YSC84_YEAST
ID YSC84_YEAST Reviewed; 468 AA.
AC P32793; D3DKW1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protein YSC84;
DE AltName: Full=LAS seventeen-binding protein 4;
DE Short=LAS17-binding protein 4;
GN Name=YSC84; Synonyms=LSB4; OrderedLocusNames=YHR016C;
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], AND INDUCTION.
RX PubMed=8256520; DOI=10.1002/yea.320091012;
RA Rocco V., Daly M.J., Matre V., Lichten M., Nicolas A.;
RT "Identification of two divergently transcribed genes centromere-proximal to
RT the ARG4 locus on chromosome VIII of Saccharomyces cerevisiae.";
RL Yeast 9:1111-1120(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 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 [5]
RP FUNCTION, INTERACTION WITH SLA1, AND SUBCELLULAR LOCATION.
RX PubMed=12388763; DOI=10.1091/mbc.e02-05-0262;
RA Dewar H., Warren D.T., Gardiner F.C., Gourlay C.G., Satish N.,
RA Richardson M.R., Andrews P.D., Ayscough K.R.;
RT "Novel proteins linking the actin cytoskeleton to the endocytic machinery
RT in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 13:3646-3661(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-311, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-311, 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 -!- FUNCTION: Essential for the organization of the actin cytoskeleton,
CC fluid phase endocytosis and vesicle trafficking, together with LSB5.
CC {ECO:0000269|PubMed:12388763}.
CC -!- SUBUNIT: Interacts with LAS17 and SLA1. {ECO:0000269|PubMed:10512884,
CC ECO:0000269|PubMed:12388763}.
CC -!- INTERACTION:
CC P32793; P15891: ABP1; NbExp=4; IntAct=EBI-24460, EBI-2036;
CC P32793; Q12168: ACF2; NbExp=7; IntAct=EBI-24460, EBI-32973;
CC P32793; P47129: ACF4; NbExp=4; IntAct=EBI-24460, EBI-25556;
CC P32793; P38090: AGP2; NbExp=2; IntAct=EBI-24460, EBI-2362;
CC P32793; P38266: AIM3; NbExp=5; IntAct=EBI-24460, EBI-21584;
CC P32793; P53933: APP1; NbExp=6; IntAct=EBI-24460, EBI-28798;
CC P32793; Q06604: BSP1; NbExp=6; IntAct=EBI-24460, EBI-37047;
CC P32793; Q12510: CMR1; NbExp=2; IntAct=EBI-24460, EBI-35343;
CC P32793; Q08412: CUE5; NbExp=7; IntAct=EBI-24460, EBI-37580;
CC P32793; P38140: ERT1; NbExp=4; IntAct=EBI-24460, EBI-21048;
CC P32793; P40956: GTS1; NbExp=4; IntAct=EBI-24460, EBI-7968;
CC P32793; Q04322: GYL1; NbExp=6; IntAct=EBI-24460, EBI-27427;
CC P32793; Q12344: GYP5; NbExp=2; IntAct=EBI-24460, EBI-38508;
CC P32793; P40325: HUA1; NbExp=3; IntAct=EBI-24460, EBI-23614;
CC P32793; Q12446: LAS17; NbExp=7; IntAct=EBI-24460, EBI-10022;
CC P32793; P43603: LSB3; NbExp=4; IntAct=EBI-24460, EBI-22980;
CC P32793; Q08229: NBA1; NbExp=2; IntAct=EBI-24460, EBI-36841;
CC P32793; Q12164: POM33; NbExp=2; IntAct=EBI-24460, EBI-30000;
CC P32793; P33400: RIM101; NbExp=2; IntAct=EBI-24460, EBI-14422;
CC P32793; P32855: SEC8; NbExp=4; IntAct=EBI-24460, EBI-16896;
CC P32793; P32790: SLA1; NbExp=7; IntAct=EBI-24460, EBI-17313;
CC P32793; P25604: STP22; NbExp=2; IntAct=EBI-24460, EBI-411625;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:12388763}. Note=Cortical actin patches.
CC -!- INDUCTION: Induced during sporulation. {ECO:0000269|PubMed:8256520}.
CC -!- SIMILARITY: Belongs to the SH3YL1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA56990.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U10400; AAB68945.1; -; Genomic_DNA.
DR EMBL; L06795; AAA56990.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006934; DAA06705.1; -; Genomic_DNA.
DR PIR; S46791; S46791.
DR RefSeq; NP_011880.1; NM_001179146.1.
DR PDB; 2A08; X-ray; 1.54 A; A/B=413-468.
DR PDBsum; 2A08; -.
DR AlphaFoldDB; P32793; -.
DR SMR; P32793; -.
DR BioGRID; 36445; 84.
DR DIP; DIP-2026N; -.
DR IntAct; P32793; 86.
DR MINT; P32793; -.
DR STRING; 4932.YHR016C; -.
DR iPTMnet; P32793; -.
DR MaxQB; P32793; -.
DR PaxDb; P32793; -.
DR PRIDE; P32793; -.
DR EnsemblFungi; YHR016C_mRNA; YHR016C; YHR016C.
DR GeneID; 856409; -.
DR KEGG; sce:YHR016C; -.
DR SGD; S000001058; YSC84.
DR VEuPathDB; FungiDB:YHR016C; -.
DR eggNOG; KOG1843; Eukaryota.
DR GeneTree; ENSGT00510000048137; -.
DR HOGENOM; CLU_015320_2_0_1; -.
DR InParanoid; P32793; -.
DR OMA; VYDQQPR; -.
DR BioCyc; YEAST:G3O-31078-MON; -.
DR EvolutionaryTrace; P32793; -.
DR PRO; PR:P32793; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P32793; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:SGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:SGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:SGD.
DR GO; GO:0006897; P:endocytosis; IGI:SGD.
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; Cytoskeleton; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..468
FT /note="Protein YSC84"
FT /id="PRO_0000202887"
FT DOMAIN 409..468
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 220..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:2A08"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:2A08"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:2A08"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:2A08"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:2A08"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:2A08"
SQ SEQUENCE 468 AA; 50902 MW; DE42E8ECF5B83C92 CRC64;
MGINNPIPRS LKSETKKAAK VLRSFVKPNQ VFGADQVIPP YVLKRAKGLA IITVLKAGFL
FSGRAGSGVI VARLKDGTWS APSAIAMAGA GAGGMVGVEL TDFVFILNSE EAVRSFSEFG
TITLGGNVSV SAGPLGRSAE AAASASTGGV SAVFAYSKSK GLFAGVSVEG SAILERREAN
RKFYGDNCTS KMILSGRVKV PPAADPLLRI LESRAFNFTR HDHDDNASGD DFYDDGQYSD
NTSHYYDDIP DSFDSTDESS TRPNTRSSRR RGMSLGSRSR YDDDYDDDGY GRGRGYGDFD
SEDEDYDYGR SPNRNSSRNR GPQIDRGTKP RANTRWEDDL YDRDTEYSRP NHSGRDYDNT
RGNRRGYGRE RGYSLGHGPT HPSNMSNVDD LSHKMSKTGL GNESTATNSA TPTAVALYNF
AGEQPGDLAF KKGDVITILK KSDSQNDWWT GRTNGKEGIF PANYVRVS
