CYC_PICKU
ID CYC_PICKU Reviewed; 109 AA.
AC P00041;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cytochrome c;
GN Name=CYC1;
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=5669923; DOI=10.1093/oxfordjournals.jbchem.a128765;
RA Narita K., Titani K.;
RT "The amino acid sequence of cytochrome C from Candida krusei.";
RL J. Biochem. 63:226-241(1968).
RN [2]
RP SEQUENCE REVISION TO 22.
RX PubMed=4344910; DOI=10.1111/j.1432-1033.1972.tb02512.x;
RA Lederer F.;
RT "Candida krusei chtochrome c: a correction to the sequence. Glutamine-16,
RT an invariant residue in mitochondrial cytochrome c?";
RL Eur. J. Biochem. 31:144-147(1972).
RN [3]
RP SEQUENCE REVISION TO 22.
RX PubMed=4357820; DOI=10.1016/0014-5793(73)80462-4;
RA Machleidt W., Wachter E., Scheulen M., Otto J.;
RT "Solid-phase Edman degradation of a protein: N-terminal sequence of
RT cytochrome c from Candida krusei.";
RL FEBS Lett. 37:217-220(1973).
RN [4]
RP METHYLATION AT LYS-78.
RX PubMed=5459636; DOI=10.1016/s0021-9258(18)62998-9;
RA Delange R.J., Glazer A.N., Smith E.L.;
RT "Identification and location of epsilon-N-trimethyllysine in yeast
RT cytochromes c.";
RL J. Biol. Chem. 245:3325-3327(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 -!- 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";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A91919; CCCK.
DR AlphaFoldDB; P00041; -.
DR BMRB; P00041; -.
DR SMR; P00041; -.
DR PRIDE; P00041; -.
DR VEuPathDB; FungiDB:C5L36_0B08680; -.
DR eggNOG; KOG3453; Eukaryota.
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 Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Methylation; Mitochondrion; Respiratory chain; Transport.
FT CHAIN 1..109
FT /note="Cytochrome c"
FT /id="PRO_0000108326"
FT BINDING 20
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:5669923"
FT BINDING 23
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:5669923"
FT BINDING 24
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 86
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 78
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000305|PubMed:5459636"
SQ SEQUENCE 109 AA; 11888 MW; 966817336C59330D CRC64;
PAPFEQGSAK KGATLFKTRC AQCHTIEAGG PHKVGPNLHG IFSRHSGQAE GYSYTDANKR
AGVEWAEPTM SDYLENPKKY IPGTKMAFGG LKKAKDRNDL VTYMLEASK
