LSB3_YEAST
ID LSB3_YEAST Reviewed; 459 AA.
AC P43603; D6VTQ4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=LAS seventeen-binding protein 3;
DE Short=LAS17-binding protein 3;
GN Name=LSB3; OrderedLocusNames=YFR024C-A; ORFNames=YFR024C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-303; THR-393 AND
RP SER-402, AND IDENTIFICATION BY 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-303 AND SER-416, 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 [6]
RP REVISION OF GENE MODEL.
RG Saccharomyces Genome Database (SGD);
RL Unpublished observations (JUN-2008).
RN [7]
RP INTERACTION WITH LAS17.
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 [8]
RP IDENTIFICATION OF INTRON.
RX PubMed=10734188; DOI=10.1093/nar/28.8.1700;
RA Davis C.A., Grate L., Spingola M., Ares M. Jr.;
RT "Test of intron predictions reveals novel splice sites, alternatively
RT spliced mRNAs and new introns in meiotically regulated genes of yeast.";
RL Nucleic Acids Res. 28:1700-1706(2000).
RN [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; THR-298; SER-300;
RP SER-303; THR-393; SER-397 AND SER-402, AND IDENTIFICATION BY MASS
RP 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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 393-451.
RA Kursula P., Lehmann F., Song Y.H., Wilmanns M.;
RT "Crystal structure of the SH3 domain from a S.cerevisiae hypothetical 40.4
RT kDa protein at 1.39 A resolution.";
RL Submitted (APR-2004) to the PDB data bank.
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 393-451.
RA Kursula P., Kursula I., Lehmann F., Song Y.H., Wilmanns M.;
RT "Yeast SH3 domain structural genomics.";
RL Submitted (APR-2005) to the PDB data bank.
CC -!- SUBUNIT: Interacts with LAS17. {ECO:0000269|PubMed:10512884}.
CC -!- INTERACTION:
CC P43603; P15891: ABP1; NbExp=6; IntAct=EBI-22980, EBI-2036;
CC P43603; Q12168: ACF2; NbExp=7; IntAct=EBI-22980, EBI-32973;
CC P43603; P47129: ACF4; NbExp=4; IntAct=EBI-22980, EBI-25556;
CC P43603; P38090: AGP2; NbExp=2; IntAct=EBI-22980, EBI-2362;
CC P43603; P40563: AIM21; NbExp=2; IntAct=EBI-22980, EBI-25376;
CC P43603; P38266: AIM3; NbExp=4; IntAct=EBI-22980, EBI-21584;
CC P43603; P53933: APP1; NbExp=8; IntAct=EBI-22980, EBI-28798;
CC P43603; Q06604: BSP1; NbExp=7; IntAct=EBI-22980, EBI-37047;
CC P43603; P09119: CDC6; NbExp=2; IntAct=EBI-22980, EBI-4447;
CC P43603; Q12510: CMR1; NbExp=2; IntAct=EBI-22980, EBI-35343;
CC P43603; Q08412: CUE5; NbExp=8; IntAct=EBI-22980, EBI-37580;
CC P43603; P38140: ERT1; NbExp=3; IntAct=EBI-22980, EBI-21048;
CC P43603; P40956: GTS1; NbExp=4; IntAct=EBI-22980, EBI-7968;
CC P43603; Q04322: GYL1; NbExp=6; IntAct=EBI-22980, EBI-27427;
CC P43603; Q12344: GYP5; NbExp=3; IntAct=EBI-22980, EBI-38508;
CC P43603; P40325: HUA1; NbExp=5; IntAct=EBI-22980, EBI-23614;
CC P43603; Q12446: LAS17; NbExp=8; IntAct=EBI-22980, EBI-10022;
CC P43603; P43603: LSB3; NbExp=3; IntAct=EBI-22980, EBI-22980;
CC P43603; P33400: RIM101; NbExp=2; IntAct=EBI-22980, EBI-14422;
CC P43603; P53118: ROG1; NbExp=2; IntAct=EBI-22980, EBI-24005;
CC P43603; P32855: SEC8; NbExp=3; IntAct=EBI-22980, EBI-16896;
CC P43603; P32790: SLA1; NbExp=7; IntAct=EBI-22980, EBI-17313;
CC P43603; P53955: SLM2; NbExp=2; IntAct=EBI-22980, EBI-28706;
CC P43603; P25604: STP22; NbExp=3; IntAct=EBI-22980, EBI-411625;
CC P43603; P40453: UBP7; NbExp=2; IntAct=EBI-22980, EBI-19857;
CC P43603; P53169: YBP2; NbExp=2; IntAct=EBI-22980, EBI-23796;
CC P43603; P38870: YHR182W; NbExp=2; IntAct=EBI-22980, EBI-24848;
CC P43603; P32793: YSC84; NbExp=4; IntAct=EBI-22980, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylation of Ser-397 is induced 2-fold in response to mating
CC pheromone.
CC -!- MISCELLANEOUS: Present with 18000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SH3YL1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09263.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D50617; BAA09263.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006940; DAA12464.1; -; Genomic_DNA.
DR RefSeq; NP_219497.4; NM_001180865.3.
DR PDB; 1OOT; X-ray; 1.39 A; A=401-459.
DR PDB; 1SSH; X-ray; 1.40 A; A=401-459.
DR PDBsum; 1OOT; -.
DR PDBsum; 1SSH; -.
DR AlphaFoldDB; P43603; -.
DR SMR; P43603; -.
DR BioGRID; 31177; 235.
DR DIP; DIP-6259N; -.
DR IntAct; P43603; 133.
DR MINT; P43603; -.
DR STRING; 4932.YFR024C-A; -.
DR iPTMnet; P43603; -.
DR MaxQB; P43603; -.
DR PaxDb; P43603; -.
DR PRIDE; P43603; -.
DR EnsemblFungi; YFR024C-A_mRNA; YFR024C-A; YFR024C-A.
DR GeneID; 850580; -.
DR KEGG; sce:YFR024C-A; -.
DR SGD; S000002968; LSB3.
DR VEuPathDB; FungiDB:YFR024C-A; -.
DR eggNOG; KOG1843; Eukaryota.
DR GeneTree; ENSGT00510000048137; -.
DR HOGENOM; CLU_015320_2_0_1; -.
DR InParanoid; P43603; -.
DR OMA; NDAMYND; -.
DR BioCyc; YEAST:G3O-30504-MON; -.
DR EvolutionaryTrace; P43603; -.
DR PRO; PR:P43603; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43603; protein.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:SGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR CDD; cd11525; SYLF_SH3YL1_like; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR033643; SYLF_SH3YL1-like.
DR InterPro; IPR007461; Ysc84_actin-binding.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF04366; Ysc84; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..459
FT /note="LAS seventeen-binding protein 3"
FT /id="PRO_0000202691"
FT DOMAIN 400..459
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 219..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 393
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:1OOT"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:1OOT"
FT STRAND 438..444
FT /evidence="ECO:0007829|PDB:1OOT"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:1OOT"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:1OOT"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:1OOT"
SQ SEQUENCE 459 AA; 49344 MW; F486C787B5771AAC CRC64;
MGINNPIPRS LKSETKKAAK ILASFVKPNQ VFGADQVIPP DVLKRAKGLA IITILKAGFL
FSGRAGSGVI VARLKDGTWS APSAIAMAGA GAGGMVGIEL TDFVFILNTQ DAVKSFSEFG
TITLGGNVSV SAGPLGRSAE AAASASAGGV AAVFAYSKSK GLFAGVSVEG SAIIERREAN
RKFYGDNCTA KMILSGRIRP PPAVDPLFRV LESRAFNYRP SNGGRGSFDD DEDDYYDDDD
YYNDIPSSFS STDASSTRPN TRSTRRRAQS GSRYTFDDDD DDDDYGTGYS RNSRLAPTNS
GGSGGKLDDP SGASSYYASH RRSGTAQSRA RSSRNRWADD EYDDYDDDYE SGYRRGNGRD
RTKDREVDDL SNRFSKSRIS SASTPQTSQG RFTAPTSPST SSPKAVALYS FAGEESGDLP
FRKGDVITIL KKSDSQNDWW TGRVNGREGI FPANYVELV
