ID SLA1_YEAST Reviewed; 1244 AA.
AC P32790; D6VPZ3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 27-MAR-2024, entry version 220.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1;
GN Name=SLA1; OrderedLocusNames=YBL007C; ORFNames=YBL0321;
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 FUNCTION.
RC STRAIN=DDY 228;
RX PubMed=8335689; DOI=10.1083/jcb.122.3.635;
RA Holtzman D.A., Yang S., Drubin D.G.;
RT "Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2,
RT that control membrane cytoskeleton assembly in Saccharomyces cerevisiae.";
RL J. Cell Biol. 122:635-644(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441753; DOI=10.1002/yea.320080909;
RA Delaveau T., Jacq C., Perea J.;
RT "Sequence of a 12.7 kb segment of yeast chromosome II identifies a PDR-like
RT gene and several new open reading frames.";
RL Yeast 8:761-768(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=8756649; DOI=10.1128/mcb.16.9.4897;
RA Tang H.-Y., Cai M.;
RT "The EH-domain-containing protein Pan1 is required for normal organization
RT of the actin cytoskeleton in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:4897-4914(1996).
RN [6]
RP FUNCTION.
RX PubMed=9008707; DOI=10.1083/jcb.136.1.111;
RA Yang S., Ayscough K.R., Drubin D.G.;
RT "A role for the actin cytoskeleton of Saccharomyces cerevisiae in bipolar
RT bud-site selection.";
RL J. Cell Biol. 136:111-123(1997).
RN [7]
RP INTERACTION WITH LAS17.
RX PubMed=9024694; DOI=10.1083/jcb.136.3.649;
RA Li R.;
RT "Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein,
RT is critical for the assembly of cortical actin cytoskeleton.";
RL J. Cell Biol. 136:649-658(1997).
RN [8]
RP FUNCTION.
RX PubMed=9128251; DOI=10.1083/jcb.137.2.399;
RA Ayscough K.R., Stryker J., Pokala N., Sanders M., Crews P., Drubin D.G.;
RT "High rates of actin filament turnover in budding yeast and roles for actin
RT in establishment and maintenance of cell polarity revealed using the actin
RT inhibitor latrunculin-A.";
RL J. Cell Biol. 137:399-416(1997).
RN [9]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10198057; DOI=10.1091/mbc.10.4.1061;
RA Ayscough K.R., Eby J.J., Lila T., Dewar H., Kozminski K.G., Drubin D.G.;
RT "Sla1p is a functionally modular component of the yeast cortical actin
RT cytoskeleton required for correct localization of both Rho1p-GTPase and
RT Sla2p, a protein with talin homology.";
RL Mol. Biol. Cell 10:1061-1075(1999).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN THE PAN1 COMPLEX.
RX PubMed=10594004; DOI=10.1128/mcb.20.1.12-25.2000;
RA Tang H.-Y., Xu J., Cai M.;
RT "Pan1p, End3p, and Sla1p, three yeast proteins required for normal cortical
RT actin cytoskeleton organization, associate with each other and play
RT essential roles in cell wall morphogenesis.";
RL Mol. Cell. Biol. 20:12-25(2000).
RN [11]
RP IDENTIFICATION IN THE PAN1 COMPLEX, PHOSPHORYLATION BY PRK1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11739778; DOI=10.1091/mbc.12.12.3759;
RA Zeng G., Yu X., Cai M.;
RT "Regulation of yeast actin cytoskeleton-regulatory complex
RT Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p.";
RL Mol. Biol. Cell 12:3759-3772(2001).
RN [12]
RP FUNCTION.
RX PubMed=11940605; DOI=10.1083/jcb.200110027;
RA Howard J.P., Hutton J.L., Olson J.M., Payne G.S.;
RT "Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-
RT mediated endocytosis.";
RL J. Cell Biol. 157:315-326(2002).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ABP1 AND LAS17.
RX PubMed=11950888; DOI=10.1242/jcs.115.8.1703;
RA Warren D.T., Andrews P.D., Gourlay C.W., Ayscough K.R.;
RT "Sla1p couples the yeast endocytic machinery to proteins regulating actin
RT dynamics.";
RL J. Cell Sci. 115:1703-1715(2002).
RN [14]
RP FUNCTION, AND INTERACTION WITH LSB5 AND YSC84.
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 [15]
RP FUNCTION, AND 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 [16]
RP FUNCTION.
RX PubMed=12814545; DOI=10.1016/s0960-9822(03)00383-x;
RA Rodal A.A., Manning A.L., Goode B.L., Drubin D.G.;
RT "Negative regulation of yeast WASp by two SH3 domain-containing proteins.";
RL Curr. Biol. 13:1000-1008(2003).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SLA2.
RX PubMed=12734398; DOI=10.1242/jcs.00454;
RA Gourlay C.W., Dewar H., Warren D.T., Costa R., Satish N., Ayscough K.R.;
RT "An interaction between Sla1p and Sla2p plays a role in regulating actin
RT dynamics and endocytosis in budding yeast.";
RL J. Cell Sci. 116:2551-2564(2003).
RN [18]
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 [19]
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 [20]
RP FUNCTION, AND INTERACTION WITH RSP5 AND RVS167.
RX PubMed=14761940; DOI=10.1074/jbc.m313479200;
RA Stamenova S.D., Dunn R., Adler A.S., Hicke L.;
RT "The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast
RT CIN85-endophilin complex, Sla1-Rvs167.";
RL J. Biol. Chem. 279:16017-16025(2004).
RN [21]
RP INTERACTION WITH LSB5.
RX PubMed=15651983; DOI=10.1042/bj20041729;
RA Costa R., Warren D.T., Ayscough K.R.;
RT "Lsb5p interacts with actin regulators Sla1p and Las17p, ubiquitin and
RT Arf3p to couple actin dynamics to membrane trafficking processes.";
RL Biochem. J. 387:649-658(2005).
RN [22]
RP INTERACTION WITH VPS1.
RX PubMed=15265985; DOI=10.1242/jcs.01239;
RA Yu X., Cai M.;
RT "The yeast dynamin-related GTPase Vps1p functions in the organization of
RT the actin cytoskeleton via interaction with Sla1p.";
RL J. Cell Sci. 117:3839-3853(2004).
RN [23]
RP FUNCTION.
RX PubMed=15525671; DOI=10.1091/mbc.e04-08-0734;
RA Rodal A.A., Kozubowski L., Goode B.L., Drubin D.G., Hartwig J.H.;
RT "Actin and septin ultrastructures at the budding yeast cell cortex.";
RL Mol. Biol. Cell 16:372-384(2005).
RN [24]
RP 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 [25]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17286805; DOI=10.1111/j.1600-0854.2007.00534.x;
RA Gardiner F.C., Costa R., Ayscough K.R.;
RT "Nucleocytoplasmic trafficking is required for functioning of the adaptor
RT protein Sla1p in endocytosis.";
RL Traffic 8:347-358(2007).
RN [26]
RP PHOSPHORYLATION BY ARK1.
RX PubMed=17978096; DOI=10.1091/mbc.e07-06-0530;
RA Jin M., Cai M.;
RT "A novel function of Arp2p in mediating Prk1p-specific regulation of actin
RT and endocytosis in yeast.";
RL Mol. Biol. Cell 19:297-307(2008).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799; THR-831; THR-858;
RP THR-887; THR-904; THR-984 AND SER-996, AND IDENTIFICATION BY MASS
RP 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447; SER-449; SER-454;
RP THR-887; THR-904; THR-984; THR-993; SER-996 AND THR-1075, 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).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [30]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-471 AND LYS-548, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [31]
RP STRUCTURE BY NMR OF 495-560, AND DOMAIN.
RX PubMed=17363896; DOI=10.1038/sj.emboj.7601646;
RA Mahadev R.K., Di Pietro S.M., Olson J.M., Piao H.L., Payne G.S.,
RA Overduin M.;
RT "Structure of Sla1p homology domain 1 and interaction with the NPFxD
RT endocytic internalization motif.";
RL EMBO J. 26:1963-1971(2007).
RN [32]
RP STRUCTURE BY NMR OF 350-420, AND DOMAIN.
RX PubMed=17765920; DOI=10.1016/j.jmb.2007.07.074;
RA He Y., Hicke L., Radhakrishnan I.;
RT "Structural basis for ubiquitin recognition by SH3 domains.";
RL J. Mol. Biol. 373:190-196(2007).
CC -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC required for the internalization of endosomes during actin-coupled
CC endocytosis. The complex links the site of endocytosis to the cell
CC membrane-associated actin cytoskeleton. Mediates uptake of external
CC molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC role in the proper organization of the cell membrane-associated actin
CC cytoskeleton and promotes its destabilization.
CC {ECO:0000269|PubMed:10198057, ECO:0000269|PubMed:10594004,
CC ECO:0000269|PubMed:11940605, ECO:0000269|PubMed:11950888,
CC ECO:0000269|PubMed:12237851, ECO:0000269|PubMed:12388763,
CC ECO:0000269|PubMed:12734398, ECO:0000269|PubMed:12814545,
CC ECO:0000269|PubMed:14761940, ECO:0000269|PubMed:15525671,
CC ECO:0000269|PubMed:17286805, ECO:0000269|PubMed:8335689,
CC ECO:0000269|PubMed:8756649, ECO:0000269|PubMed:9008707,
CC ECO:0000269|PubMed:9128251}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC Interacts with ABP1, KRE6, LAS17, LSB5, RSP5, RVS167, VPS1 and YSC84.
CC {ECO:0000269|PubMed:10594004, ECO:0000269|PubMed:11739778,
CC ECO:0000269|PubMed:11950888, ECO:0000269|PubMed:12237851,
CC ECO:0000269|PubMed:12388763, ECO:0000269|PubMed:12734398,
CC ECO:0000269|PubMed:14761940, ECO:0000269|PubMed:15265985,
CC ECO:0000269|PubMed:15651983, ECO:0000269|PubMed:9024694}.
CC -!- INTERACTION:
CC P32790; P15891: ABP1; NbExp=4; IntAct=EBI-17313, EBI-2036;
CC P32790; P40563: AIM21; NbExp=4; IntAct=EBI-17313, EBI-25376;
CC P32790; P53933: APP1; NbExp=4; IntAct=EBI-17313, EBI-28798;
CC P32790; Q06604: BSP1; NbExp=5; IntAct=EBI-17313, EBI-37047;
CC P32790; P22137: CHC1; NbExp=4; IntAct=EBI-17313, EBI-4766;
CC P32790; P32525: ECM25; NbExp=4; IntAct=EBI-17313, EBI-26215;
CC P32790; P39013: END3; NbExp=4; IntAct=EBI-17313, EBI-6460;
CC P32790; P13134: KEX2; NbExp=16; IntAct=EBI-17313, EBI-9658;
CC P32790; Q12446: LAS17; NbExp=7; IntAct=EBI-17313, EBI-10022;
CC P32790; P43603: LSB3; NbExp=7; IntAct=EBI-17313, EBI-22980;
CC P32790; P25369: LSB5; NbExp=5; IntAct=EBI-17313, EBI-10218;
CC P32790; P54199: MPS1; NbExp=2; IntAct=EBI-17313, EBI-11224;
CC P32790; P32521: PAN1; NbExp=5; IntAct=EBI-17313, EBI-12875;
CC P32790; P25368: RRP7; NbExp=3; IntAct=EBI-17313, EBI-16019;
CC P32790; P32790: SLA1; NbExp=10; IntAct=EBI-17313, EBI-17313;
CC P32790; Q02794: STD1; NbExp=3; IntAct=EBI-17313, EBI-18344;
CC P32790; P32793: YSC84; NbExp=7; IntAct=EBI-17313, EBI-24460;
CC P32790; P54786: ZDS2; NbExp=3; IntAct=EBI-17313, EBI-29637;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side. Endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton, actin patch.
CC Note=Cytoplasmic and cortical actin patches. Is associated with
CC cortical actin patches in its dephosphorylated form and dissociates
CC upon phosphorylation by PRK1.
CC -!- PTM: Phosphorylated by PRK1. {ECO:0000269|PubMed:11739778,
CC ECO:0000269|PubMed:17978096}.
CC -!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SLA1 family. {ECO:0000305}.
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DR EMBL; Z22810; CAA80463.1; -; Genomic_DNA.
DR EMBL; Z35768; CAA84826.1; -; Genomic_DNA.
DR EMBL; S47695; AAB23985.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07113.1; -; Genomic_DNA.
DR PIR; S25327; S25327.
DR RefSeq; NP_009546.1; NM_001178247.1.
DR PDB; 1SSH; X-ray; 1.40 A; B=191-202.
DR PDB; 1Z9Z; X-ray; 1.95 A; A/B=357-413.
DR PDB; 2HBP; NMR; -; A=495-560.
DR PDB; 2JT4; NMR; -; A=350-420.
DR PDB; 2V1Q; X-ray; 1.20 A; A/B=357-413.
DR PDB; 3IDW; X-ray; 1.85 A; A=653-724.
DR PDBsum; 1SSH; -.
DR PDBsum; 1Z9Z; -.
DR PDBsum; 2HBP; -.
DR PDBsum; 2JT4; -.
DR PDBsum; 2V1Q; -.
DR PDBsum; 3IDW; -.
DR AlphaFoldDB; P32790; -.
DR SMR; P32790; -.
DR BioGRID; 32692; 720.
DR ComplexPortal; CPX-1344; SLAC complex.
DR ComplexPortal; CPX-426; PAN1 actin cytoskeleton-regulatory complex.
DR DIP; DIP-695N; -.
DR IntAct; P32790; 156.
DR MINT; P32790; -.
DR STRING; 4932.YBL007C; -.
DR MoonDB; P32790; Predicted.
DR GlyGen; P32790; 12 sites, 1 O-linked glycan (12 sites).
DR iPTMnet; P32790; -.
DR MaxQB; P32790; -.
DR PaxDb; 4932-YBL007C; -.
DR PeptideAtlas; P32790; -.
DR EnsemblFungi; YBL007C_mRNA; YBL007C; YBL007C.
DR GeneID; 852276; -.
DR KEGG; sce:YBL007C; -.
DR AGR; SGD:S000000103; -.
DR SGD; S000000103; SLA1.
DR VEuPathDB; FungiDB:YBL007C; -.
DR eggNOG; ENOG502QQC3; Eukaryota.
DR HOGENOM; CLU_003674_0_0_1; -.
DR InParanoid; P32790; -.
DR OMA; FMAQGED; -.
DR OrthoDB; 2906837at2759; -.
DR BioCyc; YEAST:G3O-28913-MONOMER; -.
DR BioGRID-ORCS; 852276; 2 hits in 10 CRISPR screens.
DR EvolutionaryTrace; P32790; -.
DR PRO; PR:P32790; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32790; Protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:1990964; C:actin cytoskeleton-regulatory complex; IDA:SGD.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140224; C:SLAC complex; IDA:SGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0140312; F:cargo adaptor activity; IMP:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0000147; P:actin cortical patch assembly; IMP:SGD.
DR GO; GO:0071555; P:cell wall organization; IMP:ComplexPortal.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IDA:ComplexPortal.
DR CDD; cd09532; SAM_SLA1_fungal; 1.
DR CDD; cd11773; SH3_Sla1p_1; 1.
DR CDD; cd11775; SH3_Sla1p_3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR Gene3D; 2.30.30.700; SLA1 homology domain 1; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR IDEAL; IID50273; -.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR007131; SHD1.
DR InterPro; IPR035800; Sla1_SH3_1.
DR InterPro; IPR035821; Sla1_SH3_3.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF03983; SHD1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50002; SH3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell membrane; Cytoplasm; Cytoskeleton;
KW Endocytosis; Endosome; Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Ubl conjugation.
FT CHAIN 1..1244
FT /note="Actin cytoskeleton-regulatory complex protein SLA1"
FT /id="PRO_0000071943"
FT DOMAIN 3..68
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 69..132
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 353..415
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 868..874
FT /note="1"
FT REPEAT 877..883
FT /note="2"
FT REPEAT 887..893
FT /note="3"
FT REPEAT 923..929
FT /note="4"
FT REPEAT 945..951
FT /note="5"
FT REPEAT 1003..1009
FT /note="6"
FT REPEAT 1020..1026
FT /note="7"
FT REPEAT 1031..1037
FT /note="8"
FT REPEAT 1048..1054
FT /note="9"
FT REPEAT 1065..1071
FT /note="10"
FT REPEAT 1084..1090
FT /note="11"
FT REPEAT 1129..1135
FT /note="12"
FT REPEAT 1155..1161
FT /note="13"
FT REPEAT 1170..1176
FT /note="14"
FT REPEAT 1185..1191
FT /note="15"
FT REPEAT 1200..1206
FT /note="16"
FT REGION 128..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..1205
FT /note="16 X 7 AA approximate repeats of T-G-G-A-M-M-P"
FT COMPBIAS 201..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 831
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 858
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 904
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 984
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 993
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 996
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1075
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 471
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:2V1Q"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:2V1Q"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:2V1Q"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:2V1Q"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:2V1Q"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:2V1Q"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:2V1Q"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:2JT4"
FT STRAND 497..505
FT /evidence="ECO:0007829|PDB:2HBP"
FT STRAND 508..517
FT /evidence="ECO:0007829|PDB:2HBP"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:2HBP"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:2HBP"
FT HELIX 540..550
FT /evidence="ECO:0007829|PDB:2HBP"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:2HBP"
FT HELIX 657..663
FT /evidence="ECO:0007829|PDB:3IDW"
FT HELIX 668..680
FT /evidence="ECO:0007829|PDB:3IDW"
FT HELIX 685..690
FT /evidence="ECO:0007829|PDB:3IDW"
FT HELIX 693..698
FT /evidence="ECO:0007829|PDB:3IDW"
FT HELIX 703..716
FT /evidence="ECO:0007829|PDB:3IDW"
SQ SEQUENCE 1244 AA; 135848 MW; 7FD85AA776407624 CRC64;
MTVFLGIYRA VYAYEPQTPE ELAIQEDDLL YLLQKSDIDD WWTVKKRVIG SDSEEPVGLV
PSTYIEEAPV LKKVRAIYDY EQVQNADEEL TFHENDVFDV FDDKDADWLL VKSTVSNEFG
FIPGNYVEPE NGSTSKQEQA PAAAEAPAAT PAAAPASAAV LPTNFLPPPQ HNDRARMMQS
KEDQAPDEDE EGPPPAMPAR PTATTETTDA TAAAVRSRTR LSYSDNDNDD EEDDYYYNSN
SNNVGNHEYN TEYHSWNVTE IEGRKKKKAK LSIGNNKINF IPQKGTPHEW SIDKLVSYDN
EKKHMFLEFV DPYRSLELHT GNTTTCEEIM NIIGEYKGAS RDPGLREVEM ASKSKKRGIV
QYDFMAESQD ELTIKSGDKV YILDDKKSKD WWMCQLVDSG KSGLVPAQFI EPVRDKKHTE
STASGIIKSI KKNFTKSPSR SRSRSRSKSN ANASWKDDEL QNDVVGSAAG KRSRKSSLSS
HKKNSSATKD FPNPKKSRLW VDRSGTFKVD AEFIGCAKGK IHLHKANGVK IAVAADKLSN
EDLAYVEKIT GFSLEKFKAN DGSSSRGTDS RDSERERRRR LKEQEEKERD RRLKERELYE
LKKARELLDE ERSRLQEKEL PPIKPPRPTS TTSVPNTTSV PPAESSNNNN SSNKYDWFEF
FLNCGVDVSN CQRYTINFDR EQLTEDMMPD INNSMLRTLG LREGDIVRVM KHLDKKFGRE
NIASIPTNAT GNMFSQPDGS LNVATSPETS LPQQLLPQTT SPAQTAPSTS AETDDAWTVK
PASKSESNLL SKKSEFTGSM QDLLDLQPLE PKKAAASTPE PNLKDLEPVK TGGTTVPAAP
VSSAPVSSAP APLDPFKTGG NNILPLSTGF VMMPMITGGD MLPMQRTGGF VVPQTTFGMQ
SQVTGGILPV QKTGNGLIPI SNTGGAMMPQ TTFGAAATVL PLQKTGGGLI PIATTGGAQF
PQTSFNVQGQ QQLPTGSILP VQKTANGLIS ANTGVSMPTV QRTGGTMIPQ TSFGVSQQLT
GGAMMTQPQN TGSAMMPQTS FNAVPQITGG AMMPQTSFNA LPQVTGGAMM PLQRTGGALN
TFNTGGAMIP QTSFSSQAQN TGGFRPQSQF GLTLQKTGGI APLNQNQFTG GAMNTLSTGG
VLQQQQPQTM NTFNTGGVMQ ELQMMTTFNT GGAMQQPQMM NTFNTDGIMQ QPQMMNTFNT
GGAMQQPQQQ ALQNQPTGFG FGNGPQQSRQ ANIFNATASN PFGF
//
