ID MYO3_YEAST Reviewed; 1272 AA. AC P36006; D6VX66; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 21-SEP-2011, sequence version 4. DT 02-SEP-2026, entry version 215. DE RecName: Full=Myosin-3; DE AltName: Full=Actin-dependent myosin-I MYO3; DE AltName: Full=Class I unconventional myosin MYO3; DE AltName: Full=Type I myosin MYO3; GN Name=MYO3; OrderedLocusNames=YKL129C; 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]. RC STRAIN=CRY3; RX PubMed=7728870; DOI=10.1002/cm.970300109; RA Goodson H.V., Spudich J.A.; RT "Identification and molecular characterization of a yeast myosin I."; RL Cell Motil. Cytoskeleton 30:73-84(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8196765; DOI=10.1038/369371a0; RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., RA Becker I., Mewes H.-W.; RT "Complete DNA sequence of yeast chromosome XI."; RL Nature 369:371-378(1994). RN [3] RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 263-270 AND 1021. 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 FUNCTION IN ACTIN CYTOSKELETON ORGANIZATION. RX PubMed=8682864; DOI=10.1083/jcb.133.6.1277; RA Goodson H.V., Anderson B.L., Warrick H.M., Pon L.A., Spudich J.A.; RT "Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): RT myosin I proteins are required for polarization of the actin RT cytoskeleton."; RL J. Cell Biol. 133:1277-1291(1996). RN [5] RP FUNCTION IN RECEPTOR ENDOCYTOSIS. RX PubMed=8614799; DOI=10.1126/science.272.5261.533; RA Geli M.I., Riezman H.; RT "Role of type I myosins in receptor-mediated endocytosis in yeast."; RL Science 272:533-535(1996). RN [6] RP FUNCTION, PHOSPHORYLATION AT SER-357 BY CLA4 AND STE20, AND MUTAGENESIS OF RP SER-357. RX PubMed=9388196; DOI=10.1074/jbc.272.49.30623; RA Wu C., Lytvyn V., Thomas D.Y., Leberer E.; RT "The phosphorylation site for Ste20p-like protein kinases is essential for RT the function of myosin-I in yeast."; RL J. Biol. Chem. 272:30623-30626(1997). RN [7] RP FUNCTION, INTERACTION WITH ARC19; ARC40; LAS17 AND VRP1, AND MUTAGENESIS OF RP TRP-1158 AND TRP-1272. RX PubMed=10648568; DOI=10.1083/jcb.148.2.353; RA Evangelista M., Klebl B.M., Tong A.H.Y., Webb B.A., Leeuw T., Leberer E., RA Whiteway M., Thomas D.Y., Boone C.; RT "A role for myosin-I in actin assembly through interactions with Vrp1p, RT Bee1p, and the Arp2/3 complex."; RL J. Cell Biol. 148:353-362(2000). RN [8] RP FUNCTION, INTERACTION WITH ARP2 AND LAS17, AND MUTAGENESIS OF GLY-132 AND RP SER-357. RX PubMed=10648569; DOI=10.1083/jcb.148.2.363; RA Lechler T., Shevchenko A., Li R.; RT "Direct involvement of yeast type I myosins in Cdc42-dependent actin RT polymerization."; RL J. Cell Biol. 148:363-373(2000). RN [9] RP INTERACTION WITH BBC1. RX PubMed=11901111; DOI=10.1093/genetics/160.3.923; RA Mochida J., Yamamoto T., Fujimura-Kamada K., Tanaka K.; RT "The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich RT syndrome protein-interacting protein (WIP), may antagonistically regulate RT type I myosins in Saccharomyces cerevisiae."; RL Genetics 160:923-934(2002). RN [10] RP FUNCTION, AND INTERACTION WITH SHE4. RX PubMed=12725728; DOI=10.1016/s0960-9822(03)00264-1; RA Wesche S., Arnold M., Jansen R.-P.; RT "The UCS domain protein She4p binds to myosin motor domains and is RT essential for class I and class V myosin function."; RL Curr. Biol. 13:715-724(2003). RN [11] RP FUNCTION, AND INTERACTION WITH SHE4. RX PubMed=12808026; DOI=10.1091/mbc.e02-09-0616; RA Toi H., Fujimura-Kamada K., Irie K., Takai Y., Todo S., Tanaka K.; RT "She4p/Dim1p interacts with the motor domain of unconventional myosins in RT the budding yeast, Saccharomyces cerevisiae."; RL Mol. Biol. Cell 14:2237-2249(2003). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, 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 [14] RP INTERACTION WITH PAN1, AND SUBCELLULAR LOCATION. RX PubMed=17522383; DOI=10.1091/mbc.e07-05-0436; RA Barker S.L., Lee L., Pierce B.D., Maldonado-Baez L., Drubin D.G., RA Wendland B.; RT "Interaction of the endocytic scaffold protein Pan1 with the type I myosins RT contributes to the late stages of endocytosis."; RL Mol. Biol. Cell 18:2893-2903(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION BY RP 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION BY RP 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 [17] RP STRUCTURE BY NMR OF 1123-1191. RX PubMed=16600966; DOI=10.1110/ps.051785506; RA Musi V., Birdsall B., Fernandez-Ballester G., Guerrini R., Salvatori S., RA Serrano L., Pastore A.; RT "New approaches to high-throughput structure characterization of SH3 RT complexes: the example of Myosin-3 and Myosin-5 SH3 domains from RT S.cerevisiae."; RL Protein Sci. 15:795-807(2006). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1123-1191. RA Kursula P., Kursula I., Lehmann F., Song Y.H., Wilmanns M.; RT "Crystal structure of the SH3 domain from S.cerevisiae Myo3."; RL Submitted (MAR-2005) to the PDB data bank. RN [19] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1123-1191. RA Kursula P., Lehmann F., Song Y.H., Wilmanns M.; RT "High-throughput structural genomics of yeast SH3 domains."; RL Submitted (JUN-2005) to the PDB data bank. CC -!- FUNCTION: One of two redundant type-I myosins implicated in the CC organization of the actin cytoskeleton. Required for proper actin CC cytoskeleton polarization and for the internalization step in CC endocytosis. At the cell cortex, assembles in patch-like structures CC together with proteins from the actin-polymerizing machinery and CC promotes actin assembly. Functions redundantly with LAS17 as actin CC nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain CC phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated CC actin assembly. Functions together with the NPF PAN1 in late stages of CC endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and CC PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but CC not constitutive endocytosis of the G protein-coupled receptor STE2. CC {ECO:0000269|PubMed:10648568, ECO:0000269|PubMed:10648569, CC ECO:0000269|PubMed:12725728, ECO:0000269|PubMed:12808026, CC ECO:0000269|PubMed:8614799, ECO:0000269|PubMed:8682864, CC ECO:0000269|PubMed:9388196}. CC -!- SUBUNIT: Interacts (via myosin motor domain) with SHE4; this CC interaction is important for proper localization and may regulate the CC interaction of the motor domain with actin. Interacts (via SH3 domain) CC with VRP1; this interaction is required for localization to sites of CC polarized growth and may regulate the interaction of the tail domain CC with actin. Interacts (via SH3 domain) with PAN1; this interaction is CC important for late stages of endocytopsis. Interacts (via SH3 domain) CC with BBC1 and LAS17. Interacts (via C-terminal acidic tail) with ARC19 CC and ARC40; ARC19 and ARC40 are Arp2/3 complex subunits. CC {ECO:0000269|PubMed:10648568, ECO:0000269|PubMed:10648569, CC ECO:0000269|PubMed:11901111, ECO:0000269|PubMed:12725728, CC ECO:0000269|PubMed:12808026, ECO:0000269|PubMed:17522383}. CC -!- INTERACTION: CC P36006; P40563: AIM21; NbExp=3; IntAct=EBI-11670, EBI-25376; CC P36006; P38328: ARC40; NbExp=3; IntAct=EBI-11670, EBI-2777; CC P36006; P47068: BBC1; NbExp=5; IntAct=EBI-11670, EBI-3437; CC P36006; Q01389: BCK1; NbExp=6; IntAct=EBI-11670, EBI-3470; CC P36006; P41832: BNI1; NbExp=3; IntAct=EBI-11670, EBI-3692; CC P36006; P40450: BNR1; NbExp=6; IntAct=EBI-11670, EBI-3711; CC P36006; Q12446: LAS17; NbExp=3; IntAct=EBI-11670, EBI-10022; CC P36006; Q12451: OSH2; NbExp=3; IntAct=EBI-11670, EBI-12621; CC P36006; P33334: PRP8; NbExp=4; IntAct=EBI-11670, EBI-465; CC P36006; P39955: SAP1; NbExp=3; IntAct=EBI-11670, EBI-16463; CC P36006; Q03497: STE20; NbExp=3; IntAct=EBI-11670, EBI-18285; CC P36006; P40453: UBP7; NbExp=3; IntAct=EBI-11670, EBI-19857; CC P36006; P37370: VRP1; NbExp=12; IntAct=EBI-11670, EBI-20502; CC P36006; Q08912: YOR389W; NbExp=2; IntAct=EBI-11670, EBI-38289; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch CC {ECO:0000269|PubMed:17522383}. Note=Localizes to cortical patch-like CC protein structures that assemble actin patches. Enriched at sites of CC polarized growth. CC -!- DOMAIN: The myosin motor domain displays actin-stimulated ATPase CC activity and generates a mechanochemical force. CC -!- DOMAIN: The tail domain participates in molecular interactions that CC specify the role of the motor domain. It is composed of several tail CC homology (TH) domains, namely a putative phospholipid-binding myosin CC tail domain (also named TH1), an Ala- and Pro-rich domain (TH2), CC followed by an SH3 domain and a C-terminal acidic domain (TH3). CC -!- PTM: Phosphorylation of the TEDS site (Ser-357) is required for the CC polarization of the actin cytoskeleton and for ligand-induced, but not CC for constitutive internalization of STE2. Phosphorylation probably CC activates the myosin-I ATPase (By similarity). Ser-357 is CC phosphorylated by CLA4 and STE20 in vitro. {ECO:0000250, CC ECO:0000269|PubMed:9388196}. CC -!- MISCELLANEOUS: Present with 155 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {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; S76960; AAB34124.1; -; Genomic_DNA. DR EMBL; Z28129; CAA81970.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09032.2; -; Genomic_DNA. DR PIR; S37958; S37958. DR RefSeq; NP_012793.2; NM_001179695.2. DR PDB; 1RUW; X-ray; 1.80 A; A=1121-1189. DR PDB; 1VA7; X-ray; 2.90 A; A/B/C/D=1121-1189. DR PDB; 2BTT; NMR; -; A=1121-1189. DR AlphaFoldDB; P36006; -. DR BMRB; P36006; -. DR MDposit; P36006; -. DR SMR; P36006; -. DR BioGRID; 34006; 146. DR ComplexPortal; CPX-1500; Myosin class I complex, MYO3 variant. DR DIP; DIP-2221N; -. DR FunCoup; P36006; 298. DR IntAct; P36006; 66. DR MINT; P36006; -. DR STRING; 4932.YKL129C; -. DR MoonDB; P36006; Predicted. DR GlyGen; P36006; 2 sites. DR iPTMnet; P36006; -. DR PaxDb; 4932-YKL129C; -. DR PeptideAtlas; P36006; -. DR EnsemblFungi; YKL129C_mRNA; YKL129C; YKL129C. DR GeneID; 853729; -. DR KEGG; sce:YKL129C; -. DR AGR; SGD:S000001612; -. DR SGD; S000001612; MYO3. DR VEuPathDB; FungiDB:YKL129C; -. DR eggNOG; KOG0162; Eukaryota. DR HOGENOM; CLU_000192_7_6_1; -. DR InParanoid; P36006; -. DR OrthoDB; 6108017at2759; -. DR BioCyc; YEAST:G3O-31910-MONOMER; -. DR BioGRID-ORCS; 853729; 2 hits in 10 CRISPR screens. DR EvolutionaryTrace; P36006; -. DR PRO; PR:P36006; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P36006; protein. DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0071944; C:cell periphery; HDA:SGD. DR GO; GO:0051286; C:cell tip; IBA:GO_Central. DR GO; GO:0005902; C:microvillus; IBA:GO_Central. DR GO; GO:0016459; C:myosin complex; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0000146; F:microfilament motor activity; TAS:SGD. DR GO; GO:0017022; F:myosin binding; IPI:UniProtKB. DR GO; GO:0051666; P:actin cortical patch localization; IGI:SGD. DR GO; GO:0007121; P:bipolar cellular bud site selection; TAS:SGD. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR GO; GO:0006887; P:exocytosis; TAS:SGD. DR GO; GO:0031505; P:fungal-type cell wall organization; TAS:SGD. DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD. DR GO; GO:0006970; P:response to osmotic stress; TAS:SGD. DR GO; GO:0061709; P:reticulophagy; IGI:SGD. DR CDD; cd01378; MYSc_Myo1; 1. DR CDD; cd11858; SH3_Myosin-I_fungi; 1. DR FunFam; 1.10.10.820:FF:000001; Myosin heavy chain; 1. DR FunFam; 1.20.120.720:FF:000015; Myosin I; 1. DR FunFam; 2.30.30.40:FF:000254; Myosin I MyoA/Myo5; 1. DR FunFam; 1.20.5.4820:FF:000004; Myosin IE; 1. DR FunFam; 1.20.58.530:FF:000007; Myosin IE; 1. DR Gene3D; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.4820; -; 1. DR Gene3D; 1.20.58.530; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR035535; Fungal_myosin-I_SH3. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR001609; Myosin_head_motor_dom-like. DR InterPro; IPR010926; Myosin_TH1. DR InterPro; IPR036072; MYSc_Myo1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR13140; MYOSIN; 1. DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1. DR Pfam; PF00063; Myosin_head; 1. DR Pfam; PF06017; Myosin_TH1; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR SMART; SM00242; MYSc; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS51757; TH1; 1. DR PDBsum; 1RUW; -. DR PDBsum; 1VA7; -. DR PDBsum; 2BTT; -. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; KW Hydrolase; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; SH3 domain. FT CHAIN 1..1272 FT /note="Myosin-3" FT /id="PRO_0000123490" FT DOMAIN 36..715 FT /note="Myosin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT DOMAIN 719..739 FT /note="IQ 1" FT DOMAIN 740..765 FT /note="IQ 2" FT DOMAIN 771..961 FT /note="TH1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093" FT DOMAIN 1120..1182 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 588..610 FT /note="Actin-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT REGION 951..1015 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1029..1141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1217..1272 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 980..1000 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1066..1078 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1089..1098 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1109..1118 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1217..1236 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1258..1272 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 129..136 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT MOD_RES 357 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:9388196, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MUTAGEN 132 FT /note="G->R: Loss of function." FT /evidence="ECO:0000269|PubMed:10648569" FT MUTAGEN 357 FT /note="S->A: Loss of function." FT /evidence="ECO:0000269|PubMed:10648569, FT ECO:0000269|PubMed:9388196" FT MUTAGEN 357 FT /note="S->D: Has a constitutive higher activity in actin FT assembly." FT /evidence="ECO:0000269|PubMed:10648569, FT ECO:0000269|PubMed:9388196" FT MUTAGEN 1158 FT /note="W->S: Abolishes interaction with LAS17 and causes FT severe mislocalization of the protein." FT /evidence="ECO:0000269|PubMed:10648568" FT MUTAGEN 1272 FT /note="Missing: Abolishes interaction with ARC40." FT /evidence="ECO:0000269|PubMed:10648568" FT CONFLICT 95 FT /note="G -> RK (in Ref. 1; AAB34124)" FT /evidence="ECO:0000305" FT CONFLICT 168..169 FT /note="NP -> T (in Ref. 1; AAB34124)" FT /evidence="ECO:0000305" FT CONFLICT 263..270 FT /note="TADTIDDV -> SADQLMR (in Ref. 2; CAA81970)" FT /evidence="ECO:0000305" FT CONFLICT 917..918 FT /note="VG -> RLV (in Ref. 1; AAB34124)" FT /evidence="ECO:0000305" FT CONFLICT 1021 FT /note="A -> R (in Ref. 2; CAA81970)" FT /evidence="ECO:0000305" FT STRAND 1123..1129 FT /evidence="ECO:0007829|PDB:1RUW" FT STRAND 1137..1139 FT /evidence="ECO:0007829|PDB:2BTT" FT STRAND 1147..1153 FT /evidence="ECO:0007829|PDB:1RUW" FT STRAND 1157..1163 FT /evidence="ECO:0007829|PDB:1RUW" FT STRAND 1169..1173 FT /evidence="ECO:0007829|PDB:1RUW" FT HELIX 1174..1176 FT /evidence="ECO:0007829|PDB:1RUW" FT STRAND 1177..1179 FT /evidence="ECO:0007829|PDB:1RUW" SQ SEQUENCE 1272 AA; 142451 MW; 6CB13AD3CD669600 CRC64; MAVIKKGARR KDVKEPKKRS AKIKKATFDA NKKKEVGISD LTLLSKISDE SINENLKKRF KNGIIYTYIG HVLISVNPFR DLGIYTNAVL ESYKGKNRLE VPPHVFAIAE SMYYNLKSYN ENQCVIISGE SGAGKTEAAK RIMQYIAAAS NSHSESIGKI KDMVLATNPL LESFGCAKTL RNNNSSRHGK YLEIKFNSQF EPCAGNITNY LLEKQRVVGQ IKNERNFHIF YQFTKGASDT YKQMFGVQMP EQYIYTAAAG CTTADTIDDV KDYEGTLEAM RTIGLVQEEQ DQIFRMLAAI LWIGNISFIE NEEGNAQVGD TSVTDFVAYL LQVDASLLVK CLVERIMQTS HGMKRGSVYH VPLNPVQATA VRDALAKAIY NNLFDWIVDR VNVSLQAFPG ADKSIGILDI YGFEIFEHNS FEQICINYVN EKLQQIFIQL TLKAEQETYE REKIKWTPIK YFDNKVVCDL IEAKNPPGIL AAMNDSIATA HADSNAADQA FAQRLNLFNS NPYFELRANK FVIKHYAGDV TYDINGITDK NKDQLQKDLI ELIGTTTNTF LSTIFPDDVD KDSKRRPPTA GDKIIKSANE LVETLSKAEP SYIRTIKPNQ TKSPNDYDDH QVLHQVKYLG LQENVRIRRA GFAYRQTFEK FVERFYLLSP DCSYAGDYTW DGDTLEAVKL ILRDAMIPEK EFQLGVTSVF IKTPESLFAL EDMRDKYWYN MAARIQRAWR RFLQRRIDAA IKIQRTIREK KGGNKYVKLR DYGTKLLAGK KERRSMSLLG YRAFMGDYLS CNESKTKGSY IRRQVGIKDK VVFSIKGECL HSKFGRSAQR LKKVFILTKK TFYIIGQTRE QNAMKYTQDY KIDVGKIKQV SLTNLQDDWM GVILVNSTQS DPLINTPFKT ELMTRLKKLN EKIMIKVGPT IEYHKQPNKL HTVRSKISDS APKYGDIYKS STIYVRRGHP ANSKSNKKPK NPGGLSGKPI KSKKSKHKST HKHTHSHRSH RDAAKKQPLP SQKPVNPLSL AATAAQAAYN PKPDKTVPIK SSAIPAAKVS SKHSSKPSSK EKVAVKKASS SHKSSSAKQN QVSMPPSKGV EKNKEPLKET TATATANIPI PPPPPPMGQP KDPKFEAAYD FPGSGSSSEL PLKKGDIVFI SRDEPSGWSL AKLLDGSKEG WVPTAYMTPY KDTRNTVPVA ATGAVNDVTN QKSSQIDNTI SSAQEGVQFG SATVGPTSDN QSNPVGTFSD GLASALAARA NKMRAESADD DDNDDGDDDD DW //