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P36006 (MYO3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin-3
Alternative name(s):
Actin-dependent myosin-I MYO3
Class I unconventional myosin MYO3
Type I myosin MYO3
Gene names
Name:MYO3
Ordered Locus Names:YKL129C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1272 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11

Subunit structure

Interacts (via myosin motor domain) with SHE4; this interaction is important for proper localization and may regulate the interaction of the motor domain with actin. Interacts (via SH3 domain) with VRP1; this interaction is required for localization to sites of polarized growth and may regulate the interaction of the tail domain with actin. Interacts (via SH3 domain) with PAN1; this interaction is important for late stages of endocytopsis. Interacts (via SH3 domain) with BBC1 and LAS17. Interacts (via C-terminal acidic tail) with ARC19 and ARC40; ARC19 and ARC40 are Arp2/3 complex subunits. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14

Subcellular location

Cytoplasmcytoskeletonactin patch. Note: Localizes to cortical patch-like protein structures that assemble actin patches. Enriched at sites of polarized growth. Ref.14

Domain

The myosin motor domain displays actin-stimulated ATPase activity and generates a mechanochemical force.

The tail domain participates in molecular interactions that specify the role of the motor domain. It is composed of several tail homology (TH) domains, namely a putative phospholipid-binding domain (TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).

Post-translational modification

Phosphorylation of the TEDS site (Ser-357) is required for the polarization of the actin cytoskeleton and for ligand-induced, but not for constitutive internalization of STE2. Phosphorylation probably activates the myosin-I ATPase By similarity. Ser-357 is phosphorylated by CLA4 and STE20 in vitro. Ref.6

Miscellaneous

Present with 155 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

Contains 2 IQ domains.

Contains 1 myosin motor domain.

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12721272Myosin-3
PRO_0000123490

Regions

Domain36 – 715680Myosin motor
Domain719 – 73921IQ 1
Domain740 – 76526IQ 2
Domain1120 – 118263SH3
Nucleotide binding129 – 1368ATP Potential
Region404 – 48683Actin-binding By similarity
Region759 – 961203Basic, putative membrane-binding region
Compositional bias1003 – 1123121Ala/Pro-rich
Compositional bias1109 – 11168Poly-Pro
Compositional bias1259 – 127113Asp-rich (acidic)

Amino acid modifications

Modified residue3571Phosphoserine Ref.6 Ref.13 Ref.15 Ref.16

Experimental info

Mutagenesis1321G → R: Loss of function. Ref.8
Mutagenesis3571S → A: Loss of function. Ref.6 Ref.8
Mutagenesis3571S → D: Has a constitutive higher activity in actin assembly. Ref.6 Ref.8
Mutagenesis11581W → S: Abolishes interaction with LAS17 and causes severe mislocalization of the protein.
Mutagenesis12721Missing: Abolishes interaction with ARC40.
Sequence conflict951G → RK in AAB34124. Ref.1
Sequence conflict168 – 1692NP → T in AAB34124. Ref.1
Sequence conflict263 – 2708TADTIDDV → SADQLMR in CAA81970. Ref.2
Sequence conflict917 – 9182VG → RLV in AAB34124. Ref.1
Sequence conflict10211A → R in CAA81970. Ref.2

Secondary structure

............. 1272
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36006 [UniParc].

Last modified September 21, 2011. Version 4.
Checksum: 6CB13AD3CD669600

FASTA1,272142,451
        10         20         30         40         50         60 
MAVIKKGARR KDVKEPKKRS AKIKKATFDA NKKKEVGISD LTLLSKISDE SINENLKKRF 

        70         80         90        100        110        120 
KNGIIYTYIG HVLISVNPFR DLGIYTNAVL ESYKGKNRLE VPPHVFAIAE SMYYNLKSYN 

       130        140        150        160        170        180 
ENQCVIISGE SGAGKTEAAK RIMQYIAAAS NSHSESIGKI KDMVLATNPL LESFGCAKTL 

       190        200        210        220        230        240 
RNNNSSRHGK YLEIKFNSQF EPCAGNITNY LLEKQRVVGQ IKNERNFHIF YQFTKGASDT 

       250        260        270        280        290        300 
YKQMFGVQMP EQYIYTAAAG CTTADTIDDV KDYEGTLEAM RTIGLVQEEQ DQIFRMLAAI 

       310        320        330        340        350        360 
LWIGNISFIE NEEGNAQVGD TSVTDFVAYL LQVDASLLVK CLVERIMQTS HGMKRGSVYH 

       370        380        390        400        410        420 
VPLNPVQATA VRDALAKAIY NNLFDWIVDR VNVSLQAFPG ADKSIGILDI YGFEIFEHNS 

       430        440        450        460        470        480 
FEQICINYVN EKLQQIFIQL TLKAEQETYE REKIKWTPIK YFDNKVVCDL IEAKNPPGIL 

       490        500        510        520        530        540 
AAMNDSIATA HADSNAADQA FAQRLNLFNS NPYFELRANK FVIKHYAGDV TYDINGITDK 

       550        560        570        580        590        600 
NKDQLQKDLI ELIGTTTNTF LSTIFPDDVD KDSKRRPPTA GDKIIKSANE LVETLSKAEP 

       610        620        630        640        650        660 
SYIRTIKPNQ TKSPNDYDDH QVLHQVKYLG LQENVRIRRA GFAYRQTFEK FVERFYLLSP 

       670        680        690        700        710        720 
DCSYAGDYTW DGDTLEAVKL ILRDAMIPEK EFQLGVTSVF IKTPESLFAL EDMRDKYWYN 

       730        740        750        760        770        780 
MAARIQRAWR RFLQRRIDAA IKIQRTIREK KGGNKYVKLR DYGTKLLAGK KERRSMSLLG 

       790        800        810        820        830        840 
YRAFMGDYLS CNESKTKGSY IRRQVGIKDK VVFSIKGECL HSKFGRSAQR LKKVFILTKK 

       850        860        870        880        890        900 
TFYIIGQTRE QNAMKYTQDY KIDVGKIKQV SLTNLQDDWM GVILVNSTQS DPLINTPFKT 

       910        920        930        940        950        960 
ELMTRLKKLN EKIMIKVGPT IEYHKQPNKL HTVRSKISDS APKYGDIYKS STIYVRRGHP 

       970        980        990       1000       1010       1020 
ANSKSNKKPK NPGGLSGKPI KSKKSKHKST HKHTHSHRSH RDAAKKQPLP SQKPVNPLSL 

      1030       1040       1050       1060       1070       1080 
AATAAQAAYN PKPDKTVPIK SSAIPAAKVS SKHSSKPSSK EKVAVKKASS SHKSSSAKQN 

      1090       1100       1110       1120       1130       1140 
QVSMPPSKGV EKNKEPLKET TATATANIPI PPPPPPMGQP KDPKFEAAYD FPGSGSSSEL 

      1150       1160       1170       1180       1190       1200 
PLKKGDIVFI SRDEPSGWSL AKLLDGSKEG WVPTAYMTPY KDTRNTVPVA ATGAVNDVTN 

      1210       1220       1230       1240       1250       1260 
QKSSQIDNTI SSAQEGVQFG SATVGPTSDN QSNPVGTFSD GLASALAARA NKMRAESADD 

      1270 
DDNDDGDDDD DW 

« Hide

References

« Hide 'large scale' references
[1]"Identification and molecular characterization of a yeast myosin I."
Goodson H.V., Spudich J.A.
Cell Motil. Cytoskeleton 30:73-84(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CRY3.
[2]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 263-270 AND 1021.
Strain: ATCC 204508 / S288c.
[4]"Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton."
Goodson H.V., Anderson B.L., Warrick H.M., Pon L.A., Spudich J.A.
J. Cell Biol. 133:1277-1291(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIN CYTOSKELETON ORGANIZATION.
[5]"Role of type I myosins in receptor-mediated endocytosis in yeast."
Geli M.I., Riezman H.
Science 272:533-535(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RECEPTOR ENDOCYTOSIS.
[6]"The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast."
Wu C., Lytvyn V., Thomas D.Y., Leberer E.
J. Biol. Chem. 272:30623-30626(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-357 BY CLA4 AND STE20, MUTAGENESIS OF SER-357.
[7]"A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex."
Evangelista M., Klebl B.M., Tong A.H.Y., Webb B.A., Leeuw T., Leberer E., Whiteway M., Thomas D.Y., Boone C.
J. Cell Biol. 148:353-362(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARC19; ARC40; LAS17 AND VRP1.
[8]"Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization."
Lechler T., Shevchenko A., Li R.
J. Cell Biol. 148:363-373(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARP2 AND LAS17, MUTAGENESIS OF GLY-132 AND SER-357.
[9]"The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae."
Mochida J., Yamamoto T., Fujimura-Kamada K., Tanaka K.
Genetics 160:923-934(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BBC1.
[10]"The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function."
Wesche S., Arnold M., Jansen R.-P.
Curr. Biol. 13:715-724(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SHE4.
[11]"She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae."
Toi H., Fujimura-Kamada K., Irie K., Takai Y., Todo S., Tanaka K.
Mol. Biol. Cell 14:2237-2249(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SHE4.
[12]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[14]"Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis."
Barker S.L., Lee L., Pierce B.D., Maldonado-Baez L., Drubin D.G., Wendland B.
Mol. Biol. Cell 18:2893-2903(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAN1, SUBCELLULAR LOCATION.
[15]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S.cerevisiae."
Musi V., Birdsall B., Fernandez-Ballester G., Guerrini R., Salvatori S., Serrano L., Pastore A.
Protein Sci. 15:795-807(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1123-1191.
[18]"Crystal structure of the SH3 domain from S.cerevisiae Myo3."
Kursula P., Kursula I., Lehmann F., Song Y.H., Wilmanns M.
Submitted (MAR-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1123-1191.
[19]"High-throughput structural genomics of yeast SH3 domains."
Kursula P., Lehmann F., Song Y.H., Wilmanns M.
Submitted (JUN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1123-1191.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S76960 Genomic DNA. Translation: AAB34124.1.
Z28129 Genomic DNA. Translation: CAA81970.1.
BK006944 Genomic DNA. Translation: DAA09032.2.
PIRS37958.
RefSeqNP_012793.2. NM_001179695.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RUWX-ray1.80A1121-1189[»]
1VA7X-ray2.90A/B/C/D1121-1189[»]
2BTTNMR-A1121-1189[»]
ProteinModelPortalP36006.
SMRP36006. Positions 37-715, 736-764, 1121-1189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34006. 66 interactions.
DIPDIP-2221N.
IntActP36006. 57 interactions.
MINTMINT-382399.
STRING4932.YKL129C.

Proteomic databases

MaxQBP36006.
PaxDbP36006.
PeptideAtlasP36006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL129C; YKL129C; YKL129C.
GeneID853729.
KEGGsce:YKL129C.

Organism-specific databases

SGDS000001612. MYO3.

Phylogenomic databases

eggNOGCOG5022.
GeneTreeENSGT00750000117217.
HOGENOMHOG000260265.
KOK10356.
OMAAGAPMMK.
OrthoDBEOG7VDXXK.

Enzyme and pathway databases

BioCycYEAST:G3O-31910-MONOMER.

Gene expression databases

GenevestigatorP36006.

Family and domain databases

InterProIPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP36006.
NextBio974764.

Entry information

Entry nameMYO3_YEAST
AccessionPrimary (citable) accession number: P36006
Secondary accession number(s): D6VX66
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: September 21, 2011
Last modified: July 9, 2014
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references