ID A0A8G1GKW2_GIRCA Unreviewed; 379 AA. AC A0A8G1GKW2; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 29-MAY-2024, entry version 8. DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117}; GN Name=cytb {ECO:0000313|EMBL:QZA73764.1}; OS Giraffa camelopardalis camelopardalis (Nubian giraffe). OG Mitochondrion {ECO:0000313|EMBL:QZA73764.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Giraffidae; OC Giraffa. OX NCBI_TaxID=1870831 {ECO:0000313|EMBL:QZA73764.1}; RN [1] {ECO:0000313|EMBL:QZA73764.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZGA2 {ECO:0000313|EMBL:QZA73764.1}; RA Sanil R.P., Backer S.J., George N.; RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QZA73764.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZGA2 {ECO:0000313|EMBL:QZA73764.1}; RA Kulkarni T.P.; RT "This is Cytochrome b (CYTB) sequence of Nubian Giraffe at Zoological RT Garden Alipore, Kolkata India."; RL Submitted (AUG-2021) 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:0000256|ARBA:ARBA00002566, CC ECO:0000256|RuleBase:RU362117}. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|RuleBase:RU362117}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|RuleBase:RU362117}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR038885-2}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|PIRSR:PIRSR038885-2}; 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:0000256|ARBA:ARBA00011088}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004448}. CC -!- SIMILARITY: Belongs to the cytochrome b family. CC {ECO:0000256|RuleBase:RU362117}. 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; MW991403; QZA73764.1; -; Genomic_DNA. DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:TreeGrafter. DR CDD; cd00290; cytochrome_b_C; 1. DR CDD; cd00284; Cytochrome_b_N; 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; IPR048260; Cytochrome_b_C_euk/bac. DR InterPro; IPR048259; Cytochrome_b_N_euk/bac. DR InterPro; IPR016174; Di-haem_cyt_TM. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF038885; COB; 1. DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU362117}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038885-2}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038885-2}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362117}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR038885-2}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU362117}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU362117}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU362117}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU362117}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362117}; KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}. FT TRANSMEM 30..52 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 87..107 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 113..133 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 140..158 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 178..200 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 221..245 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 288..307 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 319..340 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 346..368 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT DOMAIN 1..209 FT /note="Cytochrome b/b6 N-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 210..379 FT /note="Cytochrome b/b6 C-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51003" 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:0000256|PIRSR:PIRSR038885-2" 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:0000256|PIRSR:PIRSR038885-2" 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:0000256|PIRSR:PIRSR038885-2" 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:0000256|PIRSR:PIRSR038885-2" FT BINDING 201 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1" SQ SEQUENCE 379 AA; 42875 MW; 7E9F724DD54F21D9 CRC64; MINIRKSHPL MKIVNNALID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTPDTT TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLFMHMGR GLYYGSYTFL ETWNIGVILL FTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTNM VEWIWGGFSV DKATLTRFFA FHFILPFIIM ALTMVHLLFL HETGSNNPMG IPSDMDKIPF HPYYTIKDIL GALLLILVLM LLVLFTPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALISSILI LALMPLLHTS KQRSMTFRPL SQCLFWILVA DLLTLTWIGG QPVEHPFIII GQLASIMYFL IILVLMPITS AIENNLLKW //