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   03-AUG-2022, entry version 120.
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.Solyc01g103220.2.1; -.
DR   iPTMnet; P00060; -.
DR   PaxDb; P00060; -.
DR   PRIDE; P00060; -.
DR   eggNOG; KOG3453; Eukaryota.
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; -; 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; 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