ID   CYC_COLLI               Reviewed;         105 AA.
AC   P00021;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Cytochrome c;
GN   Name=CYC;
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-105, AND PROTEIN SEQUENCE OF 90-92;
RP   93-100 AND 101-105.
RA   Wojciech R., Margoliash E.;
RL   (In) Sober H.A. (eds.);
RL   Handbook of biochemistry, pp.C158-C161, CRC Press, Cleveland (1968).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=11956295; DOI=10.1084/jem.20011971;
RA   Fremont D.H., Dai S., Chiang H., Crawford F., Marrack P., Kappler J.;
RT   "Structural basis of cytochrome c presentation by IE(k).";
RL   J. Exp. Med. 195:1043-1052(2002).
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   PIR; A00013; CCPY.
DR   RefSeq; XP_005513534.2; XM_005513477.2.
DR   PDB; 1KTD; X-ray; 2.40 A; B/D=93-105.
DR   PDBsum; 1KTD; -.
DR   AlphaFoldDB; P00021; -.
DR   SMR; P00021; -.
DR   STRING; 8932.XP_005513534.1; -.
DR   PRIDE; P00021; -.
DR   ABCD; P00021; 23 sequenced antibodies.
DR   GeneID; 102085712; -.
DR   KEGG; clv:102085712; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   OrthoDB; 1533604at2759; -.
DR   EvolutionaryTrace; P00021; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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   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   3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108240"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
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         81
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-acetylglycine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   105 AA;  11664 MW;  88C48F5B1F21BC20 CRC64;
     MGDIEKGKKI FVQKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAEGFSYT DANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFAGIKKKA ERADLIAYLK QATAK