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CYB_RHIFE
ID   CYB_RHIFE               Reviewed;         379 AA.
AC   O21298; O21297; Q8HC80; Q8HCG5; Q8HQF3;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 3.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Cytochrome b;
DE   AltName: Full=Complex III subunit 3;
DE   AltName: Full=Complex III subunit III;
DE   AltName: Full=Cytochrome b-c1 complex subunit 3;
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
GN   Name=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS   Rhinolophus ferrumequinum (Greater horseshoe bat).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC   Rhinolophinae; Rhinolophus.
OX   NCBI_TaxID=59479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sakai T., Kikkawa Y., Tuchiya K., Harada M., Kanoe M., Yoshiyuki M.,
RA   Yonekawa H.;
RT   "Bats cytochrome b gene.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-119 AND 282-379.
RX   PubMed=9144281; DOI=10.1038/387138b0;
RA   Barratt E.M., Deaville R., Burland T.M., Bruford M.W., Jones G.,
RA   Racey P.A., Wayne R.K.;
RT   "DNA answers the call of pipistrelle bat species.";
RL   Nature 387:138-139(1997).
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC       (complex III or cytochrome b-c1 complex) that is part of the
CC       mitochondrial respiratory chain. The b-c1 complex mediates electron
CC       transfer from ubiquinol to cytochrome c. Contributes to the generation
CC       of a proton gradient across the mitochondrial membrane that is then
CC       used for ATP synthesis. {ECO:0000250|UniProtKB:P00157}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P00157};
CC       Note=Binds 2 heme b groups non-covalently.
CC       {ECO:0000250|UniProtKB:P00157};
CC   -!- SUBUNIT: The cytochrome bc1 complex contains 11 subunits: 3 respiratory
CC       subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and
CC       UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7,
CC       UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of
CC       UQCRFS1). This cytochrome bc1 complex then forms a dimer.
CC       {ECO:0000250|UniProtKB:P00157}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00157}.
CC   -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at
CC       about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs
CC       at about 566 nm. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
CC   -!- CAUTION: The full-length protein contains only eight transmembrane
CC       helices, not nine as predicted by bioinformatics tools.
CC       {ECO:0000250|UniProtKB:P00157}.
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DR   EMBL; AB085721; BAC16615.1; -; Genomic_DNA.
DR   EMBL; AB085722; BAC16616.1; -; Genomic_DNA.
DR   EMBL; AB085723; BAC16617.1; -; Genomic_DNA.
DR   EMBL; AB085724; BAC16618.1; -; Genomic_DNA.
DR   EMBL; AB085725; BAC16619.1; -; Genomic_DNA.
DR   EMBL; AB085726; BAC16620.1; -; Genomic_DNA.
DR   EMBL; AB085727; BAC16621.1; -; Genomic_DNA.
DR   EMBL; AB085728; BAC16622.1; -; Genomic_DNA.
DR   EMBL; AB085729; BAC16623.1; -; Genomic_DNA.
DR   EMBL; AB085730; BAC16624.1; -; Genomic_DNA.
DR   EMBL; AB085731; BAC16625.1; -; Genomic_DNA.
DR   EMBL; U95513; AAC48750.1; -; Genomic_DNA.
DR   EMBL; U95514; AAC48751.1; -; Genomic_DNA.
DR   AlphaFoldDB; O21298; -.
DR   SMR; O21298; -.
DR   Proteomes; UP000472240; Mitochondrion.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   CDD; cd00290; cytochrome_b_C; 1.
DR   CDD; cd00284; Cytochrome_b_N; 1.
DR   Gene3D; 1.20.810.10; -; 1.
DR   InterPro; IPR005798; Cyt_b/b6_C.
DR   InterPro; IPR036150; Cyt_b/b6_C_sf.
DR   InterPro; IPR005797; Cyt_b/b6_N.
DR   InterPro; IPR027387; Cytb/b6-like_sf.
DR   InterPro; IPR030689; Cytochrome_b.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   PIRSF; PIRSF038885; COB; 1.
DR   SUPFAM; SSF81342; SSF81342; 1.
DR   SUPFAM; SSF81648; SSF81648; 1.
DR   PROSITE; PS51003; CYTB_CTER; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW   Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..379
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000061496"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        77..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         83
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b562"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         97
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b566"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         182
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b562"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         196
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b566"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         201
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   VARIANT         78
FT                   /note="V -> A"
FT   VARIANT         117
FT                   /note="I -> T"
FT   CONFLICT        303
FT                   /note="A -> V (in Ref. 2; AAC48751)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="A -> T (in Ref. 2; AAC48751)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   379 AA;  42367 MW;  0EEDEB7D29C79DFA CRC64;
     MTNIRKSHPL FKIINDSFVD LPAPSSISSW WNFGSLLGIC LAIQILTGLF LAMHYTSDTA
     TAFHSVTHIC RDVNYGWVLR YLHANGASMF FICLFLHVGR GIYYGSYTFS ETWNIGIILL
     FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYVGTTL VEWVWGGFSV DKATLTRFFA
     LHFLLPFIIA AMVMVHLLFL HETGSNNPTG IPSDADMIPF HPYYTIKDIL GLVLMLMALL
     SLVLFAPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VVALVLSILI
     LAAIPLLHTS KQRSMAFRPL SQCLFWLLVA DLLTLTWIGG QPVEHPFIII GQLASILYFL
     IILVLMPLAS IAENHLLKW
 
 
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