Q99104 (MYO5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Unconventional myosin-Va

Alternative name(s):
Dilute myosin heavy chain, non-muscle

Gene names

Name:	Myo5a
Synonyms:	Dilute

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1853 AA.
Sequence status	Complete.
Protein existence	Evidence 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.8
Subunit structure	Interacts with RIPL2, the interaction is required for its role in dendrite formation By similarity. May be a homodimer, which associates with multiple calmodulin or myosin light chains. Binds MLPH and MYRIP. Interacts with RAB10; mediates the transport to the plasma membrane of SLC2A4/GLUT4 storage vesicles. Ref.4 Ref.5 Ref.8
Tissue specificity	Detected in melanocytes.
Sequence similarities	Contains 1 dilute domain. Contains 6 IQ domains. Contains 1 myosin head-like domain.

Ontologies

Keywords
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	anagen Inferred from mutant phenotype PubMed 15550542. Source: MGI cellular response to insulin stimulus Inferred from mutant phenotype Ref.8. Source: UniProtKB endoplasmic reticulum localization Inferred from mutant phenotype PubMed 10749990PubMed 8899740. Source: MGI exocytosis Inferred from mutant phenotype PubMed 15788565. Source: MGI insulin secretion Inferred from mutant phenotype PubMed 15788565. Source: MGI locomotion involved in locomotory behavior Inferred from mutant phenotype PubMed 10536275PubMed 10749990. Source: MGI long-chain fatty acid biosynthetic process Inferred from mutant phenotype PubMed 1150661. Source: MGI melanin biosynthetic process Inferred from mutant phenotype PubMed 7665913. Source: MGI melanocyte differentiation Inferred from mutant phenotype Ref.1PubMed 2379821PubMed 7828830. Source: MGI melanosome transport Inferred from direct assay PubMed 9133672. Source: MGI myelination Inferred from mutant phenotype PubMed 1150661. Source: MGI odontogenesis Inferred from direct assay PubMed 14730011. Source: MGI protein localization to plasma membrane Inferred from mutant phenotype Ref.8. Source: UniProtKB regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Inferred from mutant phenotype PubMed 11086997. Source: MGI secretory granule localization Inferred from mutant phenotype PubMed 15788565. Source: MGI synapse organization Inferred from mutant phenotype PubMed 15316067. Source: MGI synaptic transmission Inferred from mutant phenotype PubMed 15316067. Source: MGI vesicle transport along actin filament Traceable author statement PubMed 11706052. Source: MGI visual perception Inferred from mutant phenotype PubMed 15316067. Source: MGI
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 14724135. Source: MGI actomyosin Inferred from direct assay PubMed 8188282. Source: MGI cytosol Traceable author statement. Source: Reactome insulin-responsive compartment Inferred from direct assay Ref.8. Source: UniProtKB intermediate filament Inferred from direct assay PubMed 8188282. Source: MGI melanosome Inferred from direct assay PubMed 11886590Ref.5PubMed 9133672. Source: MGI microtubule plus end Inferred from direct assay PubMed 16247022. Source: MGI myosin complex Inferred from direct assay PubMed 11706052PubMed 12403814. Source: MGI neuronal cell body Inferred from direct assay Ref.1. Source: MGI photoreceptor outer segment Inferred from direct assay PubMed 14978221. Source: MGI ruffle Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW actin binding Inferred from direct assay PubMed 11706052PubMed 12403814PubMed 16137617. Source: MGI calcium ion binding Inferred from direct assay PubMed 15007063. Source: MGI calmodulin binding Inferred from direct assay PubMed 11706052PubMed 15007063. Source: MGI microfilament motor activity Inferred from direct assay PubMed 11706052PubMed 15007063. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1853

1853

Unconventional myosin-Va

PRO_0000123457

Regions

Domain

1 – 765

765

Myosin head-like

Domain

766 – 788

23

IQ 1

Domain

789 – 813

25

IQ 2

Domain

814 – 836

23

IQ 3

Domain

837 – 861

25

IQ 4

Domain

862 – 884

23

IQ 5

Domain

885 – 913

29

IQ 6

Domain

1532 – 1808

277

Dilute

Nucleotide binding

163 – 170

8

ATP Potential

Region

643 – 665

23

Actin-binding Potential

Coiled coil

914 – 1237

324

Potential

Coiled coil

1314 – 1443

130

Potential

Amino acid modifications

Modified residue

600

1

Phosphoserine Ref.6 Ref.7

Modified residue

1450

1

Phosphoserine By similarity

Modified residue

1758

1

Phosphothreonine Potential

Experimental info

Sequence conflict

695

1

A → R in CAA40651. Ref.1

Sequence conflict

904 – 905

2

EL → DV in CAA40651. Ref.1

Secondary structure

1

.

.

.

1853

Helix Strand Turn

Details...

Helix

765 – 818

54

Sequences

	Sequence		Length	Mass (Da)
	Q99104 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: D729DF9222EBCAA0	FASTA	1,853	215,538
	10 20 30 40 50 60 MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY RLDPKTGELP 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 PPKHEPLTIF 370 380 390 400 410 420 CDLMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR DALAKHIYAK LFNWIVDHVN 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 HKKTVGHQFR NSLHLLMETL NATTPHYVRC 670 680 690 700 710 720 IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR WTYQEFFSRY RVLMKQKDVL 730 740 750 760 770 780 GDRKQTCKNV LEKLILDKDK YQFGKTKIFF RAGQVAYLEK LRADKLRAAC IRIQKTIRGW 790 800 810 820 830 840 LLRKRYLCMQ RAAITVQRYV RGYQARCYAK FLRRTKAATT IQKYWRMYVV RRRYKIRRAA 850 860 870 880 890 900 TIVIQSYLRG YLTRNRYRKI LREYKAVIIQ KRVRGWLART HYKRTMKAIV 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 DQLVSNLKEE NTLLKQEKET LNHRIVEQAK EMTETMERKL VEETKQLELD LNDERLRYQN 1090 1100 1110 1120 1130 1140 LLNEFSRLEE RYDDLKEEMT LMLNVPKPGH KRTDSTHSSN ESEYTFSSEF AETEDIAPRT 1150 1160 1170 1180 1190 1200 EEPIEKKVPL DMSLFLKLQK RVTELEQEKQ LMQDELDRKE EQVFRSKAKE EERPQIRGAE 1210 1220 1230 1240 1250 1260 LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME QLTSVSEELD 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 LTNENLYFEE LYADDPKKYQ SYRISLYKRM IDLMEQLEKQ DKTVRKLKKQ LKVFAKKIGE 1450 1460 1470 1480 1490 1500 LEVGQMENIS PGQIIDEPIR PVNIPRKEKD FQGMLEYKRE DEQKLVKNLI LELKPRGVAV 1510 1520 1530 1540 1550 1560 NLIPGLPAYI LFMCVRHADY LNDDQKVRSL LTSTINSIKK VLKKRGDDFE TVSFWLSNTC 1570 1580 1590 1600 1610 1620 RFLHCLKQYS GEEGFMKHNT SRQNEHCLTN FDLAEYRQVL SDLAIQIYQQ LVRVLENILQ 1630 1640 1650 1660 1670 1680 PMIVSGMLEH ETIQGVSGVK PTGLRKRTSS IADEGTYTLD SILRQLNSFH SVMCQHGMDP 1690 1700 1710 1720 1730 1740 ELIKQVVKQM FYIVGAITLN NLLLRKDMCS WSKGMQIRYN VSQLEEWLRD KNLMNSGAKE 1750 1760 1770 1780 1790 1800 TLEPLIQAAQ LLQVKKKTDD DAEAICSMCN ALTTAQIVKV LNLYTPVNEF EERVSVSFIR 1810 1820 1830 1840 1850 TIQMRLRDRK DSPQLLMDAK HIFPVTFPFN PSSLALETIQ IPASLGLGFI ARV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel myosin heavy chain encoded by murine dilute coat colour locus." Mercer J.A., Seperack P.K., Strobel M.C., Copeland N.G., Jenkins N.A. Nature 349:709-712(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Brain.
[2]	Erratum Mercer J.A., Seperack P.K., Strobel M.C., Copeland N.G., Jenkins N.A. Nature 352:547-547(1991) Cited for: SEQUENCE REVISION.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin." Fukuda M., Kuroda T.S. J. Biol. Chem. 277:43096-43103(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYRIP.
[5]	"Identification of an organelle receptor for myosin-Va." Wu X.S., Rao K., Zhang H., Wang F., Sellers J.R., Matesic L.E., Copeland N.G., Jenkins N.A., Hammer J.A. III Nat. Cell Biol. 4:271-278(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MLPH.
[6]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600, MASS SPECTROMETRY. Tissue: Brain cortex.
[8]	"Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes." Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S., Hammer J.A., Xu T., Lippincott-Schwartz J. J. Cell Biol. 198:545-560(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN VESICULAR TRANSPORT, INTERACTION WITH RAB10.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X57377 mRNA. Translation: CAA40651.1.
AC133947 Genomic DNA. No translation available.
CT033761 Genomic DNA. No translation available.

IPI

IPI00118120.

PIR

A46761.

RefSeq

NP_034994.2. NM_010864.2.

UniGene

Mm.3645.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IX7	X-ray	2.50	C	763-820	[»]

ProteinModelPortal

Q99104.

SMR

Q99104. Positions 2-820.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29542N.

IntAct

Q99104. 6 interactions.

MINT

MINT-243234.

PTM databases

PhosphoSite

Q99104.

Proteomic databases

PaxDb

Q99104.

PRIDE

Q99104.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000123128; ENSMUSP00000116028; ENSMUSG00000034593.

GeneID

17918.

KEGG

mmu:17918.

UCSC

uc009qrr.1. mouse.

Organism-specific databases

CTD

4644.

MGI

MGI:105976. Myo5a.

Phylogenomic databases

eggNOG

COG5022.

GeneTree

ENSGT00700000104100.

HOGENOM

HOG000171839.

HOVERGEN

HBG052556.

InParanoid

Q99104.

KO

K10357.

Enzyme and pathway databases

Reactome

REACT_118324. Disease.
REACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_88307. Membrane Trafficking.

Gene expression databases

ArrayExpress

Q99104.

Bgee

Q99104.

CleanEx

MM_MYO5A.

Genevestigator

Q99104.

GermOnline

ENSMUSG00000034593. Mus musculus.

Family and domain databases

InterPro

IPR018444. Dil_domain.
IPR002710. Dilute.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]

Pfam

PF01843. DIL. 1 hit.
PF00612. IQ. 6 hits.
PF00063. Myosin_head. 1 hit.
[Graphical view]

PRINTS

PR00193. MYOSINHEAVY.

SMART

SM00015. IQ. 6 hits.
SM00242. MYSc. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 3 hits.

PROSITE

PS51126. DILUTE. 1 hit.
PS50096. IQ. 6 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MYO5A. mouse.

EvolutionaryTrace

Q99104.

NextBio

292769.

SOURCE

Search...

Entry information

Entry name

MYO5A_MOUSE

Accession

Primary (citable) accession number: Q99104
Secondary accession number(s): E9PUE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	July 27, 2011
Last modified:	May 29, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program