MYO2_YEAST
ID MYO2_YEAST Reviewed; 1574 AA.
AC P19524; D6W323;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Myosin-2;
DE AltName: Full=Cell division control protein 66;
DE AltName: Full=Class V unconventional myosin MYO2;
DE AltName: Full=Type V myosin heavy chain MYO2;
DE Short=Myosin V MYO2;
GN Name=MYO2; Synonyms=CDC66; OrderedLocusNames=YOR326W; ORFNames=O6167;
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=S288c / GRF88;
RX PubMed=2016335; DOI=10.1083/jcb.113.3.539;
RA Johnston G.C., Prendergast J.A., Singer R.A.;
RT "The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for
RT vectorial transport of vesicles.";
RL J. Cell Biol. 113:539-551(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-748.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896266;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA Schweizer M.;
RT "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT XV reveals regions of similarity to chromosomes I and XIII.";
RL Yeast 12:1021-1031(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 677-1574.
RX PubMed=8896263;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<999::aid-yea976>3.0.co;2-e;
RA Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.;
RT "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces
RT cerevisiae chromosome XV: similarity to part of chromosome I.";
RL Yeast 12:999-1004(1996).
RN [6]
RP INTERACTION WITH CMD1.
RX PubMed=8294515; DOI=10.1083/jcb.124.3.315;
RA Brockerhoff S.E., Stevens R.C., Davis T.N.;
RT "The unconventional myosin, Myo2p, is a calmodulin target at sites of cell
RT growth in Saccharomyces cerevisiae.";
RL J. Cell Biol. 124:315-323(1994).
RN [7]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-511.
RX PubMed=8188749; DOI=10.1083/jcb.125.4.825;
RA Lillie S.H., Brown S.S.;
RT "Immunofluorescence localization of the unconventional myosin, Myo2p, and
RT the putative kinesin-related protein, Smy1p, to the same regions of
RT polarized growth in Saccharomyces cerevisiae.";
RL J. Cell Biol. 125:825-842(1994).
RN [8]
RP INTERACTION WITH MLC1.
RX PubMed=9700160; DOI=10.1083/jcb.142.3.711;
RA Stevens R.C., Davis T.N.;
RT "Mlc1p is a light chain for the unconventional myosin Myo2p in
RT Saccharomyces cerevisiae.";
RL J. Cell Biol. 142:711-722(1998).
RN [9]
RP MUTAGENESIS OF GLY-1248.
RX PubMed=9843969; DOI=10.1073/pnas.95.25.14799;
RA Catlett N.L., Weisman L.S.;
RT "The terminal tail region of a yeast myosin-V mediates its attachment to
RT vacuole membranes and sites of polarized growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14799-14804(1998).
RN [10]
RP INTERACTION WITH RHO3.
RX PubMed=10207081; DOI=10.1128/mcb.19.5.3580;
RA Robinson N.G.G., Guo L., Imai J., Toh-e A., Matsui Y., Tamanoi F.;
RT "Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton
RT and exocytosis, is a GTPase which interacts with Myo2 and Exo70.";
RL Mol. Cell. Biol. 19:3580-3587(1999).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF ASP-1297; LEU-1301; ASN-1304 AND ASN-1307.
RX PubMed=10931864; DOI=10.1083/jcb.150.3.513;
RA Catlett N.L., Duex J.E., Tang F., Weisman L.S.;
RT "Two distinct regions in a yeast myosin-V tail domain are required for the
RT movement of different cargoes.";
RL J. Cell Biol. 150:513-526(2000).
RN [12]
RP INTERACTION WITH SMY1.
RX PubMed=10679024; DOI=10.1091/mbc.11.2.691;
RA Beningo K.A., Lillie S.H., Brown S.S.;
RT "The yeast kinesin-related protein Smy1p exerts its effects on the class V
RT myosin Myo2p via a physical interaction.";
RL Mol. Biol. Cell 11:691-702(2000).
RN [13]
RP INTERACTION WITH KAR9.
RX PubMed=10984058; DOI=10.1038/35023024;
RA Yin H., Pruyne D., Huffaker T.C., Bretscher A.;
RT "Myosin V orientates the mitotic spindle in yeast.";
RL Nature 406:1013-1015(2000).
RN [14]
RP FUNCTION.
RX PubMed=11285273; DOI=10.1083/jcb.153.1.47;
RA Rossanese O.W., Reinke C.A., Bevis B.J., Hammond A.T., Sears I.B.,
RA O'Connor J., Glick B.S.;
RT "A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi
RT elements in Saccharomyces cerevisiae.";
RL J. Cell Biol. 153:47-62(2001).
RN [15]
RP FUNCTION.
RX PubMed=11381095; DOI=10.1083/jcb.153.5.1121;
RA Reck-Peterson S.L., Tyska M.J., Novick P.J., Mooseker M.S.;
RT "The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin-based
RT motors.";
RL J. Cell Biol. 153:1121-1126(2001).
RN [16]
RP ERRATUM OF PUBMED:11381095.
RA Reck-Peterson S.L., Tyska M.J., Novick P.J., Mooseker M.S.;
RL J. Cell Biol. 153:1521-1521(2001).
RN [17]
RP FUNCTION.
RX PubMed=11733545; DOI=10.1083/jcb.200107028;
RA Hoepfner D., van den Berg M., Philippsen P., Tabak H.F., Hettema E.H.;
RT "A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and
RT inheritance in Saccharomyces cerevisiae.";
RL J. Cell Biol. 155:979-990(2001).
RN [18]
RP INTERACTION WITH MLC1 AND SEC4.
RX PubMed=12456647; DOI=10.1093/emboj/cdf650;
RA Wagner W., Bielli P., Wacha S., Ragnini-Wilson A.;
RT "Mlc1p promotes septum closure during cytokinesis via the IQ motifs of the
RT vesicle motor Myo2p.";
RL EMBO J. 21:6397-6408(2002).
RN [19]
RP FUNCTION.
RX PubMed=11781333; DOI=10.1083/jcb.200110086;
RA Schott D.H., Collins R.N., Bretscher A.;
RT "Secretory vesicle transport velocity in living cells depends on the
RT myosin-V lever arm length.";
RL J. Cell Biol. 156:35-39(2002).
RN [20]
RP FUNCTION, INTERACTION WITH YPT11, AND MUTAGENESIS OF VAL-1189; VAL-1288;
RP LEU-1474; GLU-1484; LYS-1500; ASP-1511; PRO-1529; GLU-1546 AND LYS-1559.
RX PubMed=12391144; DOI=10.1128/mcb.22.22.7744-7757.2002;
RA Itoh T., Watabe A., Toh-e A., Matsui Y.;
RT "Complex formation with Ypt11p, a rab-type small GTPase, is essential to
RT facilitate the function of Myo2p, a class V myosin, in mitochondrial
RT distribution in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 22:7744-7757(2002).
RN [21]
RP 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 [22]
RP INTERACTION WITH VAC17, AND MUTAGENESIS OF SER-1247; VAL-1262; PHE-1264;
RP SER-1268; THR-1274; PHE-1275 AND VAL-1288.
RX PubMed=12642614; DOI=10.1083/jcb.200210139;
RA Ishikawa K., Catlett N.L., Novak J.L., Tang F., Nau J.J., Weisman L.S.;
RT "Identification of an organelle-specific myosin V receptor.";
RL J. Cell Biol. 160:887-897(2003).
RN [23]
RP FUNCTION.
RX PubMed=12743102; DOI=10.1083/jcb.200302030;
RA Hwang E., Kusch J., Barral Y., Huffaker T.C.;
RT "Spindle orientation in Saccharomyces cerevisiae depends on the transport
RT of microtubule ends along polarized actin cables.";
RL J. Cell Biol. 161:483-488(2003).
RN [24]
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 [25]
RP INTERACTION WITH MMR1.
RX PubMed=15201867; DOI=10.1038/sj.emboj.7600271;
RA Itoh T., Toh-e A., Matsui Y.;
RT "Mmr1p is a mitochondrial factor for Myo2p-dependent inheritance of
RT mitochondria in the budding yeast.";
RL EMBO J. 23:2520-2530(2004).
RN [26]
RP INTERACTION WITH SRO7.
RX PubMed=15964280; DOI=10.1016/j.cub.2005.05.046;
RA Gangar A., Rossi G., Andreeva A., Hales R., Brennwald P.;
RT "Structurally conserved interaction of Lgl family with SNAREs is critical
RT to their cellular function.";
RL Curr. Biol. 15:1136-1142(2005).
RN [27]
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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1097 AND SER-1121, AND
RP IDENTIFICATION BY 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 [29]
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 [30]
RP FUNCTION, AND INTERACTION WITH SRO7.
RX PubMed=21248204; DOI=10.1091/mbc.e10-07-0570;
RA Rossi G., Brennwald P.;
RT "Yeast homologues of lethal giant larvae and type V myosin cooperate in the
RT regulation of Rab-dependent vesicle clustering and polarized exocytosis.";
RL Mol. Biol. Cell 22:842-857(2011).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [32]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 806-878 IN COMPLEX WITH MLC1.
RX PubMed=12351846; DOI=10.1107/s0907444902013951;
RA Terrak M., Otterbein L.R., Wu G., Palecanda L.A., Lu R.C., Dominguez R.;
RT "Crystallization, X-ray characterization and selenomethionine phasing of
RT Mlc1p bound to IQ motifs from myosin V.";
RL Acta Crystallogr. D 58:1882-1885(2002).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 806-830 AND 854-878 IN COMPLEX
RP WITH MLC1.
RX PubMed=12554638; DOI=10.1093/emboj/cdg058;
RA Terrak M., Wu G., Stafford W.F., Lu R.C., Dominguez R.;
RT "Two distinct myosin light chain structures are induced by specific
RT variations within the bound IQ motifs-functional implications.";
RL EMBO J. 22:362-371(2003).
CC -!- FUNCTION: Myosin heavy chain that is required for the cell cycle-
CC regulated transport of various organelles and proteins for their
CC segregation. Functions by binding with its tail domain to receptor
CC proteins on organelles and exerting force with its N-terminal motor
CC domain against actin filaments, thereby transporting its cargo along
CC polarized actin cables. Essential for the delivery of secretory
CC vesicles to sites of active growth during bud emergence and
CC cytokinesis. Required for segregation and inheritance of peroxisomes,
CC late Golgi compartments, mitochondria and the vacuole to the daughter
CC cell during cell division. Also required for correct alignment of the
CC spindle during mitosis. {ECO:0000269|PubMed:10931864,
CC ECO:0000269|PubMed:11285273, ECO:0000269|PubMed:11381095,
CC ECO:0000269|PubMed:11733545, ECO:0000269|PubMed:11781333,
CC ECO:0000269|PubMed:12391144, ECO:0000269|PubMed:12743102,
CC ECO:0000269|PubMed:21248204}.
CC -!- SUBUNIT: Homodimer. Interacts with calmodulin (CMD1) and the myosin
CC light chain MLC1 through its IQ repeats. Binds to the membrane
CC receptors SEC4 and VAC17 to transport secretory vesicles and the
CC vacuole, respectively. Binds to KAR9, which transports BIM1-coated
CC cytoplasmic microtubules that are attached to the spindle pole body
CC into the emerging bud, thereby correctly orienting the mitotic spindle.
CC Interacts with YPT11 and MMR1 to accelerate mitochondrial distribution
CC to the bud. Interacts with SHE4 and localizes it to the bud tip.
CC Interacts with RHO3 and SMY1, putative regulators of MYO2 function.
CC Interacts with SRO7. {ECO:0000269|PubMed:10207081,
CC ECO:0000269|PubMed:10679024, ECO:0000269|PubMed:10984058,
CC ECO:0000269|PubMed:12351846, ECO:0000269|PubMed:12391144,
CC ECO:0000269|PubMed:12456647, ECO:0000269|PubMed:12554638,
CC ECO:0000269|PubMed:12642614, ECO:0000269|PubMed:12725728,
CC ECO:0000269|PubMed:15201867, ECO:0000269|PubMed:15964280,
CC ECO:0000269|PubMed:21248204, ECO:0000269|PubMed:8294515,
CC ECO:0000269|PubMed:9700160}.
CC -!- INTERACTION:
CC P19524; Q03824: INP2; NbExp=3; IntAct=EBI-11659, EBI-27354;
CC P19524; P32526: KAR9; NbExp=2; IntAct=EBI-11659, EBI-9516;
CC P19524; P53141: MLC1; NbExp=3; IntAct=EBI-11659, EBI-10988;
CC P19524; P51534: SHE4; NbExp=2; IntAct=EBI-11659, EBI-17086;
CC P19524; P25591: VAC17; NbExp=7; IntAct=EBI-11659, EBI-21800;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:8188749}. Bud tip
CC {ECO:0000269|PubMed:8188749}. Note=Concentrates to sites of polarized
CC growth, namely to the bud tip during S and G2 phases of the cell cycle
CC and to the bud neck during cytokinesis.
CC -!- DOMAIN: The myosin motor domain binds to actin.
CC -!- DOMAIN: The IQ domains provide the interaction surface for the myosin
CC light chain MLC1.
CC -!- DOMAIN: The coiled-coiled domain is necessary for dimerization.
CC -!- DOMAIN: The tail domain is a globular cargo-binding domain involved in
CC vectorial vesicle transport.
CC -!- MISCELLANEOUS: Present with 4339 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Moves with an average velocity of 3 um/s along actin
CC cables.
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; M35532; AAA34810.1; -; Genomic_DNA.
DR EMBL; Z75234; CAA99646.1; -; Genomic_DNA.
DR EMBL; Z75235; CAA99648.1; -; Genomic_DNA.
DR EMBL; X90565; CAA62184.1; -; Genomic_DNA.
DR EMBL; Z49821; CAA89973.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11089.1; -; Genomic_DNA.
DR PIR; A38454; A38454.
DR RefSeq; NP_014971.1; NM_001183746.1.
DR PDB; 1M45; X-ray; 1.65 A; B=806-830.
DR PDB; 1M46; X-ray; 2.10 A; B=854-878.
DR PDB; 1N2D; X-ray; 2.00 A; C=806-853.
DR PDB; 2F6H; X-ray; 2.25 A; X=1152-1570.
DR PDB; 6EYW; X-ray; 2.88 A; X=1150-1574.
DR PDB; 6IXO; X-ray; 1.90 A; A=1152-1574.
DR PDB; 6IXP; X-ray; 2.73 A; A/D=1152-1574.
DR PDB; 6IXQ; X-ray; 3.06 A; A=1152-1574.
DR PDB; 6IXR; X-ray; 2.85 A; A=1152-1574.
DR PDBsum; 1M45; -.
DR PDBsum; 1M46; -.
DR PDBsum; 1N2D; -.
DR PDBsum; 2F6H; -.
DR PDBsum; 6EYW; -.
DR PDBsum; 6IXO; -.
DR PDBsum; 6IXP; -.
DR PDBsum; 6IXQ; -.
DR PDBsum; 6IXR; -.
DR AlphaFoldDB; P19524; -.
DR SMR; P19524; -.
DR BioGRID; 34711; 692.
DR ComplexPortal; CPX-1304; MYO2-VAC17-VAC8 transport complex.
DR ComplexPortal; CPX-2225; Myosin class V complex, MYO2 variant.
DR DIP; DIP-2308N; -.
DR IntAct; P19524; 50.
DR MINT; P19524; -.
DR STRING; 4932.YOR326W; -.
DR CarbonylDB; P19524; -.
DR iPTMnet; P19524; -.
DR MaxQB; P19524; -.
DR PaxDb; P19524; -.
DR PRIDE; P19524; -.
DR EnsemblFungi; YOR326W_mRNA; YOR326W; YOR326W.
DR GeneID; 854504; -.
DR KEGG; sce:YOR326W; -.
DR SGD; S000005853; MYO2.
DR VEuPathDB; FungiDB:YOR326W; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000170389; -.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; P19524; -.
DR OMA; PDPTEGW; -.
DR BioCyc; YEAST:G3O-33803-MON; -.
DR Reactome; R-SCE-9013419; RHOT2 GTPase cycle.
DR Reactome; R-SCE-9013425; RHOT1 GTPase cycle.
DR EvolutionaryTrace; P19524; -.
DR PRO; PR:P19524; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P19524; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; IMP:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0031941; C:filamentous actin; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IMP:SGD.
DR GO; GO:0071563; C:Myo2p-Vac17p-Vac8p transport complex; IPI:SGD.
DR GO; GO:0031475; C:myosin V complex; IC:ComplexPortal.
DR GO; GO:0030133; C:transport vesicle; IDA:SGD.
DR GO; GO:0031982; C:vesicle; IDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:SGD.
DR GO; GO:0000146; F:microfilament motor activity; IDA:SGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD.
DR GO; GO:0048313; P:Golgi inheritance; IMP:SGD.
DR GO; GO:0007107; P:membrane addition at site of cytokinesis; IMP:SGD.
DR GO; GO:0045033; P:peroxisome inheritance; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IDA:ComplexPortal.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IGI:SGD.
DR GO; GO:0030050; P:vesicle transport along actin filament; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
KW Cell cycle; Cell division; Coiled coil; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1574
FT /note="Myosin-2"
FT /id="PRO_0000123489"
FT DOMAIN 4..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 70..781
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 784..806
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 807..831
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 832..855
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 856..879
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 880..902
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 903..932
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1226..1501
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 443..523
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1087..1574
FT /note="Non alpha-helical, tail domain"
FT COILED 933..1088
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 1097
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 511
FT /note="E->K: In MYO2-66; disrupts actin binding."
FT /evidence="ECO:0000269|PubMed:8188749"
FT MUTAGEN 1189
FT /note="V->A: In MYO2-573; causes a mitochondria inheritance
FT defect; when associated with G-1288; M-1500; S-1529; G-1546
FT and R-1559."
FT /evidence="ECO:0000269|PubMed:12391144"
FT MUTAGEN 1247
FT /note="S->G: Intragenic suppressor of MYO2-2."
FT /evidence="ECO:0000269|PubMed:12642614"
FT MUTAGEN 1248
FT /note="G->D: In MYO2-2; causes a vacuole inheritance
FT defect."
FT /evidence="ECO:0000269|PubMed:9843969"
FT MUTAGEN 1262
FT /note="V->A: Intragenic suppressor of MYO2-2."
FT /evidence="ECO:0000269|PubMed:12642614"
FT MUTAGEN 1264
FT /note="F->S: Intragenic suppressor of MYO2-2."
FT /evidence="ECO:0000269|PubMed:12642614"
FT MUTAGEN 1268
FT /note="S->P: Intragenic suppressor of MYO2-2."
FT /evidence="ECO:0000269|PubMed:12642614"
FT MUTAGEN 1274
FT /note="T->M: Intragenic suppressor of MYO2-2."
FT /evidence="ECO:0000269|PubMed:12642614"
FT MUTAGEN 1275
FT /note="F->S: Intragenic suppressor of MYO2-2."
FT /evidence="ECO:0000269|PubMed:12642614"
FT MUTAGEN 1288
FT /note="V->A: Intragenic suppressor of MYO2-2."
FT /evidence="ECO:0000269|PubMed:12391144,
FT ECO:0000269|PubMed:12642614"
FT MUTAGEN 1288
FT /note="V->G: In MYO2-573; causes a mitochondria inheritance
FT defect; when associated with A-1189; M-1500; S-1529; G-1546
FT and R-1559."
FT /evidence="ECO:0000269|PubMed:12391144,
FT ECO:0000269|PubMed:12642614"
FT MUTAGEN 1297
FT /note="D->G,N,V: Causes a vacuole inheritance defect."
FT /evidence="ECO:0000269|PubMed:10931864"
FT MUTAGEN 1301
FT /note="L->P: Causes a vacuole inheritance defect."
FT /evidence="ECO:0000269|PubMed:10931864"
FT MUTAGEN 1304
FT /note="N->D,S: Causes a vacuole inheritance defect."
FT /evidence="ECO:0000269|PubMed:10931864"
FT MUTAGEN 1307
FT /note="N->D: Causes a vacuole inheritance defect."
FT /evidence="ECO:0000269|PubMed:10931864"
FT MUTAGEN 1474
FT /note="L->S: In MYO2-338; abolishes interaction with YPT11;
FT when associated with G-1484 and G-1511."
FT /evidence="ECO:0000269|PubMed:12391144"
FT MUTAGEN 1484
FT /note="E->G: In MYO2-338; abolishes interaction with YPT11;
FT when associated with S-1474 and G-1511."
FT /evidence="ECO:0000269|PubMed:12391144"
FT MUTAGEN 1500
FT /note="K->M: In MYO2-573; causes a mitochondria inheritance
FT defect; when associated with A-1189; G-1288; S-1529; G-1546
FT and R-1559."
FT /evidence="ECO:0000269|PubMed:12391144"
FT MUTAGEN 1511
FT /note="D->G: In MYO2-338; abolishes interaction with YPT11;
FT when associated with S-1474 and G-1484."
FT /evidence="ECO:0000269|PubMed:12391144"
FT MUTAGEN 1529
FT /note="P->S: In MYO2-573; causes a mitochondria inheritance
FT defect; when associated with A-1189; G-1288; M-1500; G-1546
FT and R-1559."
FT /evidence="ECO:0000269|PubMed:12391144"
FT MUTAGEN 1546
FT /note="E->G: In MYO2-573; causes a mitochondria inheritance
FT defect; when associated with A-1189; G-1288; M-1500; S-1529
FT and R-1559."
FT /evidence="ECO:0000269|PubMed:12391144"
FT MUTAGEN 1559
FT /note="K->R: In MYO2-573; causes a mitochondria inheritance
FT defect; when associated with A-1189; G-1288; M-1500; S-1529
FT and G-1546."
FT /evidence="ECO:0000269|PubMed:12391144"
FT HELIX 807..829
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 855..877
FT /evidence="ECO:0007829|PDB:1M46"
FT HELIX 1153..1165
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1167..1176
FT /evidence="ECO:0007829|PDB:6IXO"
FT TURN 1177..1181
FT /evidence="ECO:0007829|PDB:6IXO"
FT STRAND 1188..1191
FT /evidence="ECO:0007829|PDB:6IXR"
FT HELIX 1195..1198
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1200..1214
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1218..1237
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1241..1243
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1244..1271
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1273..1276
FT /evidence="ECO:0007829|PDB:6IXP"
FT HELIX 1281..1326
FT /evidence="ECO:0007829|PDB:6IXO"
FT TURN 1332..1335
FT /evidence="ECO:0007829|PDB:2F6H"
FT HELIX 1355..1371
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1376..1400
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1407..1426
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1432..1435
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1437..1447
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1453..1462
FT /evidence="ECO:0007829|PDB:6IXO"
FT TURN 1463..1465
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1468..1476
FT /evidence="ECO:0007829|PDB:6IXO"
FT STRAND 1482..1484
FT /evidence="ECO:0007829|PDB:6IXR"
FT HELIX 1489..1503
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1505..1507
FT /evidence="ECO:0007829|PDB:2F6H"
FT HELIX 1533..1536
FT /evidence="ECO:0007829|PDB:6IXO"
FT HELIX 1556..1568
FT /evidence="ECO:0007829|PDB:6IXO"
SQ SEQUENCE 1574 AA; 180680 MW; 1F7E2887C1E59D54 CRC64;
MSFEVGTRCW YPHKELGWIG AEVIKNEFND GKYHLELQLE DDEIVSVDTK DLNNDKDQSL
PLLRNPPILE ATEDLTSLSY LNEPAVLHAI KQRYSQLNIY TYSGIVLIAT NPFDRVDQLY
TQDMIQAYAG KRRGELEPHL FAIAEEAYRL MKNDKQNQTI VVSGESGAGK TVSAKYIMRY
FASVEEENSA TVQHQVEMSE TEQKILATNP IMEAFGNAKT TRNDNSSRFG KYLEILFDKD
TSIIGARIRT YLLERSRLVY QPPIERNYHI FYQLMAGLPA QTKEELHLTD ASDYFYMNQG
GDTKINGIDD AKEYKITVDA LTLVGITKET QHQIFKILAA LLHIGNIEIK KTRNDASLSA
DEPNLKLACE LLGIDAYNFA KWVTKKQIIT RSEKIVSNLN YSQALVAKDS VAKFIYSALF
DWLVENINTV LCNPAVNDQI SSFIGVLDIY GFEHFEKNSF EQFCINYANE KLQQEFNQHV
FKLEQEEYVK EEIEWSFIEF NDNQPCIDLI ENKLGILSLL DEESRLPAGS DESWTQKLYQ
TLDKSPTNKV FSKPRFGQTK FIVSHYALDV AYDVEGFIEK NRDTVSDGHL EVLKASTNET
LINILEGLEK AAKKLEEAKK LELEQAGSKK PGPIRTVNRK PTLGSMFKQS LIELMNTINS
TNVHYIRCIK PNADKEAWQF DNLMVLSQLR ACGVLETIRI SCAGFPSRWT FEEFVLRYYI
LIPHEQWDLI FKKKETTEED IISVVKMILD ATVKDKSKYQ IGNTKIFFKA GMLAYLEKLR
SNKMHNSIVM IQKKIRAKYY RKQYLQISQA IKYLQNNIKG FIIRQRVNDE MKVNCATLLQ
AAYRGHSIRA NVFSVLRTIT NLQKKIRKEL KQRQLKQEHE YNAAVTIQSK VRTFEPRSRF
LRTKKDTVVV QSLIRRRAAQ RKLKQLKADA KSVNHLKEVS YKLENKVIEL TQNLASKVKE
NKEMTERIKE LQVQVEESAK LQETLENMKK EHLIDIDNQK SKDMELQKTI ENNLQSTEQT
LKDAQLELED MVKQHDELKE ESKKQLEELE QTKKTLVEYQ TLNGDLQNEV KSLKEEIARL
QTAMSLGTVT TSVLPQTPLK DVMGGGASNF NNMMLENSDL SPNDLNLKSR STPSSGNNHI
DSLSVDRENG VNATQINEEL YRLLEDTEIL NQEITEGLLK GFEVPDAGVA IQLSKRDVVY
PARILIIVLS EMWRFGLTKQ SESFLAQVLT TIQKVVTQLK GNDLIPSGVF WLANVRELYS
FVVFALNSIL TEETFKNGMT DEEYKEYVSL VTELKDDFEA LSYNIYNIWL KKLQKQLQKK
AINAVVISES LPGFSAGETS GFLNKIFANT EEYTMDDILT FFNSIYWCMK SFHIENEVFH
AVVTTLLNYV DAICFNELIM KRNFLSWKRG LQLNYNVTRL EEWCKTHGLT DGTECLQHLI
QTAKLLQVRK YTIEDIDILR GICYSLTPAQ LQKLISQYQV ADYESPIPQE ILRYVADIVK
KEAALSSSGN DSKGHEHSSS IFITPETGPF TDPFSLIKTR KFDQVEAYIP AWLSLPSTKR
IVDLVAQQVV QDGH
