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
//