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Phosphatidylinositol 4,5-bisphosphate-binding protein SLM2 (Synthetic lethal with MSS4 protein 2) (TORC2 effector protein SLM2)

 SLM2_YEAST              Reviewed;         656 AA.
P53955; D6W1D2; Q2VQW4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 142.
RecName: Full=Phosphatidylinositol 4,5-bisphosphate-binding protein SLM2;
AltName: Full=Synthetic lethal with MSS4 protein 2;
AltName: Full=TORC2 effector protein SLM2;
Name=SLM2; Synonyms=LIT1; OrderedLocusNames=YNL047C;
ORFNames=N2515, YNL2515P;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8740423;
DOI=10.1002/(SICI)1097-0061(199604)12:5<493::AID-YEA929>3.0.CO;2-W;
Nasr F., Becam A.-M., Herbert C.J.;
"The sequence of 12.8 kb from the left arm of chromosome XIV reveals a
sigma element, a pro-tRNA and six complete open reading frames, one of
which encodes a protein similar to the human leukotriene A4
hydrolase.";
Yeast 12:493-499(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-65.
STRAIN=ATCC 208353 / W303-1A;
PubMed=16012843; DOI=10.1007/s00294-005-0001-x;
Zhang Z., Dietrich F.S.;
"Identification and characterization of upstream open reading frames
(uORF) in the 5' untranslated regions (UTR) of genes in Saccharomyces
cerevisiae.";
Curr. Genet. 48:77-87(2005).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-656.
STRAIN=S288c / FY1676;
PubMed=8533472; DOI=10.1002/yea.320111008;
Bergez P., Doignon F., Crouzet M.;
"The sequence of a 44 420 bp fragment located on the left arm of
chromosome XIV from Saccharomyces cerevisiae.";
Yeast 11:967-974(1995).
[7]
ERRATUM.
PubMed=8904343;
DOI=10.1002/(SICI)1097-0061(19960315)12:3<297::AID-YEA940>3.0.CO;2-D;
Bergez P., Doignon F., Crouzet M.;
Yeast 12:297-297(1996).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY TORC2, AND
INTERACTION WITH SLM1.
PubMed=15372071; DOI=10.1038/sj.emboj.7600384;
Audhya A., Loewith R., Parsons A.B., Gao L., Tabuchi M., Zhou H.,
Boone C., Hall M.N., Emr S.D.;
"Genome-wide lethality screen identifies new PI4,5P2 effectors that
regulate the actin cytoskeleton.";
EMBO J. 23:3747-3757(2004).
[10]
PHOSPHOINOSITIDE-BINDING, AND SUBCELLULAR LOCATION.
PubMed=15023338; DOI=10.1016/S1097-2765(04)00083-8;
Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B.,
Murray D., Emr S.D., Lemmon M.A.;
"Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin
homology domains.";
Mol. Cell 13:677-688(2004).
[11]
FUNCTION, INTERACTION WITH AVO2; BIT2; BIT61 AND TOR2, AND SUBCELLULAR
LOCATION.
PubMed=15689497; DOI=10.1091/mbc.E04-07-0564;
Fadri M., Daquinag A., Wang S., Xue T., Kunz J.;
"The pleckstrin homology domain proteins Slm1 and Slm2 are required
for actin cytoskeleton organization in yeast and bind
phosphatidylinositol-4,5-bisphosphate and TORC2.";
Mol. Biol. Cell 16:1883-1900(2005).
[12]
FUNCTION, DEPHOSPHORYLATION BY CALCINEURIN, AND INTERACTION WITH CNA1
AND CNA2.
PubMed=16738335; DOI=10.1128/MCB.01973-05;
Bultynck G., Heath V.L., Majeed A.P., Galan J.-M.,
Haguenauer-Tsapis R., Cyert M.S.;
"Slm1 and slm2 are novel substrates of the calcineurin phosphatase
required for heat stress-induced endocytosis of the yeast uracil
permease.";
Mol. Cell. Biol. 26:4729-4745(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649 AND SER-653, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-649 AND
SER-653, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Together with SLM1, effector of the TORC2- and
calcineurin-signaling pathways. Phosphorylated and activated by
TORC2 under favorable growth conditions. Mediates actin
polarization via inhibition of calcineurin-dependent
transcription. Upon nutrient limitation or environmental stress,
gets dephosphorylated by calcineurin, inhibiting interaction with
TORC2, thereby antagonizing TORC2 signaling and mediating
calcineurin-dependent actin depolarization. Also functions in
heat-induced, calcineurin-mediated uracil permease (FUR4)
endocytosis. {ECO:0000269|PubMed:15372071,
ECO:0000269|PubMed:15689497, ECO:0000269|PubMed:16738335}.
-!- SUBUNIT: Heterodimer of SLM1-SLM2. Binds phosphatidylinositol 4,5-
bisphosphate, which is required for function. Interacts with the
TORC2 subunits AVO2, BIT61 and TOR2. Interacts with the
calcineurin catalytic subunits CNA1 and CNA2.
{ECO:0000269|PubMed:15372071, ECO:0000269|PubMed:15689497,
ECO:0000269|PubMed:16738335}.
-!- INTERACTION:
P43603:LSB3; NbExp=2; IntAct=EBI-28706, EBI-22980;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15023338,
ECO:0000269|PubMed:15372071, ECO:0000269|PubMed:15689497};
Peripheral membrane protein {ECO:0000269|PubMed:15023338,
ECO:0000269|PubMed:15372071, ECO:0000269|PubMed:15689497};
Cytoplasmic side {ECO:0000269|PubMed:15023338,
ECO:0000269|PubMed:15372071, ECO:0000269|PubMed:15689497}.
-!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; X94547; CAA64235.1; -; Genomic_DNA.
EMBL; Z71323; CAA95915.1; -; Genomic_DNA.
EMBL; AY692658; AAT92677.1; -; Genomic_DNA.
EMBL; AY899254; AAX83939.1; -; mRNA.
EMBL; U12141; AAA99665.1; -; Genomic_DNA.
EMBL; BK006947; DAA10498.1; -; Genomic_DNA.
PIR; S61097; S61097.
RefSeq; NP_014351.3; NM_001182886.3.
ProteinModelPortal; P53955; -.
SMR; P53955; -.
BioGrid; 35777; 154.
DIP; DIP-1269N; -.
IntAct; P53955; 10.
MINT; MINT-397465; -.
STRING; 4932.YNL047C; -.
iPTMnet; P53955; -.
MaxQB; P53955; -.
PRIDE; P53955; -.
EnsemblFungi; YNL047C; YNL047C; YNL047C.
GeneID; 855680; -.
KEGG; sce:YNL047C; -.
EuPathDB; FungiDB:YNL047C; -.
SGD; S000004992; SLM2.
GeneTree; ENSGT00390000002928; -.
HOGENOM; HOG000066129; -.
InParanoid; P53955; -.
OMA; YLPERTT; -.
OrthoDB; EOG092C2NCC; -.
BioCyc; YEAST:G3O-33081-MONOMER; -.
PRO; PR:P53955; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0031932; C:TORC2 complex; IEA:InterPro.
GO; GO:0035091; F:phosphatidylinositol binding; TAS:SGD.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
GO; GO:0030036; P:actin cytoskeleton organization; IGI:SGD.
GO; GO:0051017; P:actin filament bundle assembly; IGI:SGD.
GO; GO:0070941; P:eisosome assembly; IGI:SGD.
GO; GO:0016197; P:endosomal transport; IGI:SGD.
GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IPI:SGD.
GO; GO:0072659; P:protein localization to plasma membrane; IGI:SGD.
GO; GO:0001558; P:regulation of cell growth; IGI:SGD.
GO; GO:0031929; P:TOR signaling; IPI:SGD.
GO; GO:0038203; P:TORC2 signaling; IEA:InterPro.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR033191; Slm1/Slm2.
PANTHER; PTHR31941:SF7; PTHR31941:SF7; 2.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Membrane; Phosphoprotein;
Reference proteome.
CHAIN 1 656 Phosphatidylinositol 4,5-bisphosphate-
binding protein SLM2.
/FTId=PRO_0000203453.
DOMAIN 445 555 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
MOTIF 640 645 PXIXIT-like, required for interaction
with CNA1 and CNA2, and calcineurin-
dependent dephosphorylation.
MOD_RES 626 626 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
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


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