ID   CYC_ATESP               Reviewed;         105 AA.
AC   P00003;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-NOV-2008, entry version 67.
DE   RecName: Full=Cytochrome c;
GN   Name=CYCS; Synonyms=CYC;
OS   Ateles sp. (Spider monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Atelidae; Atelinae; Ateles.
OX   NCBI_TaxID=9511;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-105.
RX   MEDLINE=82069044; PubMed=6272840; DOI=10.1021/bi00525a030;
RA   Shelnutt J.A., Rousseau D.L., Dethmers J.K., Margoliash E.;
RT   "Protein influences on porphyrin structure in cytochrome c: evidence
RT   from Raman difference spectroscopy.";
RL   Biochemistry 20:6485-6497(1981).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
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DR   PIR; A00004; CCMKP.
DR   HSSP; P00004; 2PCB.
DR   SMR; P00003; 2-105.
DR   HOVERGEN; P00003; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005746; C:mitochondrial respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electron...; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation during apoptosis; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003088; Cyt_CI.
DR   InterPro; IPR002327; Cyt_CIAB.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   ProDom; PD000375; Cyt_CIAB; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c.
FT                                /FTId=PRO_0000108208.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine (Probable).
SQ   SEQUENCE   105 AA;  11841 MW;  F552A2FC63C0CEBE CRC64;
     MGDVFKGKRI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQASGFTYT EANKNKGIIW
     GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
//