SLM2_YEAST
ID SLM2_YEAST Reviewed; 656 AA.
AC P53955; D6W1D2; Q2VQW4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate-binding protein SLM2;
DE AltName: Full=Synthetic lethal with MSS4 protein 2;
DE AltName: Full=TORC2 effector protein SLM2;
GN Name=SLM2; Synonyms=LIT1; OrderedLocusNames=YNL047C;
GN ORFNames=N2515, YNL2515P;
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 96604 / S288c / FY1679;
RX PubMed=8740423;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<493::aid-yea929>3.0.co;2-w;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 12.8 kb from the left arm of chromosome XIV reveals a
RT sigma element, a pro-tRNA and six complete open reading frames, one of
RT which encodes a protein similar to the human leukotriene A4 hydrolase.";
RL Yeast 12:493-499(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-65.
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16012843; DOI=10.1007/s00294-005-0001-x;
RA Zhang Z., Dietrich F.S.;
RT "Identification and characterization of upstream open reading frames (uORF)
RT in the 5' untranslated regions (UTR) of genes in Saccharomyces
RT cerevisiae.";
RL Curr. Genet. 48:77-87(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-656.
RC STRAIN=S288c / FY1676;
RX PubMed=8533472; DOI=10.1002/yea.320111008;
RA Bergez P., Doignon F., Crouzet M.;
RT "The sequence of a 44 420 bp fragment located on the left arm of chromosome
RT XIV from Saccharomyces cerevisiae.";
RL Yeast 11:967-974(1995).
RN [7]
RP ERRATUM OF PUBMED:8533472.
RX PubMed=8904343;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d;
RA Bergez P., Doignon F., Crouzet M.;
RL Yeast 12:297-297(1996).
RN [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY TORC2, AND INTERACTION
RP WITH SLM1.
RX PubMed=15372071; DOI=10.1038/sj.emboj.7600384;
RA Audhya A., Loewith R., Parsons A.B., Gao L., Tabuchi M., Zhou H., Boone C.,
RA Hall M.N., Emr S.D.;
RT "Genome-wide lethality screen identifies new PI4,5P2 effectors that
RT regulate the actin cytoskeleton.";
RL EMBO J. 23:3747-3757(2004).
RN [10]
RP PHOSPHOINOSITIDE-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=15023338; DOI=10.1016/s1097-2765(04)00083-8;
RA Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B.,
RA Murray D., Emr S.D., Lemmon M.A.;
RT "Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin
RT homology domains.";
RL Mol. Cell 13:677-688(2004).
RN [11]
RP FUNCTION, INTERACTION WITH AVO2; BIT2; BIT61 AND TOR2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15689497; DOI=10.1091/mbc.e04-07-0564;
RA Fadri M., Daquinag A., Wang S., Xue T., Kunz J.;
RT "The pleckstrin homology domain proteins Slm1 and Slm2 are required for
RT actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-
RT bisphosphate and TORC2.";
RL Mol. Biol. Cell 16:1883-1900(2005).
RN [12]
RP FUNCTION, DEPHOSPHORYLATION BY CALCINEURIN, AND INTERACTION WITH CNA1 AND
RP CNA2.
RX PubMed=16738335; DOI=10.1128/mcb.01973-05;
RA Bultynck G., Heath V.L., Majeed A.P., Galan J.-M., Haguenauer-Tsapis R.,
RA Cyert M.S.;
RT "Slm1 and slm2 are novel substrates of the calcineurin phosphatase required
RT for heat stress-induced endocytosis of the yeast uracil permease.";
RL Mol. Cell. Biol. 26:4729-4745(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649 AND SER-653, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-649 AND SER-653, 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: Together with SLM1, effector of the TORC2- and calcineurin-
CC signaling pathways. Phosphorylated and activated by TORC2 under
CC favorable growth conditions. Mediates actin polarization via inhibition
CC of calcineurin-dependent transcription. Upon nutrient limitation or
CC environmental stress, gets dephosphorylated by calcineurin, inhibiting
CC interaction with TORC2, thereby antagonizing TORC2 signaling and
CC mediating calcineurin-dependent actin depolarization. Also functions in
CC heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis.
CC {ECO:0000269|PubMed:15372071, ECO:0000269|PubMed:15689497,
CC ECO:0000269|PubMed:16738335}.
CC -!- SUBUNIT: Heterodimer of SLM1-SLM2. Binds phosphatidylinositol 4,5-
CC bisphosphate, which is required for function. Interacts with the TORC2
CC subunits AVO2, BIT61 and TOR2. Interacts with the calcineurin catalytic
CC subunits CNA1 and CNA2. {ECO:0000269|PubMed:15372071,
CC ECO:0000269|PubMed:15689497, ECO:0000269|PubMed:16738335}.
CC -!- INTERACTION:
CC P53955; P43603: LSB3; NbExp=2; IntAct=EBI-28706, EBI-22980;
CC P53955; P40485: SLM1; NbExp=3; IntAct=EBI-28706, EBI-25172;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15023338,
CC ECO:0000269|PubMed:15372071, ECO:0000269|PubMed:15689497}; Peripheral
CC membrane protein {ECO:0000269|PubMed:15023338,
CC ECO:0000269|PubMed:15372071, ECO:0000269|PubMed:15689497}; Cytoplasmic
CC side {ECO:0000269|PubMed:15023338, ECO:0000269|PubMed:15372071,
CC ECO:0000269|PubMed:15689497}.
CC -!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X94547; CAA64235.1; -; Genomic_DNA.
DR EMBL; Z71323; CAA95915.1; -; Genomic_DNA.
DR EMBL; AY692658; AAT92677.1; -; Genomic_DNA.
DR EMBL; AY899254; AAX83939.1; -; mRNA.
DR EMBL; U12141; AAA99665.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10498.1; -; Genomic_DNA.
DR PIR; S61097; S61097.
DR RefSeq; NP_014351.3; NM_001182886.3.
DR AlphaFoldDB; P53955; -.
DR BioGRID; 35777; 159.
DR DIP; DIP-1269N; -.
DR IntAct; P53955; 10.
DR MINT; P53955; -.
DR STRING; 4932.YNL047C; -.
DR iPTMnet; P53955; -.
DR MaxQB; P53955; -.
DR PaxDb; P53955; -.
DR PRIDE; P53955; -.
DR EnsemblFungi; YNL047C_mRNA; YNL047C; YNL047C.
DR GeneID; 855680; -.
DR KEGG; sce:YNL047C; -.
DR SGD; S000004992; SLM2.
DR VEuPathDB; FungiDB:YNL047C; -.
DR eggNOG; ENOG502QRAF; Eukaryota.
DR GeneTree; ENSGT00940000176324; -.
DR HOGENOM; CLU_013663_1_0_1; -.
DR InParanoid; P53955; -.
DR OMA; MSIPLVE; -.
DR BioCyc; YEAST:G3O-33081-MON; -.
DR PRO; PR:P53955; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53955; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0031932; C:TORC2 complex; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; TAS:SGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:SGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IGI:SGD.
DR GO; GO:0070941; P:eisosome assembly; IGI:SGD.
DR GO; GO:0016197; P:endosomal transport; IGI:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IPI:SGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IGI:SGD.
DR GO; GO:0001558; P:regulation of cell growth; IGI:SGD.
DR GO; GO:0031929; P:TOR signaling; IPI:SGD.
DR GO; GO:0038203; P:TORC2 signaling; IEA:InterPro.
DR CDD; cd13311; PH_Slm1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR033191; Slm1/Slm2.
DR InterPro; IPR043453; Slm1_PH.
DR PANTHER; PTHR31941:SF12; PTHR31941:SF12; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..656
FT /note="Phosphatidylinositol 4,5-bisphosphate-binding
FT protein SLM2"
FT /id="PRO_0000203453"
FT DOMAIN 445..555
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 577..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 640..645
FT /note="PXIXIT-like, required for interaction with CNA1 and
FT CNA2, and calcineurin-dependent dephosphorylation"
FT COMPBIAS 582..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 656 AA; 74785 MW; 85E65FE60312B875 CRC64;
MSYQRNSARA SLDLRSQYQQ LEGRMRSEHF NPAYQQQQQK GQNIPLSLPS SLAQRNPIPY
PIDAVTSDPT IPAQLNVYDH DRQNSIVDAA AGTNTTHSLN SNNIPSSQNN NINNNNINNV
GSFTDPSMLT LPKMSLHSHQ KQYDSNQNDP RSPLAILIPT SAQPTDVLSA RFSAWRNVIR
AILVYLSETA SIQDEIVRQQ LRLSHAVQFP FFSIENQYQP VSNEDKSMQK FFLPLGSGSV
QDLPTMLTKY HDNLASLASK SSKELTSEII PRLEDLRRDL LVKIKEIKAL QSDFKNSCNK
ELQQTKHLMK LFNESLKECK LGTPKSDPFL IKLQLEKQIK RQLVEENYLH EAFDNLQNSG
AQLESVIVME IQNGLTSYAR ILGKEAQVVF DSVISKLDST ILNKNTNLEW DSFILRNISN
FVPPNLPMRR FKEISYSNQN DPFTFEVKSG FLEKRSKFLK SYSRGFYVLT PSFLHEFKTP
DKHKFSTPLM SIPLVECTVT EHSKKTKSNS EQGKNKFILR TNSNGLIHRG HNWVFKVDSY
DDMIEWFGNI KALSSLPNYD DKCKYVSKVA KLSKEKAKSN ENTTESVTPQ VTNEQHTRYD
DVSSSNFPLN SIPKLDNLTI TNTTSSIPET NDSQIQNRVP EFYIENVDSP RKSNQL
