ID   SFK1_YEAST              Reviewed;         353 AA.
AC   P35735; D6VXN6;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   04-NOV-2026, entry version 160.
DE   RecName: Full=Protein SFK1;
DE   AltName: Full=Suppressor of four kinase protein 1;
GN   Name=SFK1; OrderedLocusNames=YKL051W; ORFNames=YKL303;
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 204508 / S288c;
RX   PubMed=8091862; DOI=10.1002/yea.320100008;
RA   Rasmussen S.W.;
RT   "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and
RT   TOA2 genes, an open reading frame (ORF) similar to a translationally
RT   controlled tumour protein, one ORF containing motifs also found in plant
RT   storage proteins and 13 ORFs with weak or no homology to known proteins.";
RL   Yeast 10:S63-S68(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
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   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12015967; DOI=10.1016/s1534-5807(02)00168-5;
RA   Audhya A., Emr S.D.;
RT   "Stt4 PI 4-kinase localizes to the plasma membrane and functions in the
RT   Pkc1-mediated MAP kinase cascade.";
RL   Dev. Cell 2:593-605(2002).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP   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: May control the production of phosphatidylinositol 4-
CC       phosphate (PI4P) by the STT4 PI 4-kinase. Mediates proper localization
CC       of STT4 to the plasma membrane. {ECO:0000269|PubMed:12015967}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12015967,
CC       ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:12015967, ECO:0000269|PubMed:14562095}.
CC   -!- SIMILARITY: Belongs to the SFK1 family. {ECO:0000305}.
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DR   EMBL; X75781; CAA53425.1; -; Genomic_DNA.
DR   EMBL; Z28051; CAA81886.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09106.1; -; Genomic_DNA.
DR   PIR; S37873; S37873.
DR   RefSeq; NP_012873.1; NM_001179617.1.
DR   AlphaFoldDB; P35735; -.
DR   SMR; P35735; -.
DR   BioGRID; 34082; 117.
DR   DIP; DIP-5309N; -.
DR   FunCoup; P35735; 118.
DR   IntAct; P35735; 47.
DR   STRING; 4932.YKL051W; -.
DR   iPTMnet; P35735; -.
DR   PaxDb; 4932-YKL051W; -.
DR   PeptideAtlas; P35735; -.
DR   EnsemblFungi; YKL051W_mRNA; YKL051W; YKL051W.
DR   GeneID; 853815; -.
DR   KEGG; sce:YKL051W; -.
DR   AGR; SGD:S000001534; -.
DR   SGD; S000001534; SFK1.
DR   VEuPathDB; FungiDB:YKL051W; -.
DR   eggNOG; ENOG502RZQS; Eukaryota.
DR   HOGENOM; CLU_050573_1_0_1; -.
DR   InParanoid; P35735; -.
DR   OMA; ACFKTFW; -.
DR   OrthoDB; 10032492at2759; -.
DR   BioCyc; YEAST:G3O-31852-MONOMER; -.
DR   BioGRID-ORCS; 853815; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P35735; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P35735; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IGI:SGD.
DR   GO; GO:0061093; P:negative regulation of phospholipid translocation; IMP:SGD.
DR   GO; GO:0007033; P:vacuole organization; IGI:SGD.
DR   InterPro; IPR019402; CWH43_N.
DR   InterPro; IPR050911; DRAM/TMEM150_Autophagy_Mod.
DR   PANTHER; PTHR21324:SF2; EG:22E5.9 PROTEIN; 1.
DR   PANTHER; PTHR21324; FASTING-INDUCIBLE INTEGRAL MEMBRANE PROTEIN TM6P1-RELATED; 1.
DR   Pfam; PF10277; Frag1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..353
FT                   /note="Protein SFK1"
FT                   /id="PRO_0000203179"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..62
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..130
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        152..160
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..231
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..263
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285..353
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   353 AA;  40463 MW;  BB66ED73F1181331 CRC64;
     MIQFKSPGNW LFIVPWIAFI PWYGMLIAML ICWASQGHPI YWFMHSEQFP VYISDIGATN
     LRPLFISCAG WQGLGYVITV ALEFFQRSGY LPFQLKKKDP SISDSTSYAE KLHSGKYLMP
     PYYTKDERNL IFAAFVLGSI GELALLFSSI FSTALYHRVH IAMVSVFVVF MFLSTCCLIA
     EYFLMGRHYA SVHPLASPHF NPQSSEKSFN QDYNTVDELP WYKWKGHVWN KFTISATLKV
     IWLTLAVVWA ICFGAINDRS KSACFEWLLA FWFGIIFMIL SADFYLGGRY RQSRYFNHVE
     SFSGYYKYDK ALGLYHSEDV LPSDDNAGVI ATETASSNIY NNSSSNESIQ VVV
//