ID CYC_CHICK Reviewed; 105 AA. AC P67881; P00016; Q9PRU4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 126. DE RecName: Full=Cytochrome c; GN Name=CYC; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6324108; DOI=10.1093/nar/11.24.8931; RA Limbach K.J., Wu R.; RT "Isolation and characterization of two alleles of the chicken cytochrome c RT gene."; RL Nucleic Acids Res. 11:8931-8950(1983). RN [2] RP PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2. RC TISSUE=Heart; RX PubMed=5903744; DOI=10.1016/s0021-9258(18)96945-0; RA Chan S.K., Margoliash E.; RT "Amino acid sequence of chicken heart cytochrome c."; RL J. Biol. Chem. 241:507-515(1966). CC -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome CC c heme group can accept an electron from the heme group of the CC cytochrome c1 subunit of cytochrome reductase. Cytochrome c then CC transfers this electron to the cytochrome oxidase complex, the final CC protein carrier in the mitochondrial electron-transport chain. CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely CC associated with the inner membrane. CC -!- PTM: Binds 1 heme c group covalently per subunit. CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of CC November 2006; CC URL="https://web.expasy.org/spotlight/back_issues/076"; 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; K02303; AAA48741.1; -; Genomic_DNA. DR EMBL; X00230; CAA25046.1; -; Genomic_DNA. DR PIR; A00014; CCCH. DR RefSeq; NP_001072946.1; NM_001079478.1. DR RefSeq; XP_015136937.1; XM_015281451.1. DR RefSeq; XP_015136938.1; XM_015281452.1. DR RefSeq; XP_015136939.1; XM_015281453.1. DR AlphaFoldDB; P67881; -. DR SMR; P67881; -. DR STRING; 9031.ENSGALP00000017934; -. DR iPTMnet; P67881; -. DR PaxDb; 9031-ENSGALP00000017934; -. DR Ensembl; ENSGALT00000134828; ENSGALP00000082349; ENSGALG00000011020. DR Ensembl; ENSGALT00010005531.1; ENSGALP00010003370.1; ENSGALG00010002409.1. DR Ensembl; ENSGALT00015002702; ENSGALP00015001718; ENSGALG00015001283. DR GeneID; 420624; -. DR KEGG; gga:420624; -. DR CTD; 54205; -. DR VEuPathDB; HostDB:geneid_420624; -. DR eggNOG; KOG3453; Eukaryota. DR GeneTree; ENSGT00390000009405; -. DR HOGENOM; CLU_060944_3_0_1; -. DR InParanoid; P67881; -. DR OMA; WGCPASE; -. DR OrthoDB; 4150at2759; -. DR PhylomeDB; P67881; -. DR Reactome; R-GGA-111457; Release of apoptotic factors from the mitochondria. DR Reactome; R-GGA-111458; Formation of apoptosome. DR Reactome; R-GGA-111459; Activation of caspases through apoptosome-mediated cleavage. DR Reactome; R-GGA-3299685; Detoxification of Reactive Oxygen Species. DR Reactome; R-GGA-5620971; Pyroptosis. DR Reactome; R-GGA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-GGA-611105; Respiratory electron transport. DR Reactome; R-GGA-9627069; Regulation of the apoptosome activity. DR Reactome; R-GGA-9707564; Cytoprotection by HMOX1. DR PRO; PR:P67881; -. DR Proteomes; UP000000539; Chromosome 2. DR Bgee; ENSGALG00000011020; Expressed in heart and 14 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:AgBase. DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:AgBase. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central. DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR036909; Cyt_c-like_dom_sf. DR InterPro; IPR002327; Cyt_c_1A/1B. DR PANTHER; PTHR11961; CYTOCHROME C; 1. DR PANTHER; PTHR11961:SF12; CYTOCHROME C; 1. DR Pfam; PF00034; Cytochrom_C; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR SUPFAM; SSF46626; Cytochrome c; 1. DR PROSITE; PS51007; CYTC; 1. PE 1: Evidence at protein level; KW Acetylation; Direct protein sequencing; Electron transport; Heme; Iron; KW Metal-binding; Mitochondrion; Reference proteome; Respiratory chain; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:5903744" FT CHAIN 2..105 FT /note="Cytochrome c" FT /id="PRO_0000108239" FT BINDING 15 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, FT ECO:0000269|PubMed:5903744" FT BINDING 18 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, FT ECO:0000269|PubMed:5903744" FT BINDING 19 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT BINDING 81 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0000269|PubMed:5903744" SQ SEQUENCE 105 AA; 11711 MW; 293CEF5B11DABC36 CRC64; MGDIEKGKKI FVQKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAEGFSYT DANKNKGITW GEDTLMEYLE NPKKYIPGTK MIFAGIKKKS ERVDLIAYLK DATSK //