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CYB_CAEBR
ID   CYB_CAEBR               Reviewed;         370 AA.
AC   Q8HEC2; B1PE38; B1PE50; B1PE62; B1PED4; B1PEF8; B1PEI2; B1PEK6; B1PEP2;
AC   B1PEU0;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 3.
DT   03-AUG-2022, entry version 88.
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=ctb-1; Synonyms=cob, cytb, Mtcyb;
OS   Caenorhabditis briggsae.
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-97; LEU-321 AND
RP   PHE-342.
RC   STRAIN=PB800;
RX   PubMed=12644560; DOI=10.1093/molbev/msg044;
RA   Denver D.R., Morris K., Thomas W.K.;
RT   "Phylogenetics in Caenorhabditis elegans: an analysis of divergence and
RT   outcrossing.";
RL   Mol. Biol. Evol. 20:393-400(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-54; THR-97; LEU-142;
RP   ILE-205; THR-222; PHE-234; LEU-257; VAL-297; TRP-317; LEU-321; PHE-342;
RP   ILE-342 AND VAL-353.
RC   STRAIN=BW287, ED3032, ED3033, ED3034, ED3035, ED3036, ED3037, ED3083,
RC   ED3092, ED3101, EG4181, EG4207A, HK104, HK105, JU403, JU439, JU516, JU725,
RC   JU726, JU793, PB800, PB826, and VT847;
RX   PubMed=18302772; DOI=10.1186/1471-2148-8-62;
RA   Howe D.K., Denver D.R.;
RT   "Muller's Ratchet and compensatory mutation in Caenorhabditis briggsae
RT   mitochondrial genome evolution.";
RL   BMC Evol. Biol. 8:62-62(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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:P00163}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P00163};
CC       Note=Binds 2 heme b groups non-covalently.
CC       {ECO:0000250|UniProtKB:P00163};
CC   -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC       cytochrome c1 and the Rieske protein. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00163}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00163}.
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 protein contains an even number of transmembrane helices,
CC       fewer than predicted by bioinformatics tools.
CC       {ECO:0000250|UniProtKB:P00163}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO13511.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY171104; AAO13511.1; ALT_INIT; Genomic_DNA.
DR   EMBL; EU407781; ACB06105.1; -; Genomic_DNA.
DR   EMBL; EU407782; ACB06117.1; -; Genomic_DNA.
DR   EMBL; EU407783; ACB06129.1; -; Genomic_DNA.
DR   EMBL; EU407784; ACB06141.1; -; Genomic_DNA.
DR   EMBL; EU407785; ACB06153.1; -; Genomic_DNA.
DR   EMBL; EU407786; ACB06165.1; -; Genomic_DNA.
DR   EMBL; EU407787; ACB06177.1; -; Genomic_DNA.
DR   EMBL; EU407788; ACB06189.1; -; Genomic_DNA.
DR   EMBL; EU407789; ACB06201.1; -; Genomic_DNA.
DR   EMBL; EU407790; ACB06213.1; -; Genomic_DNA.
DR   EMBL; EU407791; ACB06225.1; -; Genomic_DNA.
DR   EMBL; EU407792; ACB06237.1; -; Genomic_DNA.
DR   EMBL; EU407793; ACB06249.1; -; Genomic_DNA.
DR   EMBL; EU407794; ACB06261.1; -; Genomic_DNA.
DR   EMBL; EU407795; ACB06273.1; -; Genomic_DNA.
DR   EMBL; EU407796; ACB06285.1; -; Genomic_DNA.
DR   EMBL; EU407797; ACB06297.1; -; Genomic_DNA.
DR   EMBL; EU407798; ACB06309.1; -; Genomic_DNA.
DR   EMBL; EU407799; ACB06321.1; -; Genomic_DNA.
DR   EMBL; EU407800; ACB06333.1; -; Genomic_DNA.
DR   EMBL; EU407801; ACB06345.1; -; Genomic_DNA.
DR   EMBL; EU407802; ACB06357.1; -; Genomic_DNA.
DR   EMBL; EU407803; ACB06369.1; -; Genomic_DNA.
DR   EMBL; AC186293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; YP_001552233.1; NC_009885.1.
DR   AlphaFoldDB; Q8HEC2; -.
DR   SMR; Q8HEC2; -.
DR   GeneID; 5666637; -.
DR   KEGG; cbr:CYTB; -.
DR   CTD; 4519; -.
DR   InParanoid; Q8HEC2; -.
DR   Proteomes; UP000008549; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR016174; Di-haem_cyt_TM.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 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..370
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000060702"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        74..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        221..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         80
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:P00163"
FT   BINDING         94
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:P00163"
FT   BINDING         179
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:P00163"
FT   BINDING         193
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:P00163"
FT   BINDING         198
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   VARIANT         54
FT                   /note="P -> S (in strain: JU403, JU439, JU516 and JU793)"
FT                   /evidence="ECO:0000269|PubMed:18302772"
FT   VARIANT         97
FT                   /note="K -> T (in strain: PB800)"
FT                   /evidence="ECO:0000269|PubMed:12644560,
FT                   ECO:0000269|PubMed:18302772"
FT   VARIANT         142
FT                   /note="V -> L (in strain: EG4181)"
FT                   /evidence="ECO:0000269|PubMed:18302772"
FT   VARIANT         205
FT                   /note="S -> I (in strain: JU403, JU439, JU516 and JU793)"
FT                   /evidence="ECO:0000269|PubMed:18302772"
FT   VARIANT         222
FT                   /note="I -> T (in strain: ED3092 and ED3101)"
FT                   /evidence="ECO:0000269|PubMed:18302772"
FT   VARIANT         234
FT                   /note="V -> F (in strain: ED3092 and ED3101)"
FT                   /evidence="ECO:0000269|PubMed:18302772"
FT   VARIANT         257
FT                   /note="P -> L (in strain: HK104)"
FT                   /evidence="ECO:0000269|PubMed:18302772"
FT   VARIANT         297
FT                   /note="F -> V (in strain: JU725)"
FT                   /evidence="ECO:0000269|PubMed:18302772"
FT   VARIANT         317
FT                   /note="L -> W (in strain: JU725)"
FT                   /evidence="ECO:0000269|PubMed:18302772"
FT   VARIANT         321
FT                   /note="F -> L (in strain: PB800)"
FT                   /evidence="ECO:0000269|PubMed:12644560,
FT                   ECO:0000269|PubMed:18302772"
FT   VARIANT         342
FT                   /note="V -> F (in strain: BW287, EG4181, EG4207A, HK104,
FT                   HK105, JU403, JU439, JU516, JU725, JU793, PB800 and PB826)"
FT                   /evidence="ECO:0000269|PubMed:12644560,
FT                   ECO:0000269|PubMed:18302772"
FT   VARIANT         342
FT                   /note="V -> I (in strain: ED3033, ED3034, ED3035, ED3037,
FT                   ED3092, ED3101 and VT847)"
FT                   /evidence="ECO:0000269|PubMed:18302772"
FT   VARIANT         353
FT                   /note="G -> V (in strain: PB826)"
FT                   /evidence="ECO:0000269|PubMed:18302772"
FT   CONFLICT        188
FT                   /note="F -> V (in Ref. 1; AAO13511 and 2; ACB06105/
FT                   ACB06117/ACB06129/ACB06141/ACB06153/ACB06165/ACB06177/
FT                   ACB06189/ACB06201/ACB06213/ACB06225/ACB06237/ACB06249/
FT                   ACB06261/ACB06273/ACB06285/ACB06297/ACB06309/ACB06321/
FT                   ACB06333/ACB06345/ACB06357/ACB06369)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   370 AA;  42442 MW;  998F4A83D21B036F CRC64;
     MKINNSLLNF VNGMLVTLPS SKTLTLSWNF GSMLGMVLVF QIVTGTFLAF YYTPDSLMAF
     STVQYIMYEV NFGWIFRIFH FNGASLFFIF LYLHIFKGLF FMSYRLKKVW MSGLTIYLLV
     MMEAFMGYVL VWAQMSFWAA VVITSLLSVI PIWGPTIVTW IWSGFGVTGA TLKFFFVLHF
     LLPWAILFIV LGHLIFLHST GSTSSLYCHG DYDKVCFSPE YIGKDAYNIV VWLVFIVLSL
     IYPFNLGDAE MFIEADPMMS PVHIVPEWYF LFAYAILRAI PNKVLGVIAL LMSIVTFYFF
     ALVNNYTSCL TKLNKFLVFL FIISSVILSW LGQCMVEDPF TVLSPLFSVI YFGLAYLLLG
     IFMTSKLLFK
 
 
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