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CYB_SUSVE
ID   CYB_SUSVE               Reviewed;         379 AA.
AC   Q8M700; Q8M701;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 77.
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   Sus verrucosus (Javan warty pig).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=159856;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate Sve1, and Isolate Sve2;
RA   Randi E., d'Huart J.P., Lucchini V., Aman R.;
RT   "Evidence of two genetically deeply divergent species of warthog,
RT   Phacochoerus africanus and P. aethiopicus (Artiodactyla: Suiformes) in East
RT   Africa.";
RL   Submitted (MAY-2001) 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   -!- 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; AJ314552; CAC85253.1; -; Genomic_DNA.
DR   EMBL; AJ314553; CAC85254.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8M700; -.
DR   SMR; Q8M700; -.
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_0000254766"
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         281
FT                   /note="L -> V (in strain: Isolate Sve2)"
SQ   SEQUENCE   379 AA;  42790 MW;  CD23D4FB4A807824 CRC64;
     MTNIRKSHPL MKIINNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTT
     TAFSSVTHIC RDVNYGWLIR YLHANGASMF FICLFIHVGR GLYYGSYMFL ETWNIGVILL
     FTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VEWIWGGFSV DKATLTRFFA
     FHFILPFVIT ALAAVHLLFL HETGSNNPTG IPSDMDKIPF HPYYTIKDIL GALFMMLILL
     ILVLFSPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLAVVTSILI
     LILMPMLHTS KQRSMMFRPV SQCLFWMVVA DLITLTWIGG QPVEHPLIII GQLASILYFL
     IILVLMPITS IIENNLLKW
 
 
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