STF2_YEAST
ID STF2_YEAST Reviewed; 84 AA.
AC P16965; D6VUE5; P89099;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=ATPase-stabilizing factor 15 kDa protein;
GN Name=STF2; OrderedLocusNames=YGR008C; ORFNames=G3858;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=2169416; DOI=10.1111/j.1432-1033.1990.tb19193.x;
RA Yoshida Y., Sato T., Hashimoto T., Ichikawa N., Nakai S., Yoshikawa H.,
RA Imamoto F., Tagawa K.;
RT "Isolation of a gene for a regulatory 15-kDa subunit of mitochondrial F1F0-
RT ATPase and construction of mutant yeast lacking the protein.";
RL Eur. J. Biochem. 192:49-53(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=8982874; DOI=10.1093/oxfordjournals.jbchem.a021497;
RA Min-Seok R., Kawamata Y., Nakamura H., Ohta A., Takagi M.;
RT "Isolation and characterization of ECT1 gene encoding CTP:
RT phosphoethanolamine cytidylyltransferase of Saccharomyces cerevisiae.";
RL J. Biochem. 120:1040-1047(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PROTEIN SEQUENCE OF 2-84.
RA Yoshida Y., Wakabayashi S., Matsubara H., Hashimoto T., Tagawa K.;
RT "Primary structure of a regulating factor, 15 kDa protein, of ATP synthase
RT in yeast mitochondria.";
RL FEBS Lett. 170:135-138(1984).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-69, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-69, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-69, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: This is one of two stabilizing factors of the inactive
CC mitochondrial F0F1-ATPase. It binds to the F0 part and facilitates the
CC binding of both the inhibitor and the 9 kDa protein to F1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- MISCELLANEOUS: Present with 5330 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the STF2 family. {ECO:0000305}.
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DR EMBL; D00444; BAA00345.1; -; Genomic_DNA.
DR EMBL; D50644; BAA09311.1; -; Genomic_DNA.
DR EMBL; Z72793; CAA96991.1; -; Genomic_DNA.
DR EMBL; AY558270; AAS56596.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08106.1; -; Genomic_DNA.
DR PIR; S12201; S12201.
DR RefSeq; NP_011522.1; NM_001181137.1.
DR AlphaFoldDB; P16965; -.
DR BioGRID; 33252; 82.
DR IntAct; P16965; 2.
DR MINT; P16965; -.
DR STRING; 4932.YGR008C; -.
DR iPTMnet; P16965; -.
DR MaxQB; P16965; -.
DR PaxDb; P16965; -.
DR PRIDE; P16965; -.
DR EnsemblFungi; YGR008C_mRNA; YGR008C; YGR008C.
DR GeneID; 852891; -.
DR KEGG; sce:YGR008C; -.
DR SGD; S000003240; STF2.
DR VEuPathDB; FungiDB:YGR008C; -.
DR eggNOG; ENOG502S4WH; Eukaryota.
DR HOGENOM; CLU_186295_0_0_1; -.
DR InParanoid; P16965; -.
DR OMA; DNGEIPP; -.
DR BioCyc; YEAST:G3O-30738-MON; -.
DR ChiTaRS; STF2; yeast.
DR PRO; PR:P16965; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P16965; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0071465; P:cellular response to desiccation; IMP:SGD.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Mitochondrion; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..84
FT /note="ATPase-stabilizing factor 15 kDa protein"
FT /id="PRO_0000072269"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 15
FT /note="D -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="E -> Q (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="N -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..84
FT /note="VFKKDRRGSNLQSHEQKFENVQKE -> SVQER (in Ref. 2;
FT BAA09311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 84 AA; 9615 MW; 1B9B753F4F3C15B7 CRC64;
MTRTNKWTER EGKADPKYFS HTGNYGESPN HIKKQGSGKG NWGKPGDEID DLIDNGEIPP
VFKKDRRGSN LQSHEQKFEN VQKE
