ID MYO5_YEAST Reviewed; 1219 AA. AC Q04439; D6VZT2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 210. DE RecName: Full=Myosin-5; DE AltName: Full=Actin-dependent myosin-I MYO5; DE AltName: Full=Class I unconventional myosin MYO5; DE AltName: Full=Type I myosin MYO5; GN Name=MYO5; OrderedLocusNames=YMR109W; ORFNames=YM9718.08; 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], FUNCTION, AND SUBCELLULAR LOCATION. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). 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 FUNCTION IN RECEPTOR ENDOCYTOSIS, AND MUTAGENESIS OF GLU-472. 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 [5] RP FUNCTION, INTERACTION WITH VRP1, AND SUBCELLULAR LOCATION. RX PubMed=9628892; DOI=10.1083/jcb.141.6.1357; RA Anderson B.L., Boldogh I., Evangelista M., Boone C., Greene L.A., Pon L.A.; RT "The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to RT verprolin and is required for targeting to sites of actin polarization."; RL J. Cell Biol. 141:1357-1370(1998). RN [6] RP FUNCTION, INTERACTION WITH VRP1, AND MUTAGENESIS OF TRP-1123. RX PubMed=10944111; DOI=10.1093/emboj/19.16.4281; RA Geli M.I., Lombardi R., Schmelzl B., Riezman H.; RT "An intact SH3 domain is required for myosin I-induced actin RT polymerization."; RL EMBO J. 19:4281-4291(2000). RN [7] RP FUNCTION, AND INTERACTION WITH ARC19 AND ARC40. 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, AND INTERACTION WITH LAS17. 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, AND MUTAGENESIS OF TRP-1123. 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 INTERACTION WITH BZZ1. RX PubMed=12391157; DOI=10.1128/mcb.22.22.7889-7906.2002; RA Soulard A., Lechler T., Spiridonov V., Shevchenko A., Shevchenko A., Li R., RA Winsor B.; RT "Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin RT patch polarization and is able to recruit actin-polymerizing machinery in RT vitro."; RL Mol. Cell. Biol. 22:7889-7906(2002). RN [11] 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 [12] RP FUNCTION, INTERACTION WITH SHE4, AND MUTAGENESIS OF VAL-164; ASN-168; RP ASN-209 AND LYS-377. 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 [13] 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 [14] RP FUNCTION, PHOSPHORYLATION AT SER-357 AND SER-777, IDENTIFICATION BY MASS RP SPECTROMETRY, MUTAGENESIS OF SER-357, SUBCELLULAR LOCATION, AND INTERACTION RP WITH PKH1; PKH2; YPK1 AND YPK2. RX PubMed=16478726; DOI=10.1074/jbc.m508933200; RA Grosshans B.L., Groetsch H., Mukhopadhyay D., Fernandez I.M., RA Pfannstiel J., Idrissi F.-Z., Lechner J., Riezman H., Geli M.I.; RT "TEDS site phosphorylation of the yeast myosins I is required for ligand- RT induced but not for constitutive endocytosis of the G protein-coupled RT receptor Ste2p."; RL J. Biol. Chem. 281:11104-11114(2006). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; TYR-359; SER-992 AND RP SER-1205, 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 [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [18] 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1205, 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 [20] RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1088-1145. RA Gonfloni S., Kursula P., Sacco R., Cesareni G., Wilmanns M.; RT "Yeast Myo5 SH3 domain, tetragonal crystal form."; RL Submitted (JAN-2006) to the PDB data bank. RN [21] RP X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 1088-1145. RA Wilmanns M., Kursula P., Gonfloni S., Ferracuti S., Cesareni G.; RT "High-resolution structure of yeast Myo5 SH3 domain."; RL Submitted (OCT-2006) 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:10944111, ECO:0000269|PubMed:12725728, CC ECO:0000269|PubMed:12808026, ECO:0000269|PubMed:16478726, CC ECO:0000269|PubMed:8614799, ECO:0000269|PubMed:8682864, CC ECO:0000269|PubMed:9628892}. 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. Interacts with CC BZZ1, PKH1, PKH2, YPK1 and YPK2. {ECO:0000269|PubMed:10648568, CC ECO:0000269|PubMed:10648569, ECO:0000269|PubMed:10944111, CC ECO:0000269|PubMed:11901111, ECO:0000269|PubMed:12391157, CC ECO:0000269|PubMed:12725728, ECO:0000269|PubMed:12808026, CC ECO:0000269|PubMed:16478726, ECO:0000269|PubMed:17522383, CC ECO:0000269|PubMed:9628892}. CC -!- INTERACTION: CC Q04439; P40563: AIM21; NbExp=2; IntAct=EBI-11687, EBI-25376; CC Q04439; P53933: APP1; NbExp=2; IntAct=EBI-11687, EBI-28798; CC Q04439; P38328: ARC40; NbExp=3; IntAct=EBI-11687, EBI-2777; CC Q04439; P47068: BBC1; NbExp=6; IntAct=EBI-11687, EBI-3437; CC Q04439; Q01389: BCK1; NbExp=6; IntAct=EBI-11687, EBI-3470; CC Q04439; P40450: BNR1; NbExp=7; IntAct=EBI-11687, EBI-3711; CC Q04439; P38822: BZZ1; NbExp=5; IntAct=EBI-11687, EBI-3889; CC Q04439; Q00362: CDC55; NbExp=4; IntAct=EBI-11687, EBI-1942; CC Q04439; P48562: CLA4; NbExp=3; IntAct=EBI-11687, EBI-4750; CC Q04439; P06787: CMD1; NbExp=8; IntAct=EBI-11687, EBI-3976; CC Q04439; Q12446: LAS17; NbExp=7; IntAct=EBI-11687, EBI-10022; CC Q04439; Q04439: MYO5; NbExp=7; IntAct=EBI-11687, EBI-11687; CC Q04439; Q12451: OSH2; NbExp=6; IntAct=EBI-11687, EBI-12621; CC Q04439; P32521: PAN1; NbExp=2; IntAct=EBI-11687, EBI-12875; CC Q04439; Q03306: PKH3; NbExp=2; IntAct=EBI-11687, EBI-37683; CC Q04439; P33334: PRP8; NbExp=4; IntAct=EBI-11687, EBI-465; CC Q04439; P39743: RVS167; NbExp=3; IntAct=EBI-11687, EBI-14500; CC Q04439; P39955: SAP1; NbExp=4; IntAct=EBI-11687, EBI-16463; CC Q04439; Q03497: STE20; NbExp=4; IntAct=EBI-11687, EBI-18285; CC Q04439; P40453: UBP7; NbExp=4; IntAct=EBI-11687, EBI-19857; CC Q04439; P37370: VRP1; NbExp=19; IntAct=EBI-11687, EBI-20502; CC Q04439; Q08912: YOR389W; NbExp=2; IntAct=EBI-11687, EBI-38289; CC Q04439; P40021: ZRG8; NbExp=2; IntAct=EBI-11687, EBI-22484; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch CC {ECO:0000269|PubMed:16478726, ECO:0000269|PubMed:17522383, CC ECO:0000269|PubMed:8682864, ECO:0000269|PubMed:9628892}. Note=Localizes CC to cortical patch-like protein structures that assemble actin patches. CC Enriched at sites of 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 activity. Ser-357 is phosphorylated by CC YPK2 in vitro. {ECO:0000269|PubMed:16478726}. CC -!- MISCELLANEOUS: Present with 2280 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; Z49702; CAA89745.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10006.1; -; Genomic_DNA. DR PIR; S54570; S54570. DR RefSeq; NP_013827.1; NM_001182609.1. DR PDB; 1YP5; X-ray; 1.68 A; A=1088-1145. DR PDB; 1ZUY; X-ray; 1.39 A; A/B=1088-1145. DR PDBsum; 1YP5; -. DR PDBsum; 1ZUY; -. DR AlphaFoldDB; Q04439; -. DR SMR; Q04439; -. DR BioGRID; 35285; 252. DR ComplexPortal; CPX-1470; Myosin class I complex, MYO5 variant. DR DIP; DIP-2222N; -. DR IntAct; Q04439; 99. DR MINT; Q04439; -. DR STRING; 4932.YMR109W; -. DR MoonDB; Q04439; Predicted. DR CarbonylDB; Q04439; -. DR iPTMnet; Q04439; -. DR MaxQB; Q04439; -. DR PaxDb; 4932-YMR109W; -. DR PeptideAtlas; Q04439; -. DR EnsemblFungi; YMR109W_mRNA; YMR109W; YMR109W. DR GeneID; 855136; -. DR KEGG; sce:YMR109W; -. DR AGR; SGD:S000004715; -. DR SGD; S000004715; MYO5. DR VEuPathDB; FungiDB:YMR109W; -. DR eggNOG; KOG0162; Eukaryota. DR GeneTree; ENSGT00940000170976; -. DR HOGENOM; CLU_000192_7_6_1; -. DR InParanoid; Q04439; -. DR OMA; MAFHWQS; -. DR OrthoDB; 1094820at2759; -. DR BioCyc; YEAST:G3O-32805-MONOMER; -. DR BioGRID-ORCS; 855136; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; Q04439; -. DR PRO; PR:Q04439; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q04439; Protein. DR GO; GO:0030479; C:actin cortical patch; IDA:SGD. 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:0005933; C:cellular bud; HDA:SGD. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0043332; C:mating projection tip; HDA:SGD. DR GO; GO:0045160; C:myosin I complex; IPI:ComplexPortal. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0031982; C:vesicle; IBA:GO_Central. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000146; F:microfilament motor activity; IDA:SGD. DR GO; GO:0051666; P:actin cortical patch localization; IMP:SGD. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0007121; P:bipolar cellular bud site selection; TAS:SGD. DR GO; GO:0006897; P:endocytosis; IMP:SGD. 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:0006898; P:receptor-mediated endocytosis; IMP:SGD. DR GO; GO:0006970; P:response to osmotic stress; TAS:SGD. DR GO; GO:0009651; P:response to salt stress; IGI:SGD. DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central. DR CDD; cd01378; MYSc_Myo1; 1. DR CDD; cd11858; SH3_Myosin-I_fungi; 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. 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. 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..1219 FT /note="Myosin-5" FT /id="PRO_0000123492" 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 1085..1147 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..1106 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1139..1167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 975..991 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1023..1052 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1070..1086 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1143..1167 FT /note="Polar 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:16478726, FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956" FT MOD_RES 359 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17330950" FT MOD_RES 777 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16478726" FT MOD_RES 992 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950" FT MOD_RES 1205 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MUTAGEN 164 FT /note="V->I: Bypasses the requirement of SHE4 for proper FT actin cytoskeleton polarization." FT /evidence="ECO:0000269|PubMed:12808026" FT MUTAGEN 168 FT /note="N->I: Bypasses the requirement of SHE4 for proper FT actin cytoskeleton polarization." FT /evidence="ECO:0000269|PubMed:12808026" FT MUTAGEN 209 FT /note="N->S: Bypasses the requirement of SHE4 for proper FT actin cytoskeleton polarization." FT /evidence="ECO:0000269|PubMed:12808026" FT MUTAGEN 357 FT /note="S->A: Leads to a depolarized actin cytoskeleton and FT a strong defect in the capacity to internalize STE2." FT /evidence="ECO:0000269|PubMed:16478726" FT MUTAGEN 357 FT /note="S->E: No growth defect, but leads to a partially FT depolarized actin cytoskeleton. Accelerates the FT constitutive internalization of STE2." FT /evidence="ECO:0000269|PubMed:16478726" FT MUTAGEN 377 FT /note="K->M: Bypasses the requirement of SHE4 for proper FT actin cytoskeleton polarization." FT /evidence="ECO:0000269|PubMed:12808026" FT MUTAGEN 472 FT /note="E->K: In MYO5-1; temperature sensitive loss of FT function." FT /evidence="ECO:0000269|PubMed:8614799" FT MUTAGEN 1123 FT /note="W->S: Abolishes interaction with BBC1 and VRP1." FT /evidence="ECO:0000269|PubMed:10944111, FT ECO:0000269|PubMed:11901111" FT STRAND 1089..1094 FT /evidence="ECO:0007829|PDB:1ZUY" FT STRAND 1112..1118 FT /evidence="ECO:0007829|PDB:1ZUY" FT STRAND 1122..1130 FT /evidence="ECO:0007829|PDB:1ZUY" FT STRAND 1134..1138 FT /evidence="ECO:0007829|PDB:1ZUY" FT HELIX 1139..1141 FT /evidence="ECO:0007829|PDB:1ZUY" FT STRAND 1142..1144 FT /evidence="ECO:0007829|PDB:1YP5" SQ SEQUENCE 1219 AA; 136899 MW; DFFB9EC16B61CD29 CRC64; MAILKRGARK KVHQEPAKRS ANIKKATFDS SKKKEVGVSD LTLLSKISDE AINENLKKRF LNATIYTYIG HVLISVNPFR DLGIYTDAVM NEYKGKNRLE VPPHVFAIAE SMYYNMKSYN ENQCVIISGE SGAGKTEAAK RIMQYIAAAS STHTESIGKI KDMVLATNPL LESFGCAKTL RNNNSSRHGK YLEIKFNNQF EPCAGNITNY LLEKQRVVSQ IKNERNFHIF YQFTKGASDA YRQTFGVQKP EQYVYTAAAG CISAETIDDL QDYQETLKAM RVIGLGQEEQ DQIFRMLAAI LWIGNVSFIE NEEGNAQVRD TSVTDFVAYL LQIDSQLLIK SLVERIMETN HGMKRGSVYH VPLNIVQADA VRDALAKAIY NNLFDWIVSR VNKSLQAFPG AEKSIGILDI YGFEIFEHNS FEQICINYVN EKLQQIFIQL TLKSEQETYE REKIQWTPIK YFDNKVVCDL IEARRPPGIF AAMNDSVATA HADSNAADQA FAQRLNLFTT NPHFDLRSNK FVIKHYAGDV TYDIDGITDK NKDQLQKDLV ELIGTTTNTF LATIFPDTVD RESKRRPPTA GDKIIKSAND LVETLSKAQP SYIRTIKPNE TKSPNDYDDR QVLHQIKYLG LQENVRIRRA GFAYRQVFEK FVERFYLLSP HCSYAGDYTW QGDTLDAVKY ILQDSSIPQQ EYQLGVTSVF IKTPETLFAL EHMRDRYWHN MAARIQRAWR RFLQRRIDAA TKIQRTIRER KEGNKYEKLR DYGTKVLGGR KERRSMSLLG YRAFMGDYLS CNESKSKGAY IKRQVSIKEK VIFSIHGEAL HTKFGRSAQR LKKTFLLTPT TLYIVGQTLV QNAMTYTQDY KIDVRNIQAV SLTNLQDDWV AIKLASSGQP DPLINTYFKT ELITHLKRLN DKIQIKIGSA IEYQKKPGKL HSVKCQINES APKYGDIYKS STISVRRGNP PNSQVHKKPR KKSSISSGYH ASSSQATRRP VSIAAAQHVP TAPASRHSKK PAPPPPGMQN KAATRRSVPN PASTLTASQS NARPSPPTAA TRATPAATPA AAAMGSGRQA NIPPPPPPPP PSSKPKEPMF EAAYDFPGSG SPSELPLKKG DVIYITREEP SGWSLGKLLD GSKEGWVPTA YMKPHSGNNN IPTPPQNRDV PKPVLNSVQH DNTSANVIPA AAQASLGDGL ANALAARANK MRLESDDEEA NEDEEEDDW //