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CX6B1_CARSF
ID   CX6B1_CARSF             Reviewed;          86 AA.
AC   Q7YRK6;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Cytochrome c oxidase subunit 6B1;
DE   AltName: Full=Cytochrome c oxidase subunit VIb isoform 1;
DE            Short=COX VIb-1;
GN   Name=COX6B1; Synonyms=COX6B;
OS   Carlito syrichta (Philippine tarsier) (Tarsius syrichta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC   Carlito.
OX   NCBI_TaxID=1868482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Doan J.W., Schmidt T.R., Wildman D.E., Goldberg A., Huttemann M.,
RA   Goodman M., Weiss M.L., Grossman L.I.;
RT   "Co-evolution in cytochrome c oxidase: 9 of 13 subunits show accelerated
RT   rates of nonsynonymous substitution in anthropoid primates.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC       {ECO:0000305}.
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DR   EMBL; AY236504; AAP43950.1; -; mRNA.
DR   RefSeq; XP_008069188.1; XM_008070997.1.
DR   AlphaFoldDB; Q7YRK6; -.
DR   SMR; Q7YRK6; -.
DR   STRING; 1868482.ENSTSYP00000013356; -.
DR   Ensembl; ENSTSYT00000014556; ENSTSYP00000013356; ENSTSYG00000014563.
DR   GeneID; 103273566; -.
DR   KEGG; csyr:103273566; -.
DR   CTD; 32989; -.
DR   HOGENOM; CLU_133964_3_1_1; -.
DR   OrthoDB; 1586678at2759; -.
DR   TreeFam; TF105065; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000189704; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Acetylation; Disulfide bond; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00429"
FT   CHAIN           2..86
FT                   /note="Cytochrome c oxidase subunit 6B1"
FT                   /id="PRO_0000194918"
FT   DOMAIN          27..73
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           30..40
FT                   /note="Cx9C motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           54..65
FT                   /note="Cx10C motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P00429"
FT   MOD_RES         62
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P56391"
FT   DISULFID        30..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        40..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   86 AA;  10187 MW;  A2F4C399A0FE599B CRC64;
     MAEDIKTKIK NYKTAPFDSR FPNQNQTRNC WQNYLDFHRC EKAMTAKGGD VSVCEWYRRV
     YKSLCPISWV STWDDRRAEG TFPGKI
 
 
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