LAS17_YEAST
ID LAS17_YEAST Reviewed; 633 AA.
AC Q12446; D6W2N7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Proline-rich protein LAS17;
GN Name=LAS17; OrderedLocusNames=YOR181W;
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].
RA Toh-e A.;
RT "Yeast mutants sensitive to local anesthetics.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 INTERACTION WITH LSB3; LSB5 AND YSC84.
RX PubMed=10512884; DOI=10.1091/mbc.10.10.3521;
RA Madania A., Dumoulin P., Grava S., Kitamoto H., Scharer-Brodbeck C.,
RA Soulard A., Moreau V., Winsor B.;
RT "The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome
RT protein Las17p interacts with the Arp2/3 complex.";
RL Mol. Biol. Cell 10:3521-3538(1999).
RN [5]
RP INTERACTION WITH KRE6.
RX PubMed=12237851; DOI=10.1002/yea.904;
RA Li H., Page N., Bussey H.;
RT "Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth
RT to daughter cells and interact with cis-Golgi protein Kre6p.";
RL Yeast 19:1097-1112(2002).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334 AND SER-337, 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 -!- SUBUNIT: Interacts with KRE6, LSB3, LSB5 and YSC84.
CC {ECO:0000269|PubMed:10512884, ECO:0000269|PubMed:12237851}.
CC -!- INTERACTION:
CC Q12446; P60010: ACT1; NbExp=4; IntAct=EBI-10022, EBI-2169;
CC Q12446; P38328: ARC40; NbExp=2; IntAct=EBI-10022, EBI-2777;
CC Q12446; P38822: BZZ1; NbExp=17; IntAct=EBI-10022, EBI-3889;
CC Q12446; Q05080: HOF1; NbExp=3; IntAct=EBI-10022, EBI-5412;
CC Q12446; P43603: LSB3; NbExp=8; IntAct=EBI-10022, EBI-22980;
CC Q12446; P25369: LSB5; NbExp=3; IntAct=EBI-10022, EBI-10218;
CC Q12446; P36006: MYO3; NbExp=3; IntAct=EBI-10022, EBI-11670;
CC Q12446; Q04439: MYO5; NbExp=7; IntAct=EBI-10022, EBI-11687;
CC Q12446; P80667: PEX13; NbExp=2; IntAct=EBI-10022, EBI-13206;
CC Q12446; Q06449: PIN3; NbExp=4; IntAct=EBI-10022, EBI-35523;
CC Q12446; P39743: RVS167; NbExp=14; IntAct=EBI-10022, EBI-14500;
CC Q12446; P40073: SHO1; NbExp=5; IntAct=EBI-10022, EBI-18140;
CC Q12446; P32790: SLA1; NbExp=7; IntAct=EBI-10022, EBI-17313;
CC Q12446; P37370: VRP1; NbExp=6; IntAct=EBI-10022, EBI-20502;
CC Q12446; P32793: YSC84; NbExp=7; IntAct=EBI-10022, EBI-24460;
CC -!- MISCELLANEOUS: Present with 8580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; D78487; BAA11386.1; -; Genomic_DNA.
DR EMBL; Z75089; CAA99390.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10953.1; -; Genomic_DNA.
DR PIR; S62057; S62057.
DR RefSeq; NP_014824.1; NM_001183600.1.
DR PDB; 1ZUK; X-ray; 1.90 A; C=350-360.
DR PDBsum; 1ZUK; -.
DR AlphaFoldDB; Q12446; -.
DR SMR; Q12446; -.
DR BioGRID; 34576; 745.
DR ComplexPortal; CPX-1344; SLAC complex.
DR DIP; DIP-963N; -.
DR IntAct; Q12446; 71.
DR MINT; Q12446; -.
DR STRING; 4932.YOR181W; -.
DR iPTMnet; Q12446; -.
DR MaxQB; Q12446; -.
DR PaxDb; Q12446; -.
DR PRIDE; Q12446; -.
DR EnsemblFungi; YOR181W_mRNA; YOR181W; YOR181W.
DR GeneID; 854353; -.
DR KEGG; sce:YOR181W; -.
DR SGD; S000005707; LAS17.
DR VEuPathDB; FungiDB:YOR181W; -.
DR eggNOG; KOG3671; Eukaryota.
DR GeneTree; ENSGT00940000176200; -.
DR HOGENOM; CLU_015385_1_2_1; -.
DR InParanoid; Q12446; -.
DR OMA; VGNTYWI; -.
DR BioCyc; YEAST:G3O-33692-MON; -.
DR EvolutionaryTrace; Q12446; -.
DR PRO; PR:Q12446; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12446; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0140224; C:SLAC complex; IDA:SGD.
DR GO; GO:0003779; F:actin binding; IDA:SGD.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:SGD.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:SGD.
DR GO; GO:0007015; P:actin filament organization; IDA:SGD.
DR GO; GO:0030041; P:actin filament polymerization; IMP:SGD.
DR GO; GO:0045010; P:actin nucleation; IDA:SGD.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IDA:SGD.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IDA:ComplexPortal.
DR CDD; cd01205; EVH1_WASP-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR027641; WASP.
DR InterPro; IPR033927; WASPfam_EVH1.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23202:SF79; PTHR23202:SF79; 1.
DR Pfam; PF00568; WH1; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00461; WH1; 1.
DR PROSITE; PS50229; WH1; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome.
FT CHAIN 1..633
FT /note="Proline-rich protein LAS17"
FT /id="PRO_0000084361"
FT DOMAIN 16..127
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT DOMAIN 547..567
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 145..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..278
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..530
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 633 AA; 67572 MW; 4488355563AA2645 CRC64;
MGLLNSSDKE IIKRALPKAS NKIIDVTVAR LYIAYPDKNE WQYTGLSGAL ALVDDLVGNT
FFLKLVDING HRGVIWDQEL YVNFEYYQDR TFFHTFEMEE CFAGLLFVDI NEASHFLKRV
QKRERYANRK TLLNKNAVAL TKKVREEQKS QVVHGPRGES LIDNQRKRYN YEDVDTIPTT
KHKAPPPPPP TAETFDSDQT SSFSDINSTT ASAPTTPAPA LPPASPEVRK EETHPKHSLP
PLPNQFAPLP DPPQHNSPPQ NNAPSQPQSN PFPFPIPEIP STQSATNPFP FPVPQQQFNQ
APSMGIPQQN RPLPQLPNRN NRPVPPPPPM RTTTEGSGVR LPAPPPPPRR GPAPPPPPHR
HVTSNTLNSA GGNSLLPQAT GRRGPAPPPP PRASRPTPNV TMQQNPQQYN NSNRPFGYQT
NSNMSSPPPP PVTTFNTLTP QMTAATGQPA VPLPQNTQAP SQATNVPVAP PPPPASLGQS
QIPQSAPSAP IPPTLPSTTS AAPPPPPAFL TQQPQSGGAP APPPPPQMPA TSTSGGGSFA
ETTGDAGRDA LLASIRGAGG IGALRKVDKS QLDKPSVLLQ EARGESASPP AAAGNGGTPG
GPPASLADAL AAALNKRKTK VGAHDDMDNG DDW
