ID CYC22_CAEEL Reviewed; 123 AA. AC Q23240; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 165. DE RecName: Full=Probable cytochrome c 2.2; GN Name=cyc-2.2; ORFNames=ZC116.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). 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 (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}. CC Note=Loosely associated with the inner membrane. {ECO:0000250}. CC -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000250}. 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; Z74046; CAA98555.1; -; Genomic_DNA. DR PIR; T27492; T27492. DR RefSeq; NP_506156.1; NM_073755.3. DR AlphaFoldDB; Q23240; -. DR SMR; Q23240; -. DR BioGRID; 44748; 12. DR STRING; 6239.ZC116.2.1; -. DR EPD; Q23240; -. DR PaxDb; 6239-ZC116-2; -. DR PeptideAtlas; Q23240; -. DR EnsemblMetazoa; ZC116.2.1; ZC116.2.1; WBGene00013854. DR GeneID; 179728; -. DR KEGG; cel:CELE_ZC116.2; -. DR AGR; WB:WBGene00013854; -. DR WormBase; ZC116.2; CE06565; WBGene00013854; cyc-2.2. DR eggNOG; KOG3453; Eukaryota. DR GeneTree; ENSGT00940000168884; -. DR HOGENOM; CLU_060944_3_1_1; -. DR InParanoid; Q23240; -. DR OMA; MPAPYKK; -. DR OrthoDB; 4150at2759; -. DR PhylomeDB; Q23240; -. DR Reactome; R-CEL-111457; Release of apoptotic factors from the mitochondria. DR Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species. DR Reactome; R-CEL-5620971; Pyroptosis. DR Reactome; R-CEL-611105; Respiratory electron transport. DR PRO; PR:Q23240; -. DR Proteomes; UP000001940; Chromosome V. DR Bgee; WBGene00013854; Expressed in adult organism and 1 other cell type or tissue. DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central. 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 3: Inferred from homology; KW Electron transport; Heme; Iron; Metal-binding; Mitochondrion; KW Reference proteome; Respiratory chain; Transport. FT CHAIN 1..123 FT /note="Probable cytochrome c 2.2" FT /id="PRO_0000108272" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 30 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT BINDING 33 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT BINDING 34 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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT BINDING 95 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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" SQ SEQUENCE 123 AA; 13362 MW; 6FBC24AF847F596C CRC64; MGKKKSDTAS GGAIPEGDNE KGKKIFKQRC EQCHVVNSLQ TKTGPTLNGV IGRQSGQVAG FDYSAANKNK GVVWDRQTLF DYLADPKKYI PGTKMVFAGL KKADERADLI KFIEVEAAKK PSA //