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Database: UniProt
Entry: CYC_KATPE
LinkDB: CYC_KATPE
Original site: CYC_KATPE 
ID   CYC_KATPE               Reviewed;         104 AA.
AC   P00025;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Cytochrome c;
GN   Name=cyc;
OS   Katsuwonus pelamis (Skipjack tuna) (Bonito).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Pelagiaria; Scombriformes; Scombridae; Katsuwonus.
OX   NCBI_TaxID=8226;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-104, AND ACETYLATION AT GLY-2.
RX   PubMed=5106585; DOI=10.1093/oxfordjournals.jbchem.a129643;
RA   Nakayama T., Titani K., Narita K.;
RT   "The amino acid sequence of cytochrome c from bonito (Katsuwonus pelamis,
RT   Linnaeus).";
RL   J. Biochem. 70:311-326(1971).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF REDUCED FORM.
RX   PubMed=166072;
RA   Tanaka N., Yamane T., Tsukihara T., Ashida T., Kakudo M.;
RT   "The crystal structure of bonito (katsuo) ferrocytochrome c at 2.3-A
RT   resolution. II. Structure and function.";
RL   J. Biochem. 77:147-162(1975).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF OXIDIZED FORM.
RX   PubMed=218921;
RA   Matsuura Y., Hata Y., Yamaguchi T., Tanaka N., Kakudo M.;
RT   "Structure of bonito heart ferricytochrome c and some remarks on molecular
RT   interaction in its crystalline state.";
RL   J. Biochem. 85:729-737(1979).
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; A00022; CCBN.
DR   PDB; 1CYC; X-ray; 2.30 A; A/B=2-104.
DR   PDBsum; 1CYC; -.
DR   AlphaFoldDB; P00025; -.
DR   BMRB; P00025; -.
DR   SMR; P00025; -.
DR   iPTMnet; P00025; -.
DR   EvolutionaryTrace; P00025; -.
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; Cytochrome c-like domain; 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; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF12; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 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                   /evidence="ECO:0000269|PubMed:5106585"
FT   CHAIN           2..104
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108253"
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:166072"
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:166072"
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                   ECO:0000269|PubMed:166072"
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                   ECO:0000269|PubMed:166072"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:5106585"
FT   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:1CYC"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:1CYC"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:1CYC"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:1CYC"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:1CYC"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:1CYC"
FT   TURN            51..56
FT                   /evidence="ECO:0007829|PDB:1CYC"
FT   HELIX           62..70
FT                   /evidence="ECO:0007829|PDB:1CYC"
FT   STRAND          72..76
FT                   /evidence="ECO:0007829|PDB:1CYC"
FT   HELIX           89..102
FT                   /evidence="ECO:0007829|PDB:1CYC"
SQ   SEQUENCE   104 AA;  11515 MW;  8947998965482F17 CRC64;
     MGDVAKGKKT FVQKCAQCHT VENGGKHKVG PNLWGLFGRK TGQAEGYSYT DANKSKGIVW
     NENTLMEYLE NPKKYIPGTK MIFAGIKKKG ERQDLVAYLK SATS
//
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