CYC_SCHPO
ID CYC_SCHPO Reviewed; 109 AA.
AC P00046;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Cytochrome c;
GN Name=cyc1; ORFNames=SPCC191.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6287225; DOI=10.1128/mcb.2.2.106-116.1982;
RA Russell P.R., Hall B.D.;
RT "Structure of the Schizosaccharomyces pombe cytochrome c gene.";
RL Mol. Cell. Biol. 2:106-116(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PROTEIN SEQUENCE OF 2-109, AND METHYLATION AT LYS-77.
RX PubMed=207525; DOI=10.1111/j.1432-1033.1978.tb12323.x;
RA Simon-Becam A.-M., Claisse M., Lederer F.;
RT "Cytochrome c from Schizosaccharomyces pombe. 2. Amino-acid sequence.";
RL Eur. J. Biochem. 86:407-416(1978).
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; J01318; AAA35300.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB41053.1; -; Genomic_DNA.
DR PIR; T41220; CCZP.
DR RefSeq; NP_588296.1; NM_001023286.2.
DR AlphaFoldDB; P00046; -.
DR SMR; P00046; -.
DR BioGRID; 275718; 2.
DR STRING; 4896.SPCC191.07.1; -.
DR MaxQB; P00046; -.
DR PaxDb; P00046; -.
DR PRIDE; P00046; -.
DR EnsemblFungi; SPCC191.07.1; SPCC191.07.1:pep; SPCC191.07.
DR GeneID; 2539146; -.
DR KEGG; spo:SPCC191.07; -.
DR PomBase; SPCC191.07; cyc1.
DR VEuPathDB; FungiDB:SPCC191.07; -.
DR eggNOG; KOG3453; Eukaryota.
DR HOGENOM; CLU_060944_3_0_1; -.
DR InParanoid; P00046; -.
DR OMA; AQCHTIN; -.
DR PhylomeDB; P00046; -.
DR Reactome; R-SPO-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SPO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-SPO-5620971; Pyroptosis.
DR Reactome; R-SPO-611105; Respiratory electron transport.
DR PRO; PR:P00046; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0005746; C:mitochondrial respirasome; ISO:PomBase.
DR GO; GO:0009055; F:electron transfer activity; ISO:PomBase.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IGI:PomBase.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; ISO:PomBase.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; ISO:PomBase.
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; Reference proteome; Respiratory chain;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:207525"
FT CHAIN 2..109
FT /note="Cytochrome c"
FT /id="PRO_0000108333"
FT BINDING 19
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 22
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 23
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 85
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 77
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:207525"
FT CONFLICT 58
FT /note="R -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="K -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 109 AA; 12022 MW; 28F4BAA1E9B906F9 CRC64;
MPYAPGDEKK GASLFKTRCA QCHTVEKGGA NKVGPNLHGV FGRKTGQAEG FSYTEANRDK
GITWDEETLF AYLENPKKYI PGTKMAFAGF KKPADRNNVI TYLKKATSE
