COX7B_MOUSE
ID COX7B_MOUSE Reviewed; 80 AA.
AC P56393;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cytochrome c oxidase subunit 7B, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VIIb;
DE Flags: Precursor;
GN Name=Cox7b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Marra M., Hillier L., Allen M., Bowles M., Dietrich N., Dubuque T.,
RA Geisel S., Kucaba T., Lacy M., Le M., Martin J., Morris M.,
RA Schellenberg K., Steptoe M., Tan F., Underwood K., Moore B., Theising B.,
RA Wylie T., Lennon G., Soares B., Wilson R., Waterston R.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
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 (By similarity). Plays a role in
CC proper central nervous system (CNS) development in vertebrates (By
CC similarity). {ECO:0000250|UniProtKB:P13183,
CC ECO:0000250|UniProtKB:P24311}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P13183}.
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:P13183}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P13183}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P13183}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase VIIb family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AA033366; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AA049075; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AA032894; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AA051290; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AA086918; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AA032640; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK002593; BAB22214.1; -; mRNA.
DR EMBL; BC024350; AAH24350.1; -; mRNA.
DR CCDS; CCDS41096.1; -.
DR RefSeq; NP_079655.1; NM_025379.2.
DR PDB; 7O37; EM; 3.20 A; k=25-80.
DR PDB; 7O3C; EM; 3.30 A; k=25-80.
DR PDB; 7O3E; EM; 3.60 A; k=25-80.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR AlphaFoldDB; P56393; -.
DR SMR; P56393; -.
DR BioGRID; 211245; 1.
DR CORUM; P56393; -.
DR STRING; 10090.ENSMUSP00000033582; -.
DR iPTMnet; P56393; -.
DR PhosphoSitePlus; P56393; -.
DR jPOST; P56393; -.
DR PaxDb; P56393; -.
DR PeptideAtlas; P56393; -.
DR PRIDE; P56393; -.
DR ProteomicsDB; 283796; -.
DR TopDownProteomics; P56393; -.
DR Antibodypedia; 44006; 93 antibodies from 23 providers.
DR DNASU; 66142; -.
DR Ensembl; ENSMUST00000033582; ENSMUSP00000033582; ENSMUSG00000031231.
DR GeneID; 66142; -.
DR KEGG; mmu:66142; -.
DR UCSC; uc009ubk.1; mouse.
DR CTD; 1349; -.
DR MGI; MGI:1913392; Cox7b.
DR VEuPathDB; HostDB:ENSMUSG00000031231; -.
DR eggNOG; ENOG502S9DG; Eukaryota.
DR GeneTree; ENSGT00390000012178; -.
DR HOGENOM; CLU_172656_0_0_1; -.
DR InParanoid; P56393; -.
DR OMA; GATFCIT; -.
DR OrthoDB; 1571716at2759; -.
DR PhylomeDB; P56393; -.
DR TreeFam; TF105068; -.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR UniPathway; UPA00705; -.
DR BioGRID-ORCS; 66142; 18 hits in 76 CRISPR screens.
DR ChiTaRS; Cox7b; mouse.
DR PRO; PR:P56393; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P56393; protein.
DR Bgee; ENSMUSG00000031231; Expressed in interventricular septum and 137 other tissues.
DR ExpressionAtlas; P56393; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0045277; C:respiratory chain complex IV; IBA:GO_Central.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01403; Cyt_c_Oxidase_VIIb; 1.
DR Gene3D; 4.10.51.10; -; 1.
DR InterPro; IPR008433; Cyt_c_oxidase_suVIIB.
DR InterPro; IPR023272; Cyt_c_oxidase_suVIIB_dom_sf.
DR PANTHER; PTHR16716; PTHR16716; 1.
DR Pfam; PF05392; COX7B; 1.
DR SUPFAM; SSF81423; SSF81423; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P13183"
FT CHAIN 25..80
FT /note="Cytochrome c oxidase subunit 7B, mitochondrial"
FT /id="PRO_0000006159"
FT TOPO_DOM 25..32
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P13183"
FT TRANSMEM 33..59
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P13183"
FT TOPO_DOM 60..80
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P13183"
FT HELIX 34..58
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:7O3C"
SQ SEQUENCE 80 AA; 9011 MW; D68B28A9FAF1E9A0 CRC64;
MLPLAKNALS RLQVRSIQQV VARQSHQKRA PSFHDKYGNA ILAGGAIFCV STWTYTATQI
GIEWNMSPVG RVTPKEWRDQ
