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 02-SEP-2026, entry version 199. 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; P38870: RGD3; NbExp=2; IntAct=EBI-22980, EBI-24848; 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; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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=400-459. DR PDB; 1SSH; X-ray; 1.40 A; A=400-459. DR AlphaFoldDB; P43603; -. DR SMR; P43603; -. DR BioGRID; 31177; 266. DR DIP; DIP-6259N; -. DR FunCoup; P43603; 224. DR IntAct; P43603; 147. DR MINT; P43603; -. DR STRING; 4932.YFR024C-A; -. DR GlyGen; P43603; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; P43603; -. DR PaxDb; 4932-YFR024C-A; -. DR PeptideAtlas; P43603; -. DR EnsemblFungi; YFR024C-A_mRNA; YFR024C-A; YFR024C-A. DR GeneID; 850580; -. DR KEGG; sce:YFR024C-A; -. DR AGR; SGD:S000002968; -. DR SGD; S000002968; LSB3. DR VEuPathDB; FungiDB:YFR024C-A; -. DR eggNOG; KOG1843; Eukaryota. DR HOGENOM; CLU_015320_2_0_1; -. DR InParanoid; P43603; -. DR OMA; SNCKARN; -. DR OrthoDB; 443981at2759; -. DR BioCyc; YEAST:G3O-30504-MONOMER; -. DR BioGRID-ORCS; 850580; 6 hits in 10 CRISPR screens. 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; cd11842; SH3_Ysc84p_like; 1. DR CDD; cd11525; SYLF_SH3YL1_like; 1. DR FunFam; 2.30.30.40:FF:000100; SH3 domain-containing YSC84-like protein 1; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR051702; SH3_domain_YSC84-like. DR InterPro; IPR033643; SYLF_SH3YL1-like. DR InterPro; IPR007461; Ysc84_actin-binding. DR PANTHER; PTHR15629:SF2; SH3 DOMAIN-CONTAINING YSC84-LIKE PROTEIN 1; 1. DR PANTHER; PTHR15629; SH3YL1 PROTEIN; 1. DR Pfam; PF00018; SH3_1; 1. DR Pfam; PF04366; Ysc84; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. DR PDBsum; 1OOT; -. DR PDBsum; 1SSH; -. 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 229..242 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..262 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 289..300 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 340..350 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 351..371 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 372..391 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 393..403 FT /note="Low complexity" 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 //