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Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1 (Synthetic lethal with MSS4 protein 1) (TORC2 effector protein SLM1)

 SLM1_YEAST              Reviewed;         686 AA.
P40485; D6VVI2;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-NOV-2017, entry version 149.
RecName: Full=Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1;
AltName: Full=Synthetic lethal with MSS4 protein 1;
AltName: Full=TORC2 effector protein SLM1;
Name=SLM1; Synonyms=LIT2; OrderedLocusNames=YIL105C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169870;
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[2]
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).
[3]
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).
[4]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY TORC2, MUTAGENESIS
OF LYS-483 AND LYS-487, AND INTERACTION WITH SLM2 AND AVO2.
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).
[5]
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).
[6]
FUNCTION, PHOSPHOINOSITIDE-BINDING, INTERACTION WITH AVO2; BIT2; BIT61
AND TOR2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 477-ARG-ARG-478;
LYS-483 AND LYS-487.
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).
[7]
FUNCTION, AND INTERACTION WITH CNA1 AND TOR2.
PubMed=16959779; DOI=10.1074/jbc.M604244200;
Mulet J.M., Martin D.E., Loewith R., Hall M.N.;
"Mutual antagonism of TOR and calcineurin signaling.";
J. Biol. Chem. 281:33000-33007(2006).
[8]
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).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-150 AND
SER-153, 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 SLM2, 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. Dephosphorylation inhibits
its 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,
ECO:0000269|PubMed:16959779}.
-!- 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, ECO:0000269|PubMed:16959779}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-25172, EBI-25172;
-!- 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}.
Note=Localizes to cortical punctate structures. Correct
localization requires phosphatidylinositol 4,5-bisphosphate and
functional TORC2.
-!- PTM: Phosphorylated by the target of rapamycin complex 2 (TORC2)
and dephosphorylated by serine/threonine-protein phosphatase 2B
(calcineurin). {ECO:0000269|PubMed:15372071}.
-!- MISCELLANEOUS: Present with 5190 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; Z38125; CAA86275.1; -; Genomic_DNA.
EMBL; BK006942; DAA08448.1; -; Genomic_DNA.
PIR; S48467; S48467.
RefSeq; NP_012161.1; NM_001179453.1.
PDB; 3NSU; X-ray; 2.00 A; A/B=469-583.
PDB; 4A5K; X-ray; 1.76 A; A/B/C/D=469-583.
PDB; 4A6F; X-ray; 1.68 A; A/B=469-583.
PDB; 4A6H; X-ray; 1.45 A; A/B/C/D=469-583.
PDB; 4A6K; X-ray; 1.80 A; A/B/C/D=469-583.
PDBsum; 3NSU; -.
PDBsum; 4A5K; -.
PDBsum; 4A6F; -.
PDBsum; 4A6H; -.
PDBsum; 4A6K; -.
ProteinModelPortal; P40485; -.
SMR; P40485; -.
BioGrid; 34886; 145.
DIP; DIP-1353N; -.
ELM; P40485; -.
IntAct; P40485; 27.
MINT; MINT-387224; -.
STRING; 4932.YIL105C; -.
iPTMnet; P40485; -.
MaxQB; P40485; -.
PRIDE; P40485; -.
EnsemblFungi; YIL105C; YIL105C; YIL105C.
GeneID; 854701; -.
KEGG; sce:YIL105C; -.
EuPathDB; FungiDB:YIL105C; -.
SGD; S000001367; SLM1.
GeneTree; ENSGT00390000002928; -.
HOGENOM; HOG000066129; -.
InParanoid; P40485; -.
OMA; RTENEIH; -.
OrthoDB; EOG092C2NCC; -.
BioCyc; YEAST:G3O-31361-MONOMER; -.
PRO; PR:P40485; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0031932; C:TORC2 complex; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:SGD.
GO; GO:0046625; F:sphingolipid binding; IDA:SGD.
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;
3D-structure; Cell membrane; Coiled coil; Complete proteome; Membrane;
Phosphoprotein; Reference proteome.
CHAIN 1 686 Phosphatidylinositol 4,5-bisphosphate-
binding protein SLM1.
/FTId=PRO_0000202965.
DOMAIN 468 581 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
COILED 296 381 {ECO:0000255}.
MOTIF 673 678 PXIXIT-like, required for interaction
with CNA1 and CNA2, and calcineurin-
dependent dephosphorylation.
COMPBIAS 45 63 Poly-Gln.
COMPBIAS 133 136 Poly-Asn.
COMPBIAS 166 172 Poly-Gln.
MOD_RES 145 145 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 477 478 RR->AA: In SLM1-PHM2; reduces
phosphoinositide binding by 95%; when
associated with A-487.
{ECO:0000269|PubMed:15689497}.
MUTAGEN 483 483 K->A: In SLM1-PHM1; reduces
phosphoinositide binding by 80% and
causes mislocalization to the cytoplasm;
when associated with A-487.
{ECO:0000269|PubMed:15372071,
ECO:0000269|PubMed:15689497}.
MUTAGEN 487 487 K->A: In SLM1-PHM1; reduces
phosphoinositide binding by 80% and
causes mislocalization to the cytoplasm;
when associated with A-483. In SLM1-PHM2;
reduces phosphoinositide binding by 95%;
when associated with 477-AA-478.
{ECO:0000269|PubMed:15372071,
ECO:0000269|PubMed:15689497}.
STRAND 470 479 {ECO:0000244|PDB:4A6H}.
TURN 480 483 {ECO:0000244|PDB:4A6H}.
STRAND 484 492 {ECO:0000244|PDB:4A6H}.
STRAND 494 502 {ECO:0000244|PDB:4A6H}.
TURN 505 507 {ECO:0000244|PDB:4A6H}.
STRAND 512 516 {ECO:0000244|PDB:4A6H}.
HELIX 517 519 {ECO:0000244|PDB:4A6H}.
STRAND 520 525 {ECO:0000244|PDB:4A6H}.
STRAND 530 533 {ECO:0000244|PDB:3NSU}.
STRAND 542 553 {ECO:0000244|PDB:4A6H}.
STRAND 558 562 {ECO:0000244|PDB:4A6H}.
HELIX 566 579 {ECO:0000244|PDB:4A6H}.
SEQUENCE 686 AA; 77995 MW; 849C82CC0960014B CRC64;
MSKNNTMTSA VSDMLSQQQL NLQHLHNLQQ HTRSMTSADH ANVLQQQQQQ QQQQQQQQQQ
QQQSASFQNG SLTSDINQQS YLNGQPVPST SNSTFQNNRT LTMNSGGLQG IISNGSPNID
SNTNVTIAVP DPNNNNGKQL QGKNSLTNTS ILSRARSSLQ RQRLAQQQQQ QQDPRSPLVI
LVPTAAQPTD ILAARFSAWR NVIKSVIVYL TEIASIQDEI VRQQLRLSHA VQFPFFSIEN
QYQPSSQEDK SVQKFFLPLG NGSIQDLPTI LNQYHESLAS SASKASRELT NDVIPRLEDL
RRDLIVKIKE IKSLQSDFKN SCSKELQQTK QAMKQFQESL KDARYSVPKQ DPFLTKLALD
RQIKKQLQEE NFLHEAFDNL ETSGAELEKI VVMEIQNSLT IYARLLGQEA QLVFDILISK
LDSGFFNVDP QFEWDNFISR DPNFLLPNLP MRTFKEIVYK YQFDPLTYEI KSGFLERRSK
FLKSYSKGYY VLTPNFLHEF KTADRKKDLV PVMSLALSEC TVTEHSRKNS TSSPNSTGSD
AKFVLHAKQN GIIRRGHNWV FKADSYESMM SWFDNLKILT STSNIQDKYK FITQKLNLNS
DGKPKLTNNH TSINKYQLSN ANSTMVENDE NDDINSNYVG STVTPKLDNQ TNTNTSMSSL
PDTNDSELQD QVPNIYIQTP INDFKS


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