CYC_HELAN
ID CYC_HELAN Reviewed; 112 AA.
AC P00070; Q39936;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cytochrome c;
GN Name=CYTC1;
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root;
RA Felitti S.A., Chan R.L., Gago G., Valle E.M., Gonzalez D.H.;
RT "Sunflower cytochrome c mRNA levels are subject to tissue-specific
RT regulation.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-112, ACETYLATION AT ALA-2, AND METHYLATION AT LYS-81
RP AND LYS-95.
RX PubMed=5500313; DOI=10.1042/bj1190535;
RA Ramshaw J.A.M., Thompson E.W., Boulter D.;
RT "The amino acid sequence of Helianthus annuus L. (sunflower) cytochrome c
RT deduced from chymotryptic peptides.";
RL Biochem. J. 119:535-539(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";
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DR EMBL; L77113; AAA92712.1; -; mRNA.
DR PIR; A00062; CCFS.
DR AlphaFoldDB; P00070; -.
DR SMR; P00070; -.
DR iPTMnet; P00070; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr11g0472061; mRNA:HanXRQr2_Chr11g0472061; HanXRQr2_Chr11g0472061.
DR Gramene; mRNA:HanXRQr2_Chr11g0472061; mRNA:HanXRQr2_Chr11g0472061; HanXRQr2_Chr11g0472061.
DR OMA; ARCKACH; -.
DR OrthoDB; 1533604at2759; -.
DR PhylomeDB; P00070; -.
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 GO; GO:0010336; P:gibberellic acid homeostasis; IEA:EnsemblPlants.
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; Methylation; Mitochondrion; Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5500313"
FT CHAIN 2..112
FT /note="Cytochrome c"
FT /id="PRO_0000108299"
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:5500313"
FT BINDING 26
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:5500313"
FT BINDING 27
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 89
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 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:5500313"
FT MOD_RES 81
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:5500313"
FT MOD_RES 95
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:5500313"
FT CONFLICT 11
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="E -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="G -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="K -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 112 AA; 12129 MW; 8FF0DDC53033411B CRC64;
MASFAEAPAG NPTTGEKIFK TKCAQCHTVE KGAGHKQGPN LNGLFGRQSG TTAGYSYSAG
NKNKAVIWEE NTLYDYLLNP KKYIPGTKMV FPGLKKPQER ADLIAYLKTS TA
