ID   CYC21_CAEBR             Reviewed;         112 AA.
AC   A8WQY3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Cytochrome c 2.1;
GN   Name=cyc-2.1 {ECO:0000312|EMBL:CAP22891.1}; ORFNames=CBG01744;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP22891.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP22891.1};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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:0000255}.
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DR   EMBL; HE601298; CAP22891.1; -; Genomic_DNA.
DR   RefSeq; XP_002634176.1; XM_002634130.1.
DR   AlphaFoldDB; A8WQY3; -.
DR   SMR; A8WQY3; -.
DR   STRING; 6238.CBG01744; -.
DR   EnsemblMetazoa; CBG01744.1; CBG01744.1; WBGene00024932.
DR   GeneID; 8576171; -.
DR   KEGG; cbr:CBG_01744; -.
DR   CTD; 8576171; -.
DR   WormBase; CBG01744; CBP06075; WBGene00024932; Cbr-cyc-2.1.
DR   eggNOG; KOG3453; Eukaryota.
DR   HOGENOM; CLU_060944_3_1_1; -.
DR   InParanoid; A8WQY3; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
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; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; ISS: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   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Reference proteome; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P19974"
FT   CHAIN           2..112
FT                   /note="Cytochrome c 2.1"
FT                   /id="PRO_0000358600"
FT   BINDING         20
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         23
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   112 AA;  12341 MW;  EE81E9B55729310C CRC64;
     MADIPAGDYE KGKKVYKQRC LQCHVVDSTA TKTGPTLYGV IGRTSGTVAG FDYSAANKSK
     GVVWTRETLF EYLLNPKKYI PGTKMVFAGL KKADERADLI KYIEVECSKP LA