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P32492 (MYO4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 133. 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-4
Alternative name(s):
SWI5-dependent HO expression protein 1
Gene names
Name:MYO4
Synonyms:SHE1
Ordered Locus Names:YAL029C
ORF Names:FUN22
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1471 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruited to specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease, via its interaction with SHE3. Ref.4 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11

Subunit structure

Interacts with SHE2 and SHE3. Ref.5 Ref.6 Ref.7 Ref.11

Subcellular location

Bud. Note: Accumulates preferentially in growing buds. Ref.8

Miscellaneous

Present with 2210 molecules/cell in log phase SD medium.

Sequence similarities

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

Contains 1 dilute domain.

Contains 5 IQ domains.

Contains 1 myosin motor domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SHE2P360684EBI-11681,EBI-26866
SHE3P382727EBI-11681,EBI-21600

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14711471Myosin-4
PRO_0000123491

Regions

Domain71 – 777707Myosin motor
Domain781 – 80121IQ 1
Domain804 – 82421IQ 2
Domain829 – 84921IQ 3
Domain876 – 89823IQ 4
Domain899 – 92830IQ 5
Domain1164 – 1419256Dilute
Nucleotide binding165 – 1728ATP Potential
Coiled coil938 – 1063126

Secondary structure

.............................................. 1471
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32492 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: E79C0FE72B041E95

FASTA1,471169,344
        10         20         30         40         50         60 
MSFEVGTKCW YPHKEQGWIG GEVTKNDFFE GTFHLELKLE DGETVSIETN SFENDDDHPT 

        70         80         90        100        110        120 
LPVLRNPPIL ESTDDLTTLS YLNEPAVLHA IKKRYMNGQI YTYSGIVLIA ANPFDKVDHL 

       130        140        150        160        170        180 
YSREMIQNYS SKRKDELEPH LFAIAEEAYR FMVHEKANQT VVVSGESGAG KTVSAKYIMR 

       190        200        210        220        230        240 
YFASVQESNN REGEVEMSQI ESQILATNPI MEAFGNAKTT RNDNSSRFGK YLQILFDENT 

       250        260        270        280        290        300 
TIRGSKIRTY LLEKSRLVYQ PETERNYHIF YQILEGLPEP VKQELHLSSP KDYHYTNQGG 

       310        320        330        340        350        360 
QPNIAGIDEA REYKITTDAL SLVGINHETQ LGIFKILAGL LHIGNIEMKM TRNDASLSSE 

       370        380        390        400        410        420 
EQNLQIACEL LGIDPFNFAK WIVKKQIVTR SEKIVTNLNY NQALIARDSV AKFIYSTLFD 

       430        440        450        460        470        480 
WLVDNINKTL YDPELDQQDH VFSFIGILDI YGFEHFEKNS FEQFCINYAN EKLQQEFNQH 

       490        500        510        520        530        540 
VFKLEQEEYV KEEIEWSFIE FSDNQPCIDL IENKLGILSL LDEESRLPSG SDESWASKLY 

       550        560        570        580        590        600 
SAFNKPPSNE VFSKPRFGQT KFIVSHYAVD VEYEVEGFIE KNRDSVSLGH LDVFKATTNP 

       610        620        630        640        650        660 
IFKQILDNRE LRSDDAPEEQ NTEKKIMIPA RLSQKKPTLG SMFKKSLGEL MAIINSTNVH 

       670        680        690        700        710        720 
YIRCIKPNSE KKPWEFDNLM VLSQLRACGV LETIRISCAG FPSRWTFDEF VQRYFLLTDY 

       730        740        750        760        770        780 
SLWSGILYNP DLPKEAIVNF CQSILDATIS DSAKYQIGNT KIFFKAGMLA FLEKLRTNKM 

       790        800        810        820        830        840 
NEICIIIQKK IRARYYRLQY LQTMESIKKC QSQIRSLLVR TRVDHELKTR AAILLQTNIR 

       850        860        870        880        890        900 
ALWKREYYRA AIGQIIKLQC TCKRKLILDS VNRKFMLMAA VIIQSYIRSY GHKTDYRTLK 

       910        920        930        940        950        960 
RSSILVQSAM RMQLARRRYI VLQKEVEERN IRASYGIGLL EEAIEFKNSF ILNLEMLNDS 

       970        980        990       1000       1010       1020 
YTRLTQLLQG DLSNIPSKQR QEYETIVNGY NDKISKLKTL QVEIMNTLNK KNALKERKKK 

      1030       1040       1050       1060       1070       1080 
QSSLIQSHMQ SLAAIKGNKP SRLSDEVKSM KQELAFIENV IAQDFTTTYS ANKNDKVKGL 

      1090       1100       1110       1120       1130       1140 
GIAGQQVKPK LVNVIRRESG NPDLLELLMD LNCYTLEVTE GYLKKVNVTE VNGDNVLGPI 

      1150       1160       1170       1180       1190       1200 
HVITTVVSSL VRNGLLIQSS KFISKVLLTV ESIVMSLPKD ETMLGGIFWL SNLSRLPAFA 

      1210       1220       1230       1240       1250       1260 
ANQKTLYEAN GGDEKDKLTL IYLNDLENET LKVFDKIYST WLVKFMKHAS AHIEIFDMVL 

      1270       1280       1290       1300       1310       1320 
NEKLFKNSGD EKFAKLFTFL NEFDAVLCKF QVVDSMHTKI FNDTLKYLNV MLFNDLITKC 

      1330       1340       1350       1360       1370       1380 
PALNWKYGYE VDRNIERLVS WFEPRIEDVR PNLIQIIQAV KILQLKISNL NEFKLLFDFW 

      1390       1400       1410       1420       1430       1440 
YALNPAQIQA ILLKYKPANK GEAGVPNEIL NYLANVIKRE NLSLPGKMEI MLSAQFDSAK 

      1450       1460       1470 
NHLRYDTSAI TQNSNTEGLA TVSKIIKLDR K 

« Hide

References

« Hide 'large scale' references
[1]"Identification of MYO4, a second class V myosin gene in yeast."
Haarer B.K., Petzold A., Lillie S.H., Brown S.S.
J. Cell Sci. 107:1055-1064(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [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.
Strain: ATCC 204508 / S288c.
[4]"Association of the class V myosin Myo4p with a localised messenger RNA in budding yeast depends on She proteins."
Munchow S., Sauter C., Jansen R.P.
J. Cell Sci. 112:1511-1518(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p."
Bohl F., Kruse C., Frank A., Ferring D., Jansen R.P.
EMBO J. 19:5514-5524(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SHE2 AND SHE3.
[6]"She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA."
Long R.M., Gu W., Lorimer E., Singer R.H., Chartrand P.
EMBO J. 19:6592-6601(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SHE3.
[7]"The myosin motor, Myo4p, binds Ash1 mRNA via the adapter protein, She3p."
Takizawa P.A., Vale R.D.
Proc. Natl. Acad. Sci. U.S.A. 97:5273-5278(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHE2 AND SHE3.
[8]"Ribonucleoprotein-dependent localization of the yeast class V myosin Myo4p."
Kruse C., Jaedicke A., Beaudouin J., Bohl F., Ferring D., Guttler T., Ellenberg J., Jansen R.P.
J. Cell Biol. 159:971-982(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"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].
[10]"ASH1 mRNA anchoring requires reorganization of the Myo4p-She3p-She2p transport complex."
Gonsalvez G.B., Little J.L., Long R.M.
J. Biol. Chem. 279:46286-46294(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The structure of the Myo4p globular tail and its function in ASH1 mRNA localization."
Heuck A., Fetka I., Brewer D.N., Huls D., Munson M., Jansen R.P., Niessing D.
J. Cell Biol. 189:497-510(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1091-1471, FUNCTION, INTERACTION WITH SHE3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M90057 Unassigned DNA. Translation: AAC37409.1.
U12980 Genomic DNA. Translation: AAC05003.1.
BK006935 Genomic DNA. Translation: DAA06959.1.
PIRS30790.
RefSeqNP_009373.1. NM_001178174.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MMIX-ray2.30A/B1091-1471[»]
4LL6X-ray2.30A1098-1471[»]
4LL8X-ray3.58A918-1471[»]
ProteinModelPortalP32492.
SMRP32492. Positions 4-840, 1016-1468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31737. 55 interactions.
DIPDIP-5761N.
IntActP32492. 31 interactions.
MINTMINT-617203.
STRING4932.YAL029C.

Proteomic databases

MaxQBP32492.
PaxDbP32492.
PeptideAtlasP32492.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL029C; YAL029C; YAL029C.
GeneID851204.
KEGGsce:YAL029C.

Organism-specific databases

CYGDYAL029c.
SGDS000000027. MYO4.

Phylogenomic databases

eggNOGCOG5022.
GeneTreeENSGT00750000117369.
HOGENOMHOG000171839.
KOK10357.
OMAAEENTIV.
OrthoDBEOG77T1CS.

Enzyme and pathway databases

BioCycYEAST:G3O-28840-MONOMER.

Gene expression databases

GenevestigatorP32492.

Family and domain databases

InterProIPR018444. Dil_domain.
IPR002710. Dilute.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR008989. Myosin_S1_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF01843. DIL. 1 hit.
PF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 4 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS51126. DILUTE. 1 hit.
PS50096. IQ. 2 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32492.
NextBio968067.

Entry information

Entry nameMYO4_YEAST
AccessionPrimary (citable) accession number: P32492
Secondary accession number(s): D6VPI9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 11, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: 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