MYO3_YEAST
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 03-AUG-2022, entry version 198.
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; 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=11; 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}.
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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 PDBsum; 1RUW; -.
DR PDBsum; 1VA7; -.
DR PDBsum; 2BTT; -.
DR AlphaFoldDB; P36006; -.
DR BMRB; P36006; -.
DR SMR; P36006; -.
DR BioGRID; 34006; 128.
DR ComplexPortal; CPX-1500; Myosin class I complex, MYO3 variant.
DR DIP; DIP-2221N; -.
DR IntAct; P36006; 57.
DR MINT; P36006; -.
DR STRING; 4932.YKL129C; -.
DR MoonDB; P36006; Predicted.
DR iPTMnet; P36006; -.
DR MaxQB; P36006; -.
DR PaxDb; P36006; -.
DR PRIDE; P36006; -.
DR EnsemblFungi; YKL129C_mRNA; YKL129C; YKL129C.
DR GeneID; 853729; -.
DR KEGG; sce:YKL129C; -.
DR SGD; S000001612; MYO3.
DR VEuPathDB; FungiDB:YKL129C; -.
DR eggNOG; KOG0162; Eukaryota.
DR GeneTree; ENSGT00940000170976; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; P36006; -.
DR BioCyc; YEAST:G3O-31910-MON; -.
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:0016459; C:myosin complex; IEA:UniProtKB-KW.
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:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
DR GO; GO:0051666; P:actin cortical patch localization; IGI: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; 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: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..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..1002
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1239
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: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
