ID   CYC_CYPCA               Reviewed;         104 AA.
AC   P00026;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Cytochrome c iso-1/iso-2;
GN   Name=cyc;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-104, AND ACETYLATION AT GLY-2.
RC   STRAIN=Amur carp, and European carp;
RX   PubMed=5434283; DOI=10.1111/j.1432-1033.1970.tb00819.x;
RA   Guertler L., Horstmann H.J.;
RT   "The amino acid sequence of cytochrome c of the carp, Cyprinus carpio.";
RL   Eur. J. Biochem. 12:48-57(1970).
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 protein was obtained from food carp that consisted
CC       of two cross-bred strains, the European carp and the Amur carp. The
CC       isocytochromes may be the result of strain differences.
CC   -!- MISCELLANEOUS: The sequence shown is the iso-1 cytochrome c.
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; A00023; CCCA.
DR   iPTMnet; P00026; -.
DR   Proteomes; UP000694384; Unplaced.
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:0000305|PubMed:5434283"
FT   CHAIN           2..104
FT                   /note="Cytochrome c iso-1/iso-2"
FT                   /id="PRO_0000108251"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:5434283"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:5434283"
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"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:5434283"
FT   VARIANT         5
FT                   /note="E -> D (in isoform iso-2)"
FT   UNSURE          22
FT                   /note="E or Q"
FT   UNSURE          23
FT                   /note="N or D"
FT   UNSURE          51
FT                   /note="D or N"
FT   UNSURE          53
FT                   /note="N or D"
FT   UNSURE          62
FT                   /note="E or Q"
FT   UNSURE          70
FT                   /note="E or Q"
FT   UNSURE          71
FT                   /note="N or D"
SQ   SEQUENCE   104 AA;  11496 MW;  23FDB6A70BCD684A CRC64;
     MGDVEKGKKV FVQKCAQCHT VENGGKHKVG PNLWGLFGRK TGQAPGFSYT DANKSKGIVW
     BEZTLMEYLE NPKKYIPGTK MIFAGIKKKG ERADLIAYLK SATS