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CYB_URSAR
ID   CYB_URSAR               Reviewed;         379 AA.
AC   Q36192; Q36191; Q36193; Q36872; Q36938; Q36990; Q37052;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 99.
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   Ursus arctos (Brown bear) (Grizzly bear).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=8744769; DOI=10.1006/mpev.1996.0051;
RA   Talbot S.L., Shields G.F.;
RT   "A phylogeny of the bears (Ursidae) inferred from complete sequences of
RT   three mitochondrial genes.";
RL   Mol. Phylogenet. Evol. 5:567-575(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7714914; DOI=10.1007/bf00166598;
RA   Arnason U., Bodin K., Gullberg A., Ledje C., Mouchaty S.;
RT   "A molecular view of pinniped relationships with particular emphasis on the
RT   true seals.";
RL   J. Mol. Evol. 40:78-85(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
RA   Lento G.M., Hickson R.E., Chambers G.K., Penny D.;
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
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   -!- POLYMORPHISM: Sequenced in lineages GB01 to GB26.
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; U18870; AAB38167.1; -; Genomic_DNA.
DR   EMBL; U18871; AAB38168.1; -; Genomic_DNA.
DR   EMBL; U18872; AAB38169.1; -; Genomic_DNA.
DR   EMBL; U18873; AAB38170.1; -; Genomic_DNA.
DR   EMBL; U18874; AAB38171.1; -; Genomic_DNA.
DR   EMBL; U18875; AAB38172.1; -; Genomic_DNA.
DR   EMBL; U18876; AAB38173.1; -; Genomic_DNA.
DR   EMBL; U18877; AAB38174.1; -; Genomic_DNA.
DR   EMBL; U18878; AAB38175.1; -; Genomic_DNA.
DR   EMBL; U18879; AAB38176.1; -; Genomic_DNA.
DR   EMBL; U18880; AAB38177.1; -; Genomic_DNA.
DR   EMBL; U18881; AAB38178.1; -; Genomic_DNA.
DR   EMBL; U18882; AAB38179.1; -; Genomic_DNA.
DR   EMBL; U18883; AAB38180.1; -; Genomic_DNA.
DR   EMBL; U18884; AAB38181.1; -; Genomic_DNA.
DR   EMBL; U18885; AAB38182.1; -; Genomic_DNA.
DR   EMBL; U18886; AAB38183.1; -; Genomic_DNA.
DR   EMBL; U18887; AAB38184.1; -; Genomic_DNA.
DR   EMBL; U18888; AAB38185.1; -; Genomic_DNA.
DR   EMBL; U18889; AAB38186.1; -; Genomic_DNA.
DR   EMBL; U18890; AAB38187.1; -; Genomic_DNA.
DR   EMBL; U18891; AAB38188.1; -; Genomic_DNA.
DR   EMBL; U18892; AAB38189.1; -; Genomic_DNA.
DR   EMBL; U18893; AAB38190.1; -; Genomic_DNA.
DR   EMBL; U18894; AAB38191.1; -; Genomic_DNA.
DR   EMBL; U18895; AAB38192.1; -; Genomic_DNA.
DR   EMBL; U18896; AAB38193.1; -; Genomic_DNA.
DR   EMBL; U18897; AAB38194.1; -; Genomic_DNA.
DR   EMBL; X82308; CAA57751.1; -; Genomic_DNA.
DR   EMBL; U12855; AAA67259.1; -; Genomic_DNA.
DR   PIR; S58454; S58454.
DR   AlphaFoldDB; Q36192; -.
DR   SMR; Q36192; -.
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; Respiratory chain; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..379
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000061703"
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         57
FT                   /note="P -> S (in lineages GB01, GB02, GB03, GB04 and
FT                   GB05)"
FT   VARIANT         89
FT                   /note="I -> M (in lineages GB01, GB02, GB03, GB04 and
FT                   GB05)"
FT   VARIANT         110
FT                   /note="P -> S (in lineages GB01, GB02, GB03, GB04, GB05,
FT                   GB08, GB09, GB10, GB12, GB14 and GB17)"
FT   VARIANT         123
FT                   /note="I -> V (in lineages GB01, GB02, GB03, GB04 and
FT                   GB05)"
FT   VARIANT         153
FT                   /note="I -> V (in lineages GB01, GB02, GB03 and GB05)"
FT   VARIANT         236
FT                   /note="A -> T (in lineages GB01, GB02, GB03, GB04 and
FT                   GB05)"
FT   VARIANT         238
FT                   /note="T -> A (in lineages GB01, GB02, GB03, GB04 and
FT                   GB05)"
FT   VARIANT         257
FT                   /note="T -> I (in lineages GB01, GB02, GB03, GB04 and
FT                   GB05)"
FT   VARIANT         303
FT                   /note="I -> L (in lineages GB01, GB02, GB03, GB04 and
FT                   GB05)"
FT   VARIANT         368
FT                   /note="I -> T (in lineage GB01)"
FT   VARIANT         375
FT                   /note="N -> S (in lineages GB10 and GB12)"
SQ   SEQUENCE   379 AA;  42459 MW;  0D82449AD05FF329 CRC64;
     MTNIRKTHPL AKIINNSFID LPTPSNISAW WNFGSLLGVC LILQILTGLF LAMHYTPDTT
     TAFSSVTHIC RDVHYGWVIR YVHANGASIF FICLFMHVGR GLYYGSYLFP ETWNIGIILL
     FTIMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VEWIWGGFSV DKATLTRFFA
     FHFILPFIIL ALAAVHLLFL HETGSNNPSG IPSDSDKIPF HPYYTIKDIL GALLLALTLA
     TLVLFSPDLL GDPDNYTPAN PLSTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALIFSILI
     LAIIPLLHTS KQRGMMFRPL SQCLFWLLVA DLLTLTWIGG QPVEHPFIII GQLASILYFT
     ILLVLMPIAG IIENNLLKW
 
 
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