CYC21_CAEEL
ID CYC21_CAEEL Reviewed; 111 AA.
AC P19974; O44479;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cytochrome c 2.1;
GN Name=cyc-2.1; ORFNames=E04A4.7;
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).
RN [2]
RP PROTEIN SEQUENCE OF 2-111, AND ACETYLATION AT SER-2.
RC STRAIN=Bristol N2;
RX PubMed=2173902; DOI=10.1042/bj2710613;
RA Vanfleteren J.R., Evers E.A.I.M., van de Werken G., van Beeumen J.J.;
RT "The primary structure of cytochrome c from the nematode Caenorhabditis
RT elegans.";
RL Biochem. J. 271:613-620(1990).
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";
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DR EMBL; FO081039; CCD68708.1; -; Genomic_DNA.
DR PIR; T32611; T32611.
DR RefSeq; NP_500629.1; NM_068228.5.
DR AlphaFoldDB; P19974; -.
DR SMR; P19974; -.
DR BioGRID; 42372; 36.
DR STRING; 6239.E04A4.7.1; -.
DR iPTMnet; P19974; -.
DR EPD; P19974; -.
DR PaxDb; P19974; -.
DR PeptideAtlas; P19974; -.
DR EnsemblMetazoa; E04A4.7.1; E04A4.7.1; WBGene00017121.
DR EnsemblMetazoa; E04A4.7.2; E04A4.7.2; WBGene00017121.
DR WormBase; E04A4.7; CE16968; WBGene00017121; cyc-2.1.
DR eggNOG; KOG3453; Eukaryota.
DR GeneTree; ENSGT00940000168884; -.
DR HOGENOM; CLU_060944_3_1_1; -.
DR InParanoid; P19974; -.
DR OrthoDB; 1533604at2759; -.
DR PhylomeDB; P19974; -.
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 PRO; PR:P19974; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00017121; Expressed in embryo and 4 other tissues.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0070469; C:respirasome; IC:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IC:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
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 GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR Gene3D; 1.10.760.10; -; 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; PTHR11961; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; SSF46626; 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:2173902"
FT CHAIN 2..111
FT /note="Cytochrome c 2.1"
FT /id="PRO_0000108271"
FT BINDING 20
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:2173902"
FT BINDING 23
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:2173902"
FT BINDING 24
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 85
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-acetylserine"
FT /evidence="ECO:0000269|PubMed:2173902"
FT CONFLICT 66
FT /note="K -> R (in Ref. 1; CCD68708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 111 AA; 12233 MW; D4161D25AC5EBEDB CRC64;
MSDIPAGDYE KGKKVYKQRC LQCHVVDSTA TKTGPTLHGV IGRTSGTVSG FDYSAANKNK
GVVWTKETLF EYLLNPKKYI PGTKMVFAGL KKADERADLI KYIEVESAKS L
