CX6C2_RAT
ID CX6C2_RAT Reviewed; 76 AA.
AC P11951; Q63703;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cytochrome c oxidase subunit 6C-2;
DE AltName: Full=Cytochrome c oxidase polypeptide VIc-2;
GN Name=Cox6c2; Synonyms=Cox6c;
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 [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=2836143; DOI=10.1089/dna.1988.7.163;
RA Suske G., Enders C., Schlerf A., Kadenbach B.;
RT "Organization and nucleotide sequence of two chromosomal genes for rat
RT cytochrome c oxidase subunit VIc: a structural and a processed gene.";
RL DNA 7:163-171(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2822403; DOI=10.1111/j.1432-1033.1987.tb13410.x;
RA Suske G., Mengel T., Cordingley M., Kadenbach B.;
RT "Molecular cloning and further characterization of cDNAs for rat nuclear-
RT encoded cytochrome c oxidase subunits VIc and VIII.";
RL Eur. J. Biochem. 168:233-237(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2854406; DOI=10.1111/j.1749-6632.1988.tb35348.x;
RA Cao X.N., Hengst L., Schlerf A., Droste M., Mengel T., Kadenbach B.;
RT "Complexity of nucleus-encoded genes of mammalian cytochrome c oxidase.";
RL Ann. N. Y. Acad. Sci. 550:337-347(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-76.
RX PubMed=6200111; DOI=10.1016/0006-291x(84)91480-3;
RA Parimoo S., Seelan R.S., Desai S., Buse G., Padmanaban G.;
RT "Construction of a cDNA clone for a nuclear-coded subunit of cytochrome c
RT oxidase from rat liver.";
RL Biochem. Biophys. Res. Commun. 118:902-909(1984).
RN [6]
RP PROTEIN SEQUENCE OF 2-11.
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 [7]
RP PROTEIN SEQUENCE OF 40-46 AND 68-76, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:P04038}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P04038}.
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:P04038}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P04038}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P04038}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6c family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA79270.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M20153; AAA41011.1; -; Genomic_DNA.
DR EMBL; M20152; AAA41011.1; JOINED; Genomic_DNA.
DR EMBL; M27466; AAA79271.1; -; mRNA.
DR EMBL; M27467; AAA79270.1; ALT_INIT; mRNA.
DR EMBL; BC058480; AAH58480.1; -; mRNA.
DR EMBL; K01565; AAA41013.1; -; mRNA.
DR PIR; S00114; S00114.
DR RefSeq; NP_062233.2; NM_019360.2.
DR AlphaFoldDB; P11951; -.
DR SMR; P11951; -.
DR BioGRID; 248538; 1.
DR IntAct; P11951; 1.
DR MINT; P11951; -.
DR STRING; 10116.ENSRNOP00000014407; -.
DR CarbonylDB; P11951; -.
DR iPTMnet; P11951; -.
DR PhosphoSitePlus; P11951; -.
DR SwissPalm; P11951; -.
DR jPOST; P11951; -.
DR PaxDb; P11951; -.
DR PRIDE; P11951; -.
DR Ensembl; ENSRNOT00000014407; ENSRNOP00000014407; ENSRNOG00000010807.
DR GeneID; 54322; -.
DR KEGG; rno:54322; -.
DR UCSC; RGD:620616; rat.
DR CTD; 1345; -.
DR RGD; 620616; Cox6c.
DR eggNOG; ENOG502SEI2; Eukaryota.
DR GeneTree; ENSGT00940000163089; -.
DR HOGENOM; CLU_196254_0_0_1; -.
DR InParanoid; P11951; -.
DR OMA; YKNYDPM; -.
DR OrthoDB; 1618740at2759; -.
DR PhylomeDB; P11951; -.
DR TreeFam; TF353619; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:P11951; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000010807; Expressed in heart and 20 other tissues.
DR Genevisible; P11951; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:RGD.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; TAS:RGD.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR CDD; cd00927; Cyt_c_Oxidase_VIc; 1.
DR Gene3D; 4.10.93.10; -; 1.
DR InterPro; IPR004204; COX6C.
DR InterPro; IPR034884; Cytochrome_c_oxidase_VIc/VIIs.
DR InterPro; IPR037169; Cytochrome_c_oxidase_VIc_sf.
DR Pfam; PF02937; COX6C; 1.
DR SUPFAM; SSF81415; SSF81415; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7601105"
FT CHAIN 2..76
FT /note="Cytochrome c oxidase subunit 6C-2"
FT /id="PRO_0000191304"
FT TOPO_DOM 4..14
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P04038"
FT TRANSMEM 15..55
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P04038"
FT TOPO_DOM 56..76
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P04038"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 29
FT /note="V -> A (in Ref. 3; AAA79270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 76 AA; 8455 MW; 988D10E1F2D387BD CRC64;
MSSGALLPKP QMRGLLAKRL RVHIVGAFVV ALGVAAAYKF GVAEPRKKAY ADFYRNYDSM
KDFEEMRQAG VFQSAK
