MYO5_YEAST
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 03-AUG-2022, entry version 203.
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}.
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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; 242.
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; Q04439; -.
DR PRIDE; Q04439; -.
DR EnsemblFungi; YMR109W_mRNA; YMR109W; YMR109W.
DR GeneID; 855136; -.
DR KEGG; sce:YMR109W; -.
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; MESKWGT; -.
DR BioCyc; YEAST:G3O-32805-MON; -.
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: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: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; 3.40.850.10; -; 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 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; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 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
