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CYB_RABIT
ID   CYB_RABIT               Reviewed;         379 AA.
AC   P34863; O79439; Q36607;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 3.
DT   03-AUG-2022, entry version 125.
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   Oryctolagus cuniculus (Rabbit).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Irwin D.M., Arnason U.;
RT   "Cytochrome b gene of marine mammals: phylogeny and evolution.";
RL   J. Mammal. Evol. 2:37-55(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke {ECO:0000312|Proteomes:UP000001811};
RX   PubMed=9653643; DOI=10.1006/geno.1998.5282;
RA   Gissi C., Gullberg A., Arnason U.;
RT   "The complete mitochondrial DNA sequence of the rabbit, Oryctolagus
RT   cuniculus.";
RL   Genomics 50:161-169(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 211-379.
RX   PubMed=2269281; DOI=10.1111/j.1432-1033.1990.tb15653.x;
RA   Mignotte F., Gueride M., Champagne A.M., Mounolou J.C.;
RT   "Direct repeats in the non-coding region of rabbit mitochondrial DNA.
RT   Involvement in the generation of intra- and inter-individual
RT   heterogeneity.";
RL   Eur. J. Biochem. 194:561-571(1990).
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; U07566; AAA19919.1; -; Genomic_DNA.
DR   EMBL; AJ001588; CAA04859.1; -; Genomic_DNA.
DR   EMBL; X54172; CAA38105.1; -; Genomic_DNA.
DR   PIR; T11492; T11492.
DR   RefSeq; NP_007561.1; NC_001913.1.
DR   AlphaFoldDB; P34863; -.
DR   SMR; P34863; -.
DR   STRING; 9986.ENSOCUP00000026191; -.
DR   Ensembl; ENSOCUT00000033140; ENSOCUP00000026191; ENSOCUG00000029115.
DR   GeneID; 808227; -.
DR   KEGG; ocu:808227; -.
DR   CTD; 4519; -.
DR   eggNOG; KOG4663; Eukaryota.
DR   GeneTree; ENSGT00390000017948; -.
DR   HOGENOM; CLU_031114_3_0_1; -.
DR   InParanoid; P34863; -.
DR   OMA; RFFAFHF; -.
DR   OrthoDB; 1125966at2759; -.
DR   TreeFam; TF353088; -.
DR   Proteomes; UP000001811; Mitochondrion.
DR   Bgee; ENSOCUG00000029115; Expressed in heart and 17 other tissues.
DR   ExpressionAtlas; P34863; baseline.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:Ensembl.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:Ensembl.
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_0000061480"
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   CONFLICT        129
FT                   /note="M -> I (in Ref. 1; AAA19919)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="F -> L (in Ref. 1; AAA19919)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="T -> S (in Ref. 1; AAA19919)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   379 AA;  42786 MW;  ACE2A95D8EFEE445 CRC64;
     MTNIRKTHPL LKIVNHSLID LPAPSNISAW WNFGSLLGLC LMIQIFTGLF LAMHYTSDTT
     TAFSSVTHIC RDVNYGWLIR YLHANGASMF FICLYMHVGR GIYYGSYTYL ETWNIGIILL
     FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTTL VEWIWGGFSV DKATLTRFFA
     FHFILPFIIA TLVLIHLLFL HETGSNNPTG IPSNSDKIPF HPYYTIKDTL GFLVAILLLL
     ILVLFSPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSILV
     LAFIPFLHMS KQRSMMFRPI SQVLFWVLVA DLLTLTWIGG QPVEHPFITI GQVASVLYFT
     TILILMPLAS LIENKILKW
 
 
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