CYB_PANOS
ID CYB_PANOS Reviewed; 372 AA.
AC Q9G210; Q9G167; Q9G1B2; Q9G1B3; Q9G1B4; Q9G1R9; Q9G1Z8; Q9G965; Q9G966;
AC Q9G967; Q9G968; Q9G969; Q9G970; Q9G971; Q9G972; Q9G973; Q9G974; Q9G975;
AC Q9G976; Q9G977; Q9G978;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Pantherophis obsoletus (Black ratsnake) (Elaphe obsoleta).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Colubrinae; Pantherophis.
OX NCBI_TaxID=39099;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11209786; DOI=10.1554/0014-3820(2000)054[2107:mdpotp]2.0.co;2;
RA Burbrink F.T., Lawson R., Slowinski J.B.;
RT "Mitochondrial DNA phylogeography of the polytypic North American rat snake
RT (Elaphe obsoleta): a critique of the subspecies concept.";
RL Evolution 54:2107-2118(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 3 respiratory subunits
CC (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and
CC probably 6 low-molecular weight proteins.
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; AF283577; AAG26393.1; -; Genomic_DNA.
DR EMBL; AF283578; AAG26394.1; -; Genomic_DNA.
DR EMBL; AF283579; AAG26395.1; -; Genomic_DNA.
DR EMBL; AF283580; AAG26396.1; -; Genomic_DNA.
DR EMBL; AF283581; AAG26397.1; -; Genomic_DNA.
DR EMBL; AF283582; AAG26398.1; -; Genomic_DNA.
DR EMBL; AF283583; AAG26399.1; -; Genomic_DNA.
DR EMBL; AF283584; AAG26400.1; -; Genomic_DNA.
DR EMBL; AF283585; AAG26401.1; -; Genomic_DNA.
DR EMBL; AF283586; AAG26402.1; -; Genomic_DNA.
DR EMBL; AF283587; AAG26403.1; -; Genomic_DNA.
DR EMBL; AF283588; AAG26404.1; -; Genomic_DNA.
DR EMBL; AF283589; AAG26405.1; -; Genomic_DNA.
DR EMBL; AF283590; AAG26406.1; -; Genomic_DNA.
DR EMBL; AF283591; AAG26407.1; -; Genomic_DNA.
DR EMBL; AF283592; AAG26408.1; -; Genomic_DNA.
DR EMBL; AF283593; AAG26409.1; -; Genomic_DNA.
DR EMBL; AF283594; AAG26410.1; -; Genomic_DNA.
DR EMBL; AF283595; AAG26411.1; -; Genomic_DNA.
DR EMBL; AF283596; AAG26412.1; -; Genomic_DNA.
DR EMBL; AF283597; AAG26413.1; -; Genomic_DNA.
DR EMBL; AF283601; AAG26417.1; -; Genomic_DNA.
DR EMBL; AF283602; AAG26418.1; -; Genomic_DNA.
DR EMBL; AF283603; AAG26419.1; -; Genomic_DNA.
DR EMBL; AF283604; AAG26420.1; -; Genomic_DNA.
DR EMBL; AF283605; AAG26421.1; -; Genomic_DNA.
DR EMBL; AF283606; AAG26422.1; -; Genomic_DNA.
DR EMBL; AF283607; AAG26423.1; -; Genomic_DNA.
DR EMBL; AF283608; AAG26424.1; -; Genomic_DNA.
DR EMBL; AF283609; AAG26425.1; -; Genomic_DNA.
DR EMBL; AF283610; AAG26426.1; -; Genomic_DNA.
DR EMBL; AF283611; AAG26427.1; -; Genomic_DNA.
DR EMBL; AF283612; AAG26428.1; -; Genomic_DNA.
DR EMBL; AF283613; AAG26429.1; -; Genomic_DNA.
DR EMBL; AF283614; AAG26430.1; -; Genomic_DNA.
DR EMBL; AF283615; AAG26431.1; -; Genomic_DNA.
DR EMBL; AF283616; AAG26432.1; -; Genomic_DNA.
DR EMBL; AF283617; AAG26433.1; -; Genomic_DNA.
DR EMBL; AF283618; AAG26434.1; -; Genomic_DNA.
DR EMBL; AF283619; AAG26435.1; -; Genomic_DNA.
DR EMBL; AF283620; AAG26436.1; -; Genomic_DNA.
DR EMBL; AF283621; AAG26437.1; -; Genomic_DNA.
DR EMBL; AF283623; AAG26439.1; -; Genomic_DNA.
DR EMBL; AF283624; AAG26440.1; -; Genomic_DNA.
DR EMBL; AF283625; AAG26441.1; -; Genomic_DNA.
DR EMBL; AF283626; AAG26442.1; -; Genomic_DNA.
DR EMBL; AF283627; AAG26443.1; -; Genomic_DNA.
DR EMBL; AF283628; AAG26444.1; -; Genomic_DNA.
DR EMBL; AF283629; AAG26445.1; -; Genomic_DNA.
DR EMBL; AF283630; AAG26446.1; -; Genomic_DNA.
DR EMBL; AF283631; AAG26447.1; -; Genomic_DNA.
DR EMBL; AF283632; AAG26448.1; -; Genomic_DNA.
DR EMBL; AF283633; AAG26449.1; -; Genomic_DNA.
DR EMBL; AF283634; AAG26450.1; -; Genomic_DNA.
DR EMBL; AF283635; AAG26451.1; -; Genomic_DNA.
DR EMBL; AF283637; AAG26453.1; -; Genomic_DNA.
DR EMBL; AF283640; AAG26456.1; -; Genomic_DNA.
DR EMBL; AF283641; AAG26457.1; -; Genomic_DNA.
DR EMBL; AF283642; AAG26458.1; -; Genomic_DNA.
DR EMBL; AF283643; AAG26459.1; -; Genomic_DNA.
DR EMBL; AF283644; AAG26460.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9G210; -.
DR SMR; Q9G210; -.
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..372
FT /note="Cytochrome b"
FT /id="PRO_0000060908"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 69..90
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 339..358
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 75
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 89
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 174
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 188
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 193
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT VARIANT 2
FT /note="S -> P"
FT VARIANT 8
FT /note="L -> M"
FT VARIANT 23
FT /note="W -> G"
FT VARIANT 38
FT /note="M -> T"
FT VARIANT 103
FT /note="N -> S"
FT VARIANT 110
FT /note="T -> M"
FT VARIANT 148
FT /note="I -> M"
FT VARIANT 218
FT /note="H -> Y"
FT VARIANT 226
FT /note="I -> M"
FT VARIANT 226
FT /note="I -> T"
FT VARIANT 230
FT /note="A -> T"
FT VARIANT 236
FT /note="S -> F"
FT VARIANT 238
FT /note="M -> T"
FT VARIANT 245
FT /note="P -> S"
FT VARIANT 298
FT /note="F -> Y"
FT VARIANT 304
FT /note="F -> M"
FT VARIANT 308
FT /note="T -> M"
FT VARIANT 315
FT /note="F -> L"
FT VARIANT 319
FT /note="T -> A"
FT VARIANT 320
FT /note="L -> M"
FT VARIANT 324
FT /note="F -> L"
FT VARIANT 335
FT /note="V -> M"
FT VARIANT 345
FT /note="A -> V"
FT VARIANT 348
FT /note="I -> S"
FT VARIANT 352
FT /note="T -> M"
SQ SEQUENCE 372 AA; 42345 MW; 4342428FD1DDEC06 CRC64;
MSNQHMLLLF NLLPVGSNIS TWWNFGSMLL TCLALQTMTG FFLAIHYTAN INLAFSSIVH
ITRDVPYGWM MQNLHAIGAS MFFICIYIHI ARGLYYGSFL NKNVWLSGTT LLIILMATAF
FGYVLPWGQM SFWAATVITN LLTAVPYIGT ELTNWLWGGF SINDPTLTRF FALHFILPFT
IISMSSIHIM LLHTEGSSNP LGTNSDIDKI PFHPYHSHKD MLMLTIMMTA LFIIMSFMPN
IFNDPENFSK ANPLVTPQHI KPEWYFLFAY GILRSIPNKL GGTVALVLSV TILMTMPFTH
TSHFRSMTFR PLMQFMFWTL VATFITITWA ATKPVEPPFT TIGQATAILY FTFFIMNPLL
GWLENKISIT NM
