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QCR7_PONAB
ID   QCR7_PONAB              Reviewed;         111 AA.
AC   Q5RC24;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Cytochrome b-c1 complex subunit 7;
DE   AltName: Full=Complex III subunit 7;
DE   AltName: Full=Complex III subunit VII;
DE   AltName: Full=Ubiquinol-cytochrome c reductase complex 14 kDa protein;
GN   Name=UQCRB;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC       multisubunit transmembrane complex that is part of the mitochondrial
CC       electron transport chain which drives oxidative phosphorylation. The
CC       respiratory chain contains 3 multisubunit complexes succinate
CC       dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC       (complex IV, CIV), that cooperate to transfer electrons derived from
CC       NADH and succinate to molecular oxygen, creating an electrochemical
CC       gradient over the inner membrane that drives transmembrane transport
CC       and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC       transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC       translocation of protons across the mitochondrial inner membrane, with
CC       protons being carried across the membrane as hydrogens on the quinol.
CC       In the process called Q cycle, 2 protons are consumed from the matrix,
CC       4 protons are released into the intermembrane space and 2 electrons are
CC       passed to cytochrome c. {ECO:0000250|UniProtKB:P00128}.
CC   -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC       composed of 11 subunits. The complex is composed of 3 respiratory
CC       subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC       protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC       weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC       UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC       protein UQCRFS1 (By similarity). The complex exists as an obligatory
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC       cytochrome c oxidase (complex IV, CIV), resulting in different
CC       assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC       MCI(2)III(2)IV(2)) (By similarity). {ECO:0000250|UniProtKB:P00129,
CC       ECO:0000250|UniProtKB:P14927}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00128}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00128}; Matrix side
CC       {ECO:0000250|UniProtKB:P00128}.
CC   -!- SIMILARITY: Belongs to the UQCRB/QCR7 family. {ECO:0000305}.
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DR   EMBL; CR858458; CAH90686.1; -; mRNA.
DR   RefSeq; NP_001125376.1; NM_001131904.2.
DR   AlphaFoldDB; Q5RC24; -.
DR   SMR; Q5RC24; -.
DR   STRING; 9601.ENSPPYP00000021046; -.
DR   Ensembl; ENSPPYT00000021888; ENSPPYP00000021046; ENSPPYG00000018763.
DR   GeneID; 100172279; -.
DR   KEGG; pon:100172279; -.
DR   CTD; 7381; -.
DR   eggNOG; KOG3440; Eukaryota.
DR   GeneTree; ENSGT00390000012916; -.
DR   HOGENOM; CLU_115154_2_0_1; -.
DR   InParanoid; Q5RC24; -.
DR   OMA; APYIMKR; -.
DR   OrthoDB; 1606436at2759; -.
DR   TreeFam; TF105035; -.
DR   Proteomes; UP000001595; Chromosome 8.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:InterPro.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
DR   Gene3D; 1.10.1090.10; -; 1.
DR   InterPro; IPR003197; QCR7.
DR   InterPro; IPR036544; QCR7_sf.
DR   PANTHER; PTHR12022; PTHR12022; 1.
DR   Pfam; PF02271; UCR_14kD; 1.
DR   PIRSF; PIRSF000022; Bc1_14K; 1.
DR   SUPFAM; SSF81524; SSF81524; 1.
PE   3: Inferred from homology;
KW   Acetylation; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00129"
FT   CHAIN           2..111
FT                   /note="Cytochrome b-c1 complex subunit 7"
FT                   /id="PRO_0000193526"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P00129"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         12
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         78
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         78
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         83
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
FT   MOD_RES         96
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D855"
SQ   SEQUENCE   111 AA;  13503 MW;  E60DA3F8D4FA55B7 CRC64;
     MAGKQAVSAS GKWLDGIRKW YYNAAGFNKL GLMRDDTIYE DEDVKEAIRR LPENLYNDRM
     FRIKRALDLS LKHQILPKEQ WTKYEEENFY LEPYLKEVIR ERKEREEWAK K
 
 
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