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CYB_CORCX
ID   CYB_CORCX               Reviewed;         308 AA.
AC   P92600; Q9B7H8; Q9B7H9; Q9B7I0; Q9B7I1; Q9B7I2; Q9B7I3; Q9G242; Q9G243;
AC   Q9G245; Q9G3J1; Q9G3J2; Q9G3J3; Q9G3J5;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 98.
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;
DE   Flags: Fragment;
GN   Name=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS   Corvus corax (Common raven).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=56781;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Cibois A., Pasquet E.;
RT   "Molecular analysis of the phylogeny of 11 genera of the Corvidae.";
RL   Ibis 141:297-306(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
RC   STRAIN=Isolate California-168, Isolate California-169,
RC   Isolate California-170, Isolate California-171, Isolate California-175,
RC   Isolate California-176, Isolate Idaho-1, Isolate Idaho-10,
RC   Isolate Idaho-11, Isolate Idaho-12, Isolate Idaho-2, Isolate Idaho-7,
RC   Isolate Idaho-8, Isolate Maine-1, Isolate Maine-2, Isolate Maine-3,
RC   Isolate New Mexico-522, Isolate New Mexico-523, Isolate Siberia-566,
RC   Isolate Washington-567, Isolate Washington-899, Isolate Washington-HAN, and
RC   Isolate Washington-SOA;
RX   PubMed=11197122; DOI=10.1098/rspb.2000.1308;
RA   Omland K.E., Tarr C.L., Boarman W.I., Marzluff J.M., Fleischer R.C.;
RT   "Cryptic genetic variation and paraphyly in ravens.";
RL   Proc. R. Soc. B 267:2475-2482(2000).
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; U86031; AAB47508.1; -; Genomic_DNA.
DR   EMBL; AY005933; AAF99344.1; -; Genomic_DNA.
DR   EMBL; AY005934; AAF99345.1; -; Genomic_DNA.
DR   EMBL; AY005935; AAF99346.1; -; Genomic_DNA.
DR   EMBL; AY005936; AAF99347.1; -; Genomic_DNA.
DR   EMBL; AY005937; AAF99348.1; -; Genomic_DNA.
DR   EMBL; AY005938; AAF99349.2; -; Genomic_DNA.
DR   EMBL; AY005939; AAF99350.1; -; Genomic_DNA.
DR   EMBL; AY005940; AAF99351.1; -; Genomic_DNA.
DR   EMBL; AY005945; AAF99356.1; -; Genomic_DNA.
DR   EMBL; AY005946; AAF99357.1; -; Genomic_DNA.
DR   EMBL; AY005948; AAF99359.1; -; Genomic_DNA.
DR   EMBL; AY005949; AAF99360.1; -; Genomic_DNA.
DR   EMBL; AY005950; AAF99361.1; -; Genomic_DNA.
DR   EMBL; AY005951; AAF99362.1; -; Genomic_DNA.
DR   EMBL; AY005952; AAF99363.2; -; Genomic_DNA.
DR   EMBL; AY005953; AAF99364.2; -; Genomic_DNA.
DR   EMBL; AY005961; AAF99372.1; -; Genomic_DNA.
DR   EMBL; AY005962; AAF99373.1; -; Genomic_DNA.
DR   EMBL; AY005965; AAF99376.2; -; Genomic_DNA.
DR   EMBL; AY005967; AAF99378.1; -; Genomic_DNA.
DR   EMBL; AY005969; AAF99380.2; -; Genomic_DNA.
DR   EMBL; AY005972; AAF99383.1; -; Genomic_DNA.
DR   EMBL; AY005973; AAF99384.2; -; Genomic_DNA.
DR   AlphaFoldDB; P92600; -.
DR   SMR; P92600; -.
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; Respiratory chain; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           <1..>308
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000060810"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        45..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         51
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         65
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         150
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         164
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         169
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   VARIANT         32
FT                   /note="T -> A (in strain: Isolate California-168, Isolate
FT                   California-169, Isolate California-170, Isolate California-
FT                   171, Isolate California-175, Isolate California-176,
FT                   Isolate Idaho-1, Isolate Idaho-2, Isolate Idaho-7, Isolate
FT                   Idaho-8, Isolate Idaho-10, Isolate Idaho-11, Isolate Idaho-
FT                   12, Isolate Washington-899 and Isolate Washington-SOA)"
FT   VARIANT         40
FT                   /note="N -> D (in strain: Isolate California-168, Isolate
FT                   California-169, Isolate California-170, Isolate California-
FT                   171, Isolate California-175, Isolate California-176,
FT                   Isolate Idaho-1, Isolate Idaho-2, Isolate Idaho-7, Isolate
FT                   Idaho-8, Isolate Idaho-10, Isolate Idaho-11, Isolate Idaho-
FT                   12, Isolate Washington-899 and Isolate Washington-SOA)"
FT   VARIANT         70
FT                   /note="I -> F (in strain: Isolate New Mexico-523)"
FT   VARIANT         97
FT                   /note="V -> L (in strain: Isolate Washington-SOA)"
FT   VARIANT         100
FT                   /note="V -> F (in strain: Isolate New Mexico-522)"
FT   NON_TER         1
FT   NON_TER         308
SQ   SEQUENCE   308 AA;  34358 MW;  8ECED874C4D853A5 CRC64;
     FGSLLGLCLI TQIITGLLLA MHYTADTSLA FTSVAHMCRN VQFGWLIRNL HANGASFFFI
     CIYLHIGRGI YYGSYLNKET WNIGVILLLT LMATAFVGYV LPWGQMSFWG ATVITNLFSA
     IPYIGQTLVE WLWGGFSVDN PTLTRFFAFH FLLPFVIAGL TLVHLTFLHE TGSNNPLGIP
     SDCDKIPFHP YYSIKDLLGF ALMLIPLITL ALFSPNLLGD PENFTPANPL ATPPHIKPEW
     YFLFAYAILR SIPNKLGGVL ALAASVLILF LIPLLHVSKQ RSMTFRPLSQ ILFWTLVADL
     LILTWVGS
 
 
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