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Protein

Myosin-5

Gene

MYO5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 STE2.9 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi129 – 136ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • microfilament motor activity Source: SGD

GO - Biological processi

  • actin cortical patch localization Source: SGD
  • bipolar cellular bud site selection Source: SGD
  • endocytosis Source: SGD
  • exocytosis Source: SGD
  • fungal-type cell wall organization Source: SGD
  • receptor-mediated endocytosis Source: SGD
  • response to osmotic stress Source: SGD
  • response to salt stress Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Motor protein, Myosin

Keywords - Ligandi

Actin-binding, ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32805-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-5
Alternative name(s):
Actin-dependent myosin-I MYO5
Class I unconventional myosin MYO5
Type I myosin MYO5
Gene namesi
Name:MYO5
Ordered Locus Names:YMR109W
ORF Names:YM9718.08
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR109W.
SGDiS000004715. MYO5.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
  • myosin complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi164V → I: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication1
Mutagenesisi168N → I: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication1
Mutagenesisi209N → S: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication1
Mutagenesisi357S → A: Leads to a depolarized actin cytoskeleton and a strong defect in the capacity to internalize STE2. 1 Publication1
Mutagenesisi357S → E: No growth defect, but leads to a partially depolarized actin cytoskeleton. Accelerates the constitutive internalization of STE2. 1 Publication1
Mutagenesisi377K → M: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication1
Mutagenesisi472E → K in MYO5-1; temperature sensitive loss of function. 1 Publication1
Mutagenesisi1123W → S: Abolishes interaction with BBC1 and VRP1. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001234921 – 1219Myosin-5Add BLAST1219

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei357PhosphoserineCombined sources1 Publication1
Modified residuei359PhosphotyrosineCombined sources1
Modified residuei777Phosphoserine1 Publication1
Modified residuei992PhosphoserineCombined sources1
Modified residuei1205PhosphoserineCombined sources1

Post-translational modificationi

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 activity. Ser-357 is phosphorylated by YPK2 in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04439.
PRIDEiQ04439.

PTM databases

iPTMnetiQ04439.

Interactioni

Subunit structurei

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. Interacts with BZZ1, PKH1, PKH2, YPK1 and YPK2.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-11687,EBI-11687
AIM21P405632EBI-11687,EBI-25376
APP1P539332EBI-11687,EBI-28798
ARC40P383283EBI-11687,EBI-2777
BBC1P470686EBI-11687,EBI-3437
BCK1Q013896EBI-11687,EBI-3470
BNR1P404507EBI-11687,EBI-3711
BZZ1P388225EBI-11687,EBI-3889
CDC55Q003624EBI-11687,EBI-1942
CLA4P485623EBI-11687,EBI-4750
CMD1P067877EBI-11687,EBI-3976
LAS17Q124467EBI-11687,EBI-10022
OSH2Q124516EBI-11687,EBI-12621
PAN1P325212EBI-11687,EBI-12875
PKH3Q033062EBI-11687,EBI-37683
PRP8P333344EBI-11687,EBI-465
RVS167P397433EBI-11687,EBI-14500
SAP1P399554EBI-11687,EBI-16463
STE20Q034974EBI-11687,EBI-18285
UBP7P404534EBI-11687,EBI-19857
VRP1P3737019EBI-11687,EBI-20502
YOR389WQ089122EBI-11687,EBI-38289
ZRG8P400212EBI-11687,EBI-22484

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi35285. 118 interactors.
DIPiDIP-2222N.
IntActiQ04439. 99 interactors.
MINTiMINT-593586.

Structurei

Secondary structure

11219
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1089 – 1094Combined sources6
Beta strandi1112 – 1118Combined sources7
Beta strandi1122 – 1130Combined sources9
Beta strandi1134 – 1138Combined sources5
Helixi1139 – 1141Combined sources3
Beta strandi1142 – 1144Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YP5X-ray1.68A1088-1145[»]
1ZUYX-ray1.39A/B1088-1145[»]
ProteinModelPortaliQ04439.
SMRiQ04439.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04439.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 715Myosin motorAdd BLAST680
Domaini719 – 739IQ 1Add BLAST21
Domaini740 – 765IQ 2Add BLAST26
Domaini771 – 961TH1PROSITE-ProRule annotationAdd BLAST191
Domaini1085 – 1147SH3PROSITE-ProRule annotationAdd BLAST63

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni404 – 486Actin-bindingBy similarityAdd BLAST83

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1000 – 1088Ala/Pro-richAdd BLAST89
Compositional biasi1011 – 1016Poly-Pro6
Compositional biasi1060 – 1063Poly-Ala4
Compositional biasi1073 – 1081Poly-Pro9
Compositional biasi1204 – 1218Asp/Glu-rich (acidic)Add BLAST15

Domaini

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 myosin tail domain (also named TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).

Sequence similaritiesi

Contains 2 IQ domains.Curated
Contains 1 myosin motor domain.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 1 TH1 (class I myosin tail homology) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

GeneTreeiENSGT00840000129697.
HOGENOMiHOG000260265.
InParanoidiQ04439.
KOiK10356.
OMAiHVILESN.
OrthoDBiEOG092C0QJU.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_TH1.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
PS51757. TH1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04439-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAILKRGARK KVHQEPAKRS ANIKKATFDS SKKKEVGVSD LTLLSKISDE
60 70 80 90 100
AINENLKKRF LNATIYTYIG HVLISVNPFR DLGIYTDAVM NEYKGKNRLE
110 120 130 140 150
VPPHVFAIAE SMYYNMKSYN ENQCVIISGE SGAGKTEAAK RIMQYIAAAS
160 170 180 190 200
STHTESIGKI KDMVLATNPL LESFGCAKTL RNNNSSRHGK YLEIKFNNQF
210 220 230 240 250
EPCAGNITNY LLEKQRVVSQ IKNERNFHIF YQFTKGASDA YRQTFGVQKP
260 270 280 290 300
EQYVYTAAAG CISAETIDDL QDYQETLKAM RVIGLGQEEQ DQIFRMLAAI
310 320 330 340 350
LWIGNVSFIE NEEGNAQVRD TSVTDFVAYL LQIDSQLLIK SLVERIMETN
360 370 380 390 400
HGMKRGSVYH VPLNIVQADA VRDALAKAIY NNLFDWIVSR VNKSLQAFPG
410 420 430 440 450
AEKSIGILDI YGFEIFEHNS FEQICINYVN EKLQQIFIQL TLKSEQETYE
460 470 480 490 500
REKIQWTPIK YFDNKVVCDL IEARRPPGIF AAMNDSVATA HADSNAADQA
510 520 530 540 550
FAQRLNLFTT NPHFDLRSNK FVIKHYAGDV TYDIDGITDK NKDQLQKDLV
560 570 580 590 600
ELIGTTTNTF LATIFPDTVD RESKRRPPTA GDKIIKSAND LVETLSKAQP
610 620 630 640 650
SYIRTIKPNE TKSPNDYDDR QVLHQIKYLG LQENVRIRRA GFAYRQVFEK
660 670 680 690 700
FVERFYLLSP HCSYAGDYTW QGDTLDAVKY ILQDSSIPQQ EYQLGVTSVF
710 720 730 740 750
IKTPETLFAL EHMRDRYWHN MAARIQRAWR RFLQRRIDAA TKIQRTIRER
760 770 780 790 800
KEGNKYEKLR DYGTKVLGGR KERRSMSLLG YRAFMGDYLS CNESKSKGAY
810 820 830 840 850
IKRQVSIKEK VIFSIHGEAL HTKFGRSAQR LKKTFLLTPT TLYIVGQTLV
860 870 880 890 900
QNAMTYTQDY KIDVRNIQAV SLTNLQDDWV AIKLASSGQP DPLINTYFKT
910 920 930 940 950
ELITHLKRLN DKIQIKIGSA IEYQKKPGKL HSVKCQINES APKYGDIYKS
960 970 980 990 1000
STISVRRGNP PNSQVHKKPR KKSSISSGYH ASSSQATRRP VSIAAAQHVP
1010 1020 1030 1040 1050
TAPASRHSKK PAPPPPGMQN KAATRRSVPN PASTLTASQS NARPSPPTAA
1060 1070 1080 1090 1100
TRATPAATPA AAAMGSGRQA NIPPPPPPPP PSSKPKEPMF EAAYDFPGSG
1110 1120 1130 1140 1150
SPSELPLKKG DVIYITREEP SGWSLGKLLD GSKEGWVPTA YMKPHSGNNN
1160 1170 1180 1190 1200
IPTPPQNRDV PKPVLNSVQH DNTSANVIPA AAQASLGDGL ANALAARANK
1210
MRLESDDEEA NEDEEEDDW
Length:1,219
Mass (Da):136,899
Last modified:November 1, 1997 - v1
Checksum:iDFFB9EC16B61CD29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49702 Genomic DNA. Translation: CAA89745.1.
BK006946 Genomic DNA. Translation: DAA10006.1.
PIRiS54570.
RefSeqiNP_013827.1. NM_001182609.1.

Genome annotation databases

EnsemblFungiiYMR109W; YMR109W; YMR109W.
GeneIDi855136.
KEGGisce:YMR109W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49702 Genomic DNA. Translation: CAA89745.1.
BK006946 Genomic DNA. Translation: DAA10006.1.
PIRiS54570.
RefSeqiNP_013827.1. NM_001182609.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YP5X-ray1.68A1088-1145[»]
1ZUYX-ray1.39A/B1088-1145[»]
ProteinModelPortaliQ04439.
SMRiQ04439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35285. 118 interactors.
DIPiDIP-2222N.
IntActiQ04439. 99 interactors.
MINTiMINT-593586.

PTM databases

iPTMnetiQ04439.

Proteomic databases

MaxQBiQ04439.
PRIDEiQ04439.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR109W; YMR109W; YMR109W.
GeneIDi855136.
KEGGisce:YMR109W.

Organism-specific databases

EuPathDBiFungiDB:YMR109W.
SGDiS000004715. MYO5.

Phylogenomic databases

GeneTreeiENSGT00840000129697.
HOGENOMiHOG000260265.
InParanoidiQ04439.
KOiK10356.
OMAiHVILESN.
OrthoDBiEOG092C0QJU.

Enzyme and pathway databases

BioCyciYEAST:G3O-32805-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ04439.
PROiQ04439.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_TH1.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
PS51757. TH1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMYO5_YEAST
AccessioniPrimary (citable) accession number: Q04439
Secondary accession number(s): D6VZT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2280 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.