPFD PRFPNQNQTR NCYQNFLDYH RCVKTMDRRG KNTQACDYYF
RVFHSLCPVS WVQRWNEQIK QGTFPGKI
