ID   CYCA_TAKRU              Reviewed;         105 AA.
AC   Q1KL06;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cytochrome c-a;
GN   Name=cyc-a;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16636282; DOI=10.1073/pnas.0601492103;
RA   Lee A.P., Koh E.G.L., Tay A., Brenner S., Venkatesh B.;
RT   "Highly conserved syntenic blocks at the vertebrate Hox loci and conserved
RT   regulatory elements within and outside Hox gene clusters.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6994-6999(2006).
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}.
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. {ECO:0000250}.
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; DQ481663; ABF22388.1; -; Genomic_DNA.
DR   RefSeq; XP_003969024.1; XM_003968975.2.
DR   RefSeq; XP_011607386.1; XM_011609084.1.
DR   AlphaFoldDB; Q1KL06; -.
DR   SMR; Q1KL06; -.
DR   STRING; 31033.ENSTRUP00000040508; -.
DR   Ensembl; ENSTRUT00000054312; ENSTRUP00000054566; ENSTRUG00000024909.
DR   GeneID; 101067333; -.
DR   KEGG; tru:101067333; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00940000157883; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; Q1KL06; -.
DR   OMA; NKGVIWG; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Proteomes; UP000005226; Chromosome 12.
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   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Reference proteome; Respiratory chain; Transport.
FT   CHAIN           1..105
FT                   /note="Cytochrome c-a"
FT                   /id="PRO_0000266003"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   105 AA;  11979 MW;  663B1E8966A286D9 CRC64;
     MGDIAKGKKI FVQRCSQCHT VTKEGRHKVG PNLWGLFGRK TGQAEGYSYT QANIEKGITW
     DEETLNVYLQ NPKKYIPGTK MNFAGIRKKR ERLDIIAYIK EATSK