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Protein

Unconventional myosin-Va

Gene

Myo5a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi163 – 1708ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: RGD
  • ATP-dependent protein binding Source: RGD
  • calcium-dependent protein binding Source: RGD
  • microfilament motor activity Source: RGD
  • motor activity Source: RGD
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • SNARE binding Source: RGD
  • syntaxin-1 binding Source: RGD

GO - Biological processi

  • actin filament-based movement Source: RGD
  • cellular response to insulin stimulus Source: UniProtKB
  • pigmentation Source: MGI
  • protein localization to plasma membrane Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of exocytosis Source: RGD
  • secretory granule localization Source: RGD
  • vesicle-mediated transport Source: UniProtKB
  • vesicle transport along actin filament Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-Va
Alternative name(s):
Dilute myosin heavy chain, non-muscle
Gene namesi
Name:Myo5a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3143. Myo5a.

Subcellular locationi

GO - Cellular componenti

  • actomyosin, myosin complex part Source: RGD
  • axon Source: RGD
  • insulin-responsive compartment Source: UniProtKB
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • secretory granule Source: RGD
  • synaptic vesicle Source: RGD
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 18281827Unconventional myosin-VaPRO_0000123458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei600 – 6001PhosphoserineCombined sources
Modified residuei1032 – 10321PhosphothreonineCombined sources
Modified residuei1425 – 14251PhosphoserineCombined sources
Modified residuei1625 – 16251PhosphoserineCombined sources
Modified residuei1733 – 17331PhosphothreonineSequence analysis

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ9QYF3.

PTM databases

iPTMnetiQ9QYF3.
PhosphoSiteiQ9QYF3.

Interactioni

Subunit structurei

May be a homodimer, which associates with multiple calmodulin or myosin light chains. Interacts with SYTL4, 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).By similarity

GO - Molecular functioni

  • ATP-dependent protein binding Source: RGD
  • calcium-dependent protein binding Source: RGD
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • SNARE binding Source: RGD
  • syntaxin-1 binding Source: RGD

Protein-protein interaction databases

BioGridi247098. 1 interaction.
IntActiQ9QYF3. 2 interactions.
MINTiMINT-7138773.

Structurei

3D structure databases

ProteinModelPortaliQ9QYF3.
SMRiQ9QYF3. Positions 2-820.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 763695Myosin motorAdd
BLAST
Domaini766 – 78823IQ 1PROSITE-ProRule annotationAdd
BLAST
Domaini789 – 81325IQ 2PROSITE-ProRule annotationAdd
BLAST
Domaini814 – 83623IQ 3PROSITE-ProRule annotationAdd
BLAST
Domaini837 – 86125IQ 4PROSITE-ProRule annotationAdd
BLAST
Domaini862 – 88423IQ 5PROSITE-ProRule annotationAdd
BLAST
Domaini885 – 91430IQ 6PROSITE-ProRule annotationAdd
BLAST
Domaini1507 – 1783277DilutePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni643 – 66523Actin-bindingSequence analysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili914 – 1239326Sequence analysisAdd
BLAST
Coiled coili1314 – 1418105Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 dilute domain.PROSITE-ProRule annotation
Contains 6 IQ domains.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

HOVERGENiHBG052556.
InParanoidiQ9QYF3.
KOiK10357.
PhylomeDBiQ9QYF3.

Family and domain databases

InterProiIPR002710. Dilute_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00612. IQ. 6 hits.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM01132. DIL. 1 hit.
SM00015. IQ. 6 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50096. IQ. 6 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QYF3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY
60 70 80 90 100
RLDPKTSELP HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY
110 120 130 140 150
TYCGIVLVAI NPYEQLPIYG EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM
160 170 180 190 200
ARDERNQSII VSGESGAGKT VSAKYAMRYF ATVSGSASEA NVEEKVLASN
210 220 230 240 250
PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR TYLLEKSRVV
260 270 280 290 300
FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADSFHYTKQ GGSPMIEGVD
310 320 330 340 350
DAKEMAHTRQ ACTLLGISES YQMGIFRILA GILHLGNVGF ASRDSDSCTI
360 370 380 390 400
PPKHEPLIIF CDLMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR
410 420 430 440 450
DALAKHIYAK LFNWIVGHVN QALHSAVKQH SFIGVLDIYG FETFEINSFE
460 470 480 490 500
QFCINYANEK LQQQFNMHVF KLEQEEYMKE QIPWTLIDFY DNQPCINLIE
510 520 530 540 550
SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK PRMSNKAFII
560 570 580 590 600
KHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS
610 620 630 640 650
PTSATSSGRT PLTRVPVKPT KGRPGQTAKE HKKTVGLQFR NSLHLLMETL
660 670 680 690 700
NATTPHYVRC IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR
710 720 730 740 750
WTYQEFFSRY RVLMKQKDVL GDRKQTCQNV LEKLILDKDK YQFGKTKIFF
760 770 780 790 800
RAGQVAYLEK LRADKLRAAC IRIQKTIRGW LLRKRYLCMQ RAAITVQRYV
810 820 830 840 850
RGYQARCYAK FLRRTKAATT IQKYWRMYVV RRKYKIRRAA TIVLQSYLRG
860 870 880 890 900
YLARNRYRKI LREHKAVIIQ KRVRGWLART HYKRTMKAII YLQCCFRRMM
910 920 930 940 950
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLMEKL
960 970 980 990 1000
TNLEGVYNSE TEKLRNDVER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE
1010 1020 1030 1040 1050
QTRSEKKSIE ERADKYKQET EQLVSNLKEE NTLLKQEKET LNHLMVEQAK
1060 1070 1080 1090 1100
EMTETMERKL VEETKQLELD LNDERLRYQN LLNEFSRLEE RYDDLKEEMT
1110 1120 1130 1140 1150
LMLNVPKPGH KRTDSTHSSN ESEYTFSSEF AETEDIAPRT EEPTEKKVPL
1160 1170 1180 1190 1200
DMSLFLKLQK RVTELGQEKQ LMQDELDRKE EQVLRSKAKG GERPQIRGAE
1210 1220 1230 1240 1250
LGYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVNAP GAPAYRVLME
1260 1270 1280 1290 1300
QLTAVSEELD VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ
1310 1320 1330 1340 1350
KMKDKGEIAQ AYIGLKETNR LLESQLQSQK RSHENEAEAL RGEIQSLKEE
1360 1370 1380 1390 1400
NNRQQQLLAQ NLQLPPEARI EASLQHEITR LTNENLDLME QLEKQDKTVR
1410 1420 1430 1440 1450
KLKKQLKVFA KKIGELEVGQ MENISPGQII DEPIRPVNIP RKGKDFQGML
1460 1470 1480 1490 1500
EYKREDEQKL VKNLILELKP RGVAVNLISG LPAYILFMCV RHADYLDDDQ
1510 1520 1530 1540 1550
KVRSLLTSTI NSIKKVLKKR GDDFETVSFW LSNTCRFLHC LKQYSGEEGF
1560 1570 1580 1590 1600
MKHNTSRQNE HCLTNFDLAE YRQVLSDLAI QIYQQLVRVL ENILQPMIVS
1610 1620 1630 1640 1650
GMLEHETIQG VSGVKPTGLR KRTSSIADEG TYTLDSILRQ LNSFHSVMCQ
1660 1670 1680 1690 1700
HGMDPELIKQ VVKQMFYIVG AITLNNLLLR KDMCSWSKGM QIRYNVSQLE
1710 1720 1730 1740 1750
EWLRDKNLMN SGAKETLEPL IQAAQLLQVK KKTDDDAEAI CSMCNALTTA
1760 1770 1780 1790 1800
QIVKVLNLYT PVNEFEERVS VSFIRTIQVR LRDRKDSPQL LMDAKHIFPV
1810 1820
TFPFNPSSLA LETIQIPASL GLGFIARV
Length:1,828
Mass (Da):211,764
Last modified:May 1, 2000 - v1
Checksum:i5B3DE1C89AE36123
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035736 mRNA. Translation: BAA88350.1.
RefSeqiNP_071514.1. NM_022178.1.
UniGeneiRn.44865.

Genome annotation databases

GeneIDi25017.
KEGGirno:25017.
UCSCiRGD:3143. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035736 mRNA. Translation: BAA88350.1.
RefSeqiNP_071514.1. NM_022178.1.
UniGeneiRn.44865.

3D structure databases

ProteinModelPortaliQ9QYF3.
SMRiQ9QYF3. Positions 2-820.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247098. 1 interaction.
IntActiQ9QYF3. 2 interactions.
MINTiMINT-7138773.

PTM databases

iPTMnetiQ9QYF3.
PhosphoSiteiQ9QYF3.

Proteomic databases

PRIDEiQ9QYF3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25017.
KEGGirno:25017.
UCSCiRGD:3143. rat.

Organism-specific databases

CTDi4644.
RGDi3143. Myo5a.

Phylogenomic databases

HOVERGENiHBG052556.
InParanoidiQ9QYF3.
KOiK10357.
PhylomeDBiQ9QYF3.

Miscellaneous databases

NextBioi605105.
PROiQ9QYF3.

Family and domain databases

InterProiIPR002710. Dilute_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00612. IQ. 6 hits.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM01132. DIL. 1 hit.
SM00015. IQ. 6 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50096. IQ. 6 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1032, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "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.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-1425 AND SER-1625, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMYO5A_RAT
AccessioniPrimary (citable) accession number: Q9QYF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.