CYB_ORYSJ
ID CYB_ORYSJ Reviewed; 397 AA.
AC P0C524; P14833; P92682; Q35293;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Oryza sativa subsp. japonica (Rice).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND RNA EDITING.
RC STRAIN=cv. Nipponbare, and cv. Taichung 65; TISSUE=Shoot;
RX PubMed=8752869; DOI=10.1266/ggs.71.85;
RA Ito Y., Nakazono M., Kadowaki K., Tsutsumi N., Hirai A.;
RT "RNA editing of transcripts of the gene for apocytochrome b (cob) in rice
RT mitochondria.";
RL Genes Genet. Syst. 71:85-89(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12471441; DOI=10.1007/s00438-002-0767-1;
RA Notsu Y., Masood S., Nishikawa T., Kubo N., Akiduki G., Nakazono M.,
RA Hirai A., Kadowaki K.;
RT "The complete sequence of the rice (Oryza sativa L.) mitochondrial genome:
RT frequent DNA sequence acquisition and loss during the evolution of
RT flowering plants.";
RL Mol. Genet. Genomics 268:434-445(2002).
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:P00163}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P00163};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:P00163};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00163}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00163}.
CC -!- RNA EDITING: Modified_positions=60 {ECO:0000269|PubMed:8752869}, 96
CC {ECO:0000269|PubMed:8752869}, 100 {ECO:0000269|PubMed:8752869}, 109
CC {ECO:0000269|PubMed:8752869}, 140 {ECO:0000269|PubMed:8752869}, 190
CC {ECO:0000269|PubMed:8752869}, 194 {ECO:0000269|PubMed:8752869}, 227
CC {ECO:0000269|PubMed:8752869}, 239 {ECO:0000269|PubMed:8752869}, 242
CC {ECO:0000269|PubMed:8752869}, 270 {ECO:0000269|PubMed:8752869}, 285
CC {ECO:0000269|PubMed:8752869}, 303 {ECO:0000269|PubMed:8752869}, 328
CC {ECO:0000269|PubMed:8752869}, 361 {ECO:0000269|PubMed:8752869}, 375
CC {ECO:0000269|PubMed:8752869};
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 protein contains only eight transmembrane helices, not
CC nine as predicted by bioinformatics tools.
CC {ECO:0000250|UniProtKB:P00163}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53710; CAA37747.1; ALT_SEQ; Genomic_DNA.
DR EMBL; D83009; BAA11679.1; -; mRNA.
DR EMBL; BA000029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; YP_002000585.1; NC_011033.1.
DR AlphaFoldDB; P0C524; -.
DR SMR; P0C524; -.
DR STRING; 39947.P0C524; -.
DR PaxDb; P0C524; -.
DR PRIDE; P0C524; -.
DR GeneID; 6450178; -.
DR KEGG; osa:6450178; -.
DR InParanoid; P0C524; -.
DR OrthoDB; 1125966at2759; -.
DR Proteomes; UP000059680; Mitochondrion.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IC:Gramene.
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 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW RNA editing; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..397
FT /note="Cytochrome b"
FT /id="PRO_0000290118"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 82..104
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT BINDING 88
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:P00163"
FT BINDING 102
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:P00163"
FT BINDING 189
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:P00163"
FT BINDING 203
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:P00163"
FT BINDING 208
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
SQ SEQUENCE 397 AA; 44907 MW; 59DC5B6447D42A42 CRC64;
MTIRNQRFSL LKQPIYSTLN QHLIDYPTPS NLSYWWGFGS LAGICLVIQI VTGVFLAMHY
TPHVDLAFNS VEHIMRDVEG GWLLRYMHAN GASMFFIVVY LHIFRGLYYA SYSSPREFVW
CLGVVIFLLM IVTAFIGYVL PWGQMSFWGA TVITSLASAI PVVGDTIVTW LWGGFSVDNA
TLNRFFSLHY LLPFILVGAS LLHLAALHQY GSNNPLGVHS EMDKIAFYPY FYVKDLVGWV
AFAIFFSIWI FFAPNVLGHP DNYIPANPMS TPPHIVPEWY FLPIYAILRS IPDKAGGVAA
IALVFISLLA LPFFKEMYVR SSSFRPIYQG IFWLLLADCL LLGWIGCQPV EAPFVTIGQI
SSFFFFLFFA ITPILGRVGR GIPKYYTDET HRTGSVS
