ID   CYC_CHLRE               Reviewed;         112 AA.
AC   P15451;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Cytochrome c;
GN   Name=CYC1;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=137c / CC-125, and cw15;
RX   PubMed=2853233; DOI=10.1007/bf02143507;
RA   Amati B.B., Goldschmidt-Clermont M., Wallace C.J.A., Rochaix J.-D.;
RT   "cDNA and deduced amino acid sequences of cytochrome c from Chlamydomonas
RT   reinhardtii: unexpected functional and phylogenetic implications.";
RL   J. Mol. Evol. 28:151-160(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=137c / CC-125;
RX   PubMed=11148274; DOI=10.1093/pcp/pcd044;
RA   Felitti S.A., Chan R.L., Sierra M.G., Gonzalez D.H.;
RT   "The cytochrome c gene from the green alga Chlamydomonas reinhardtii.
RT   Structure and expression in wild-type cells and in obligate
RT   photoautotrophic (dk) mutants.";
RL   Plant Cell Physiol. 41:1149-1156(2000).
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; M35173; AAA33084.1; -; mRNA.
DR   EMBL; Z99829; CAB16954.1; -; Genomic_DNA.
DR   PIR; S29514; S29514.
DR   RefSeq; XP_001696912.1; XM_001696860.1.
DR   AlphaFoldDB; P15451; -.
DR   SMR; P15451; -.
DR   STRING; 3055.EDP00604; -.
DR   PRIDE; P15451; -.
DR   ProMEX; P15451; -.
DR   EnsemblPlants; PNW75327; PNW75327; CHLRE_12g522600v5.
DR   GeneID; 5722552; -.
DR   Gramene; PNW75327; PNW75327; CHLRE_12g522600v5.
DR   KEGG; cre:CHLRE_12g522600v5; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   OMA; WTDANLD; -.
DR   OrthoDB; 1533604at2759; -.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
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:0010336; P:gibberellic acid homeostasis; IEA:EnsemblPlants.
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   Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..112
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108291"
FT   BINDING         23
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         26
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         27
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         89
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"
SQ   SEQUENCE   112 AA;  11958 MW;  ABFACEE87C08E212 CRC64;
     MSTFAEAPAG DLARGEKIFK TKCAQCHVAE KGGGHKQGPN LGGLFGRVSG TAAGFAYSKA
     NKEAAVTWGE STLYEYLLNP KKYMPGNKMV FAGLKKPEER ADLIAYLKQA TA