ID   CYC_MELGA               Reviewed;         105 AA.
AC   P67882; P00016; Q9PRU4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Cytochrome c;
GN   Name=CYC;
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103;
RN   [1]
RP   PARTIAL PROTEIN SEQUENCE, AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES, AND
RP   ACETYLATION AT GLY-2.
RA   Chan S.K., Tulloss I., Margoliash E.;
RL   Submitted (JUN-1966) to the PIR data bank.
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   -!- MISCELLANEOUS: The turkey sequence appears to be identical with that of
CC       chicken.
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; A04612; CCTK.
DR   RefSeq; XP_003207183.1; XM_003207135.3.
DR   RefSeq; XP_010711090.1; XM_010712788.1.
DR   RefSeq; XP_010711091.1; XM_010712789.2.
DR   AlphaFoldDB; P67882; -.
DR   SMR; P67882; -.
DR   Ensembl; ENSMGAT00000011899; ENSMGAP00000011030; ENSMGAG00000010618.
DR   GeneID; 100549365; -.
DR   KEGG; mgp:100549365; -.
DR   CTD; 40162; -.
DR   GeneTree; ENSGT00940000157883; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P67882; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000001645; Chromosome 6.
DR   Bgee; ENSMGAG00000010618; Expressed in heart and 17 other tissues.
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   Acetylation; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Metal-binding; Mitochondrion; Reference proteome; Respiratory chain;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.1"
FT   CHAIN           2..105
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108242"
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:0000269|Ref.1"
SQ   SEQUENCE   105 AA;  11711 MW;  293CEF5B11DABC36 CRC64;
     MGDIEKGKKI FVQKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAEGFSYT DANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFAGIKKKS ERVDLIAYLK DATSK