CYB_PONPY
ID CYB_PONPY Reviewed; 380 AA.
AC Q35614; P92723; Q7GIM5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 112.
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 Pongo pygmaeus (Bornean orangutan).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=7477403; DOI=10.1038/378485a0;
RA Collura R.V., Stewart C.-B.R.;
RT "Insertions and duplications of mtDNA in the nuclear genomes of Old World
RT monkeys and hominoids.";
RL Nature 378:485-489(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7530363; DOI=10.1073/pnas.92.2.532;
RA Horai S., Hayasaka K., Kondo R., Tsugane K., Takahata N.;
RT "Recent African origin of modern humans revealed by complete sequences of
RT hominoid mitochondrial DNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:532-536(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate Anna;
RX PubMed=8875856; DOI=10.1007/bf02337514;
RA Xu X., Arnason U.;
RT "The mitochondrial DNA molecule of Sumatran orangutan and a molecular
RT proposal for two (Bornean and Sumatran) species of orangutan.";
RL J. Mol. Evol. 43:431-437(1996).
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; U38274; AAA98463.1; -; Genomic_DNA.
DR EMBL; D38115; BAA85293.1; -; Genomic_DNA.
DR EMBL; X97717; CAA66303.1; -; Genomic_DNA.
DR RefSeq; NP_008237.1; NC_001646.1.
DR AlphaFoldDB; Q35614; -.
DR SMR; Q35614; -.
DR GeneID; 807904; -.
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..380
FT /note="Cytochrome b"
FT /id="PRO_0000061434"
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 3..4
FT /note="PM -> ST (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="T -> S (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="H -> R (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 45..46
FT /note="TI -> IT (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="T -> S (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="L -> F (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="I -> V (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="V -> I (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="T -> S (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="T -> M (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="T -> A (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="V -> I (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="G -> S (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="V -> T (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 368..369
FT /note="TS -> AF (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="Y -> H (in Ref. 1; AAA98463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42865 MW; 102BF5E0CE294CDB CRC64;
MTPMRKTNPL MKLINHSLID LPTPSNISAW WNFGSLLGAC LIIQTITGLF LAMHYSPDAT
TAFSSIAHIT RDVNYGWMIR HLHANGASML FICLFLHIGR GLYYGSFTHL ETWNIGIILL
FMTMMTAFMG YVLPWGQMSF WGATVITNLL SAVPYIGTDL VQWVWGGYSV NSPTLTRFFT
LHFMLPFIIT ALTTLHLLFL HETGSNNPLG IPSHSDKITF HPYYTIKDIL GLLLFLLALM
TLTLLSPDLL SDPDNYTLAN PLSTPPHIKP EWYFLFAYAI LRSVPNKLGG VMALMLSILI
LTTIPALHTS KQQSMTFRPL SQFLYWLLIT DLLVLTWIGG QPVSYPFITI GQVASVLYFT
TILLLMPTSS LIENYMLKWT
