Myosin-4 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32492 (MYO4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1471 AA.
Sequence status	Complete.
Protein existence	Evidence 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, encoding for a repressor of the HO endonuclease, via its interaction with SHE3. Ref.4 Ref.5 Ref.6 Ref.8 Ref.10 Ref.12
Subunit structure	Interacts with SHE2 and SHE3. Ref.5 Ref.6 Ref.7 Ref.12
Subcellular location	Bud. Note: Accumulates preferentially in growing buds. Ref.8
Miscellaneous	Present with 2210 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Contains 1 dilute domain. Contains 5 IQ domains. Contains 1 myosin head-like domain.

Ontologies

Keywords
Biological process	Transport mRNA transport
Domain	Coiled coil Repeat
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Motor protein Myosin
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	endoplasmic reticulum inheritance Inferred from mutant phenotype. Source: SGD intracellular mRNA localization Inferred from mutant phenotype. Source: SGD mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW mating type switching Inferred from mutant phenotype. Source: SGD
Cellular component	cellular bud tip Inferred from direct assay Ref.12. Source: SGD filamentous actin Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD myosin complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW actin filament binding Inferred from direct assay. Source: SGD calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW microfilament motor activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SHE2	P36068	4	EBI-11681,EBI-26866
SHE3	P38272	7	EBI-11681,EBI-21600

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1471

1471

Myosin-4

PRO_0000123491

Regions

Domain

1 – 777

777

Myosin head-like

Domain

781 – 801

IQ 1

Domain

804 – 824

IQ 2

Domain

829 – 849

IQ 3

Domain

876 – 898

IQ 4

Domain

899 – 928

IQ 5

Domain

1164 – 1419

256

Dilute

Nucleotide binding

165 – 172

ATP Potential

Coiled coil

938 – 1063

126

Amino acid modifications

Modified residue

965

Phosphothreonine Ref.11

Secondary structure

1471

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P32492 [UniParc].

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

FASTA

1,471

169,344

        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' referencesShow '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: 8056830] [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: 7731988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 10212145] [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: 11032818] [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: 11101531] [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: 10792032] [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: 12499354] [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: 14562106] [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: 15328357] [Abstract] Cited for: FUNCTION.
[11]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-965, MASS SPECTROMETRY.
[12]	"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: 20439999] [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.

PIR

S30790.

RefSeq

NP_009373.1. NM_001178174.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MMI	X-ray	2.30	A/B	1091-1471	[»]

ProteinModelPortal

P32492.

SMR

P32492. Positions 2-805, 829-920, 1103-1444.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5761N.

IntAct

P32492. 36 interactions.

MINT

MINT-617203.

STRING

P32492.

Proteomic databases

PeptideAtlas

P32492.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YAL029C; YAL029C; YAL029C.

GeneID

851204.

KEGG

sce:YAL029C.

NMPDR

fig|4932.3.peg.53.

Organism-specific databases

CYGD

YAL029c.

SGD

S000000027. MYO4.

Phylogenomic databases

eggNOG

fuNOG07209.

GeneTree

EFGT00050000000497.

HOGENOM

HBG717149.

OrthoDB

EOG4H1F3S.

Gene expression databases

ArrayExpress

P32492.

Genevestigator

P32492.

GermOnline

YAL029C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR018444. Dil_domain.
IPR002710. Dilute.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR008989. Myosin_S1_N.
[Graphical view]

Pfam

PF01843. DIL. 1 hit.
PF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
[Graphical view]

PRINTS

PR00193. MYOSINHEAVY.

SMART

SM00015. IQ. 4 hits.
SM00242. MYSc. 1 hit.
[Graphical view]

SUPFAM

SSF50084. Myosin_S1_N. 1 hit.

PROSITE

PS51126. DILUTE. 1 hit.
PS50096. IQ. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

968067.

Entry information

Entry name

MYO4_YEAST

Accession

Primary (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:	December 14, 2011
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome I

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents