ID CYC_WHEAT Reviewed; 112 AA.
AC P00068;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Cytochrome c;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RX PubMed=5298061; DOI=10.1016/s0021-9258(18)99634-1;
RA Stevens F.C., Glazer A.N., Smith E.L.;
RT "The amino acid sequence of wheat germ cytochrome c.";
RL J. Biol. Chem. 242:2764-2779(1967).
RN [2]
RP METHYLATION AT LYS-80 AND LYS-94.
RX PubMed=4304194; DOI=10.1016/s0021-9258(18)91855-7;
RA Delange R.J., Glazer A.N., Smith E.L.;
RT "Presence and location of an unusual amino acid, epsilon-N-trimethyllysine,
RT in cytochrome c of wheat germ and Neurospora.";
RL J. Biol. Chem. 244:1385-1388(1969).
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 tentative assignment of Gln-24 and Glu-69 is based
CC on indirect evidence (electrophoretic mobilities and comparisons with
CC other cytochromes 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; A00060; CCWT.
DR AlphaFoldDB; P00068; -.
DR SMR; P00068; -.
DR STRING; 4565.P00068; -.
DR iPTMnet; P00068; -.
DR PaxDb; 4565-Traes_1AL_45A9AD1EA-1; -.
DR EnsemblPlants; TraesCAD_scaffold_038108_01G000200.1; TraesCAD_scaffold_038108_01G000200.1; TraesCAD_scaffold_038108_01G000200.
DR EnsemblPlants; TraesCLE_scaffold_060241_01G000100.1; TraesCLE_scaffold_060241_01G000100.1; TraesCLE_scaffold_060241_01G000100.
DR EnsemblPlants; TraesKAR1B01G0315100.1; cds.TraesKAR1B01G0315100.1; TraesKAR1B01G0315100.
DR EnsemblPlants; TraesPAR_scaffold_050924_01G000200.1; TraesPAR_scaffold_050924_01G000200.1; TraesPAR_scaffold_050924_01G000200.
DR EnsemblPlants; TraesROB_scaffold_057684_01G000400.1; TraesROB_scaffold_057684_01G000400.1; TraesROB_scaffold_057684_01G000400.
DR EnsemblPlants; TraesWEE_scaffold_035863_01G000400.1; TraesWEE_scaffold_035863_01G000400.1; TraesWEE_scaffold_035863_01G000400.
DR Gramene; TraesCAD_scaffold_038108_01G000200.1; TraesCAD_scaffold_038108_01G000200.1; TraesCAD_scaffold_038108_01G000200.
DR Gramene; TraesCLE_scaffold_060241_01G000100.1; TraesCLE_scaffold_060241_01G000100.1; TraesCLE_scaffold_060241_01G000100.
DR Gramene; TraesKAR1B01G0315100.1; cds.TraesKAR1B01G0315100.1; TraesKAR1B01G0315100.
DR Gramene; TraesPAR_scaffold_050924_01G000200.1; TraesPAR_scaffold_050924_01G000200.1; TraesPAR_scaffold_050924_01G000200.
DR Gramene; TraesROB_scaffold_057684_01G000400.1; TraesROB_scaffold_057684_01G000400.1; TraesROB_scaffold_057684_01G000400.
DR Gramene; TraesWEE_scaffold_035863_01G000400.1; TraesWEE_scaffold_035863_01G000400.1; TraesWEE_scaffold_035863_01G000400.
DR eggNOG; KOG3453; Eukaryota.
DR OMA; MPAPYKK; -.
DR PRO; PR:P00068; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P00068; baseline and differential.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
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 GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
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 Acetylation; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Methylation; Mitochondrion; Reference proteome;
KW Respiratory chain; Transport.
FT CHAIN 1..112
FT /note="Cytochrome c"
FT /id="PRO_0000108313"
FT BINDING 22
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:5298061"
FT BINDING 25
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:5298061"
FT BINDING 26
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 88
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 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:5298061"
FT MOD_RES 80
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:4304194"
FT MOD_RES 94
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:4304194"
SQ SEQUENCE 112 AA; 12048 MW; A66BC561B6E5F863 CRC64;
ASFSEAPPGN PDAGAKIFKT KCAQCHTVDA GAGHKQGPNL HGLFGRQSGT TAGYSYSAAN
KNKAVEWEEN TLYDYLLNPK KYIPGTKMVF PGLKKPQDRA DLIAYLKKAT SS
//
