ID   CYC22_CAEBR             Reviewed;         135 AA.
AC   A8X769;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Probable cytochrome c 2.2;
GN   Name=cyc-2.2 {ECO:0000312|EMBL:CAP28480.2}; ORFNames=CBG08529;
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:CAP28480.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
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|UniProtKB:P84029}.
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.
CC       {ECO:0000250|UniProtKB:P19974}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000255}.
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DR   EMBL; HE601197; CAP28480.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8X769; -.
DR   SMR; A8X769; -.
DR   STRING; 6238.CBG08529; -.
DR   WormBase; CBG08529; CBP08026; WBGene00030301; Cbr-cyc-2.2.
DR   eggNOG; KOG3453; Eukaryota.
DR   HOGENOM; CLU_060944_3_1_1; -.
DR   InParanoid; A8X769; -.
DR   OMA; YSDAMKN; -.
DR   OrthoDB; 1533604at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
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   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   CHAIN           1..135
FT                   /note="Probable cytochrome c 2.2"
FT                   /id="PRO_0000395330"
FT   BINDING         30
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P19974,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         33
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P19974,
FT                   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:0000250|UniProtKB:P19974,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         101
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:0000250|UniProtKB:P19974,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   135 AA;  14876 MW;  DFBFF159C84D61F9 CRC64;
     MGKKKSDSAS GGAIPEGDYE KGKKIFKQRC EQCHVVNSLQ TKTGPTLNGV IGRQSGQVAG
     FDYSAANKNK GVVWDRQTLF EYLADPKKYI PGTKSYSFFQ MVFAGLKKAD ERADLIKFIE
     VDAAKKPSAY AHHLP