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 03-AUG-2022, entry version 123.
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; -; 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 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
