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Q9QYF3 (MYO5A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional myosin-Va
Alternative name(s):
Dilute myosin heavy chain, non-muscle
Gene names
Name:Myo5a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1828 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation. Ref.2

Subunit structure

May be a homodimer, which associates with multiple calmodulin or myosin light chains. Binds MLPH and MYRIP By similarity. Interacts with RIPL2, the interaction is required for its role in dendrite formation. Interacts with RAB10; mediates the transport to the plasma membrane of SLC2A4/GLUT4 storage vesicles By similarity. Ref.2

Involvement in disease

Defects in Myo5a are a cause of Dilute-opisthotonus (dop). Dop rats have diluted coat color and are occasionally associated with severe neurological disorders.

Sequence similarities

Contains 1 dilute domain.

Contains 6 IQ domains.

Contains 1 myosin head-like domain.

Ontologies

Keywords
   DomainCoiled coil
Repeat
   LigandATP-binding
Actin-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

pigmentation

Inferred from mutant phenotype Ref.1. Source: MGI

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of exocytosis

Inferred from mutant phenotype PubMed 16030255PubMed 16190983. Source: RGD

secretory granule localization

Inferred from direct assay PubMed 12615975. Source: RGD

vesicle transport along actin filament

Inferred from mutant phenotype PubMed 11470781PubMed 16190983. Source: RGD

vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentactomyosin, myosin complex part

Inferred from direct assay PubMed 16030255. Source: RGD

axon

Inferred from direct assay PubMed 11977091. Source: RGD

insulin-responsive compartment

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from direct assay PubMed 11977091PubMed 14568019PubMed 16166155. Source: RGD

synaptic vesicle

Inferred from direct assay PubMed 16030255. Source: RGD

   Molecular_functionATP binding

Inferred from direct assay PubMed 16030255. Source: RGD

microfilament motor activity

Inferred from direct assay PubMed 16030255. Source: RGD

protein heterodimerization activity

Inferred from direct assay PubMed 16030255. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18281828Unconventional myosin-Va
PRO_0000123458

Regions

Domain1 – 765765Myosin head-like
Domain766 – 78823IQ 1
Domain789 – 81325IQ 2
Domain814 – 83623IQ 3
Domain837 – 86125IQ 4
Domain862 – 88423IQ 5
Domain885 – 91430IQ 6
Domain1507 – 1783277Dilute
Nucleotide binding163 – 1708ATP Potential
Region643 – 66523Actin-binding Potential
Coiled coil914 – 1239326 Potential
Coiled coil1314 – 1418105 Potential

Amino acid modifications

Modified residue6001Phosphoserine By similarity
Modified residue14251Phosphoserine By similarity
Modified residue17331Phosphothreonine Potential

Sequences

Sequence LengthMass (Da)Tools
Q9QYF3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 5B3DE1C89AE36123

FASTA1,828211,764
        10         20         30         40         50         60 
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY RLDPKTSELP 

        70         80         90        100        110        120 
HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY TYCGIVLVAI NPYEQLPIYG 

       130        140        150        160        170        180 
EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM ARDERNQSII VSGESGAGKT VSAKYAMRYF 

       190        200        210        220        230        240 
ATVSGSASEA NVEEKVLASN PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR 

       250        260        270        280        290        300 
TYLLEKSRVV FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADSFHYTKQ GGSPMIEGVD 

       310        320        330        340        350        360 
DAKEMAHTRQ ACTLLGISES YQMGIFRILA GILHLGNVGF ASRDSDSCTI PPKHEPLIIF 

       370        380        390        400        410        420 
CDLMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR DALAKHIYAK LFNWIVGHVN 

       430        440        450        460        470        480 
QALHSAVKQH SFIGVLDIYG FETFEINSFE QFCINYANEK LQQQFNMHVF KLEQEEYMKE 

       490        500        510        520        530        540 
QIPWTLIDFY DNQPCINLIE SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK 

       550        560        570        580        590        600 
PRMSNKAFII KHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS 

       610        620        630        640        650        660 
PTSATSSGRT PLTRVPVKPT KGRPGQTAKE HKKTVGLQFR NSLHLLMETL NATTPHYVRC 

       670        680        690        700        710        720 
IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR WTYQEFFSRY RVLMKQKDVL 

       730        740        750        760        770        780 
GDRKQTCQNV LEKLILDKDK YQFGKTKIFF RAGQVAYLEK LRADKLRAAC IRIQKTIRGW 

       790        800        810        820        830        840 
LLRKRYLCMQ RAAITVQRYV RGYQARCYAK FLRRTKAATT IQKYWRMYVV RRKYKIRRAA 

       850        860        870        880        890        900 
TIVLQSYLRG YLARNRYRKI LREHKAVIIQ KRVRGWLART HYKRTMKAII YLQCCFRRMM 

       910        920        930        940        950        960 
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLMEKL TNLEGVYNSE 

       970        980        990       1000       1010       1020 
TEKLRNDVER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE QTRSEKKSIE ERADKYKQET 

      1030       1040       1050       1060       1070       1080 
EQLVSNLKEE NTLLKQEKET LNHLMVEQAK EMTETMERKL VEETKQLELD LNDERLRYQN 

      1090       1100       1110       1120       1130       1140 
LLNEFSRLEE RYDDLKEEMT LMLNVPKPGH KRTDSTHSSN ESEYTFSSEF AETEDIAPRT 

      1150       1160       1170       1180       1190       1200 
EEPTEKKVPL DMSLFLKLQK RVTELGQEKQ LMQDELDRKE EQVLRSKAKG GERPQIRGAE 

      1210       1220       1230       1240       1250       1260 
LGYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVNAP GAPAYRVLME QLTAVSEELD 

      1270       1280       1290       1300       1310       1320 
VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ KMKDKGEIAQ AYIGLKETNR 

      1330       1340       1350       1360       1370       1380 
LLESQLQSQK RSHENEAEAL RGEIQSLKEE NNRQQQLLAQ NLQLPPEARI EASLQHEITR 

      1390       1400       1410       1420       1430       1440 
LTNENLDLME QLEKQDKTVR KLKKQLKVFA KKIGELEVGQ MENISPGQII DEPIRPVNIP 

      1450       1460       1470       1480       1490       1500 
RKGKDFQGML EYKREDEQKL VKNLILELKP RGVAVNLISG LPAYILFMCV RHADYLDDDQ 

      1510       1520       1530       1540       1550       1560 
KVRSLLTSTI NSIKKVLKKR GDDFETVSFW LSNTCRFLHC LKQYSGEEGF MKHNTSRQNE 

      1570       1580       1590       1600       1610       1620 
HCLTNFDLAE YRQVLSDLAI QIYQQLVRVL ENILQPMIVS GMLEHETIQG VSGVKPTGLR 

      1630       1640       1650       1660       1670       1680 
KRTSSIADEG TYTLDSILRQ LNSFHSVMCQ HGMDPELIKQ VVKQMFYIVG AITLNNLLLR 

      1690       1700       1710       1720       1730       1740 
KDMCSWSKGM QIRYNVSQLE EWLRDKNLMN SGAKETLEPL IQAAQLLQVK KKTDDDAEAI 

      1750       1760       1770       1780       1790       1800 
CSMCNALTTA QIVKVLNLYT PVNEFEERVS VSFIRTIQVR LRDRKDSPQL LMDAKHIFPV 

      1810       1820 
TFPFNPSSLA LETIQIPASL GLGFIARV

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References

[1]"Identification of a novel myosin-Va mutation in an ataxic mutant rat, dilute-opisthotonus."
Futaki S., Takagishi Y., Hayashi Y., Ohmori S., Kanou Y., Inouye M., Oda S., Seo H., Iwaikawa Y., Murata Y.
Mamm. Genome 11:649-655(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Myosin-Va-interacting protein, RILPL2, controls cell shape and neuronal morphogenesis via Rac signaling."
Lise M.F., Srivastava D.P., Arstikaitis P., Lett R.L., Sheta R., Viswanathan V., Penzes P., O'Connor T.P., El-Husseini A.
J. Cell Sci. 122:3810-3821(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RIPL2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB035736 mRNA. Translation: BAA88350.1.
IPIIPI00214038.
RefSeqNP_071514.1. NM_022178.1.
UniGeneRn.44865.

3D structure databases

ProteinModelPortalQ9QYF3.
SMRQ9QYF3. Positions 2-820.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-7138773.
STRING10116.ENSRNOP00000029604.

PTM databases

PhosphoSiteQ9QYF3.

Proteomic databases

PaxDbQ9QYF3.
PRIDEQ9QYF3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25017.
KEGGrno:25017.
UCSCRGD:3143. rat.

Organism-specific databases

CTD4644.
RGD3143. Myo5a.

Phylogenomic databases

eggNOGCOG5022.
HOVERGENHBG052556.
KOK10357.

Gene expression databases

GenevestigatorQ9QYF3.
GermOnlineENSRNOG00000022968. Rattus norvegicus.

Family and domain databases

InterProIPR018444. Dil_domain.
IPR002710. Dilute.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
[Graphical view]
PfamPF01843. DIL. 1 hit.
PF00612. IQ. 6 hits.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 6 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
PROSITEPS51126. DILUTE. 1 hit.
PS50096. IQ. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio605105.

Entry information

Entry nameMYO5A_RAT
AccessionPrimary (citable) accession number: Q9QYF3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents