CYB_PHOVI
ID CYB_PHOVI Reviewed; 379 AA.
AC Q00530; Q35682;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 104.
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 Phoca vitulina (Harbor seal).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Phoca.
OX NCBI_TaxID=9720;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1593642; DOI=10.1007/bf00160463;
RA Arnason U., Johnsson E.;
RT "The complete mitochondrial DNA sequence of the harbor seal, Phoca
RT vitulina.";
RL J. Mol. Evol. 34:493-505(1992).
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).
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; X63726; CAA45269.1; -; Genomic_DNA.
DR EMBL; X82306; CAA57749.1; -; Genomic_DNA.
DR PIR; S26163; S26163.
DR RefSeq; NP_006940.1; NC_001325.1.
DR AlphaFoldDB; Q00530; -.
DR SMR; Q00530; -.
DR GeneID; 807661; -.
DR CTD; 4519; -.
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_0000061393"
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 15
FT /note="D -> N (in Ref. 1; CAA45269)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="S -> L (in Ref. 1; CAA45269)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="A -> D (in Ref. 1; CAA45269)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="N -> D (in Ref. 1; CAA45269)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="A -> P (in Ref. 1; CAA45269)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="I -> V (in Ref. 1; CAA45269)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="V -> M (in Ref. 1; CAA45269)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="I -> V (in Ref. 1; CAA45269)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="M -> T (in Ref. 1; CAA45269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42636 MW; 4AB8BAEA07ABB185 CRC64;
MTNIRKTHPL MKIIDNSFID LPTPSNISAW WNFGSLLGIC LILQILTGLF LAMHYTSDTT
TAFSSVTHIC RDVNYGWIIR YLHANGASMF FICLYMHVGR GLYYGSYTFT ETWNIGIILL
FTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYVGTDL VQWIWGGFSV DKATLTRFFA
FHFILPFVVS ALAAVHLLFL HETGSNNPSG IMSNSDKIPF HPYYTIKDIL GALLLILVLT
LLVLFSPDLL GDPDNYIPAN PLSTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSILI
LAIVPLLHTS KQRGMMFRPI SQCLFWFLVA DLLTLTWIGG QPVEHPYITI GQLASILYFM
ILLVLMPIAS IIENNILKW
