ID CYC_SOLLC Reviewed; 111 AA.
AC P00060;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=Cytochrome c;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP PROTEIN SEQUENCE, ACETYLATION AT ALA-1, AND METHYLATION AT LYS-80 AND
RP LYS-94.
RX PubMed=5044037; DOI=10.1016/0003-9861(72)90066-5;
RA Scogin R., Richardson M., Boulter D.;
RT "The amino acid sequence of cytochrome c from tomato (Lycopersicon
RT esculentum Mill.).";
RL Arch. Biochem. Biophys. 150:489-492(1972).
RN [2]
RP SEQUENCE REVISION TO 98.
RA Boulter D., Ramshaw J.A.M., Thompson E.W., Richardson M., Brown R.H.;
RT "A phylogeny of higher plants based on the amino acid sequences of
RT cytochrome c and its biological implications.";
RL Proc. R. Soc. Lond., B, Biol. Sci. 181:441-455(1972).
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; A00053; CCTO.
DR AlphaFoldDB; P00060; -.
DR SMR; P00060; -.
DR STRING; 4081.P00060; -.
DR iPTMnet; P00060; -.
DR PaxDb; 4081-Solyc01g103220-2-1; -.
DR eggNOG; KOG3453; Eukaryota.
DR InParanoid; P00060; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P00060; 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..111
FT /note="Cytochrome c"
FT /id="PRO_0000108300"
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:5044037"
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:5044037"
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:5044037"
FT MOD_RES 80
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:5044037"
FT MOD_RES 94
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:5044037"
SQ SEQUENCE 111 AA; 12023 MW; C1D10E032FD29F28 CRC64;
ASFNEAPPGN PKAGEKIFKT KCAQCHTVEK GAGHKEGPNL NGLFGRQSGT TAGYSYSAAN
KNMAVNWGEN TLYDYLLNPK KYIPGTKMVF PGLKKPQERA DLIAYLKEAT A
//
