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Protein

Unconventional myosin-X

Gene

Myo10

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

Functioni

Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. May play a role in neurite outgrowth and axon guidance. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts (By similarity). Stimulates the formation and elongation of filopodia.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Transport

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-X
Alternative name(s):
Unconventional myosin-10
Gene namesi
Name:Myo10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1307193. Myo10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004162451 – 2060Unconventional myosin-XAdd BLAST2060

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei961PhosphoserineCombined sources1
Modified residuei964PhosphoserineCombined sources1
Modified residuei967PhosphoserineCombined sources1
Modified residuei1160PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiD3ZJP6.
PeptideAtlasiD3ZJP6.
PRIDEiD3ZJP6.

PTM databases

iPTMnetiD3ZJP6.

Expressioni

Gene expression databases

BgeeiENSRNOG00000010161.
ExpressionAtlasiD3ZJP6. baseline and differential.
GenevisibleiD3ZJP6. RN.

Interactioni

Subunit structurei

Monomer, when in an inactive confomation in the cytosol. Homodimer in its active, membrane-bound conformation; antiparallel coiled coil-mediated dimer formation. Interacts with ECM29. Interacts with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding. Interacts strongly with CALM3 and weakly with CALM, the CALM3 interaction is essential for function in filopodial extension and motility. Interacts with ITGB1, ITGB3 and ITGB5. Interacts with NEO1. Interacts with VASP (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063102.

Structurei

Secondary structure

12060
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1180 – 1186Combined sources7
Turni1189 – 1191Combined sources3
Beta strandi1195 – 1202Combined sources8
Beta strandi1205 – 1211Combined sources7
Beta strandi1215 – 1223Combined sources9
Helixi1225 – 1227Combined sources3
Beta strandi1229 – 1231Combined sources3
Helixi1233 – 1235Combined sources3
Beta strandi1237 – 1243Combined sources7
Beta strandi1245 – 1253Combined sources9
Beta strandi1258 – 1264Combined sources7
Helixi1265 – 1267Combined sources3
Beta strandi1269 – 1273Combined sources5
Turni1275 – 1277Combined sources3
Beta strandi1278 – 1284Combined sources7
Beta strandi1289 – 1293Combined sources5
Helixi1297 – 1311Combined sources15
Helixi1315 – 1318Combined sources4
Turni1328 – 1330Combined sources3
Beta strandi1332 – 1336Combined sources5
Helixi1337 – 1339Combined sources3
Beta strandi1340 – 1345Combined sources6
Beta strandi1354 – 1359Combined sources6
Beta strandi1362 – 1367Combined sources6
Helixi1371 – 1381Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TFMX-ray2.53A1178-1385[»]
ProteinModelPortaliD3ZJP6.
SMRiD3ZJP6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 739Myosin motorAdd BLAST677
Domaini742 – 771IQ 1PROSITE-ProRule annotationAdd BLAST30
Domaini765 – 794IQ 2PROSITE-ProRule annotationAdd BLAST30
Domaini788 – 817IQ 3PROSITE-ProRule annotationAdd BLAST30
Domaini1214 – 1312PH 1PROSITE-ProRule annotationAdd BLAST99
Domaini1394 – 1499PH 2PROSITE-ProRule annotationAdd BLAST106
Domaini1549 – 1697MyTH4PROSITE-ProRule annotationAdd BLAST149
Domaini1702 – 2046FERMPROSITE-ProRule annotationAdd BLAST345

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni815 – 907SAHBy similarityAdd BLAST93
Regioni882 – 932Mediates antiparallel dimerizationBy similarityAdd BLAST51

Domaini

Interaction between the motor domain and the tail leads to an inactive, monomeric conformation. Phospholipid binding via the PH domains leads to the formation of the active, dimeric form of the protein and strongly increases actin-dependent ATPase activity and motor activity (By similarity).By similarity
Interacts with membranes containing phosphatidylinositol-3,4,5-trisphosphate via the PH domains.1 Publication
IQ 3 domain mediates high-affinity calcium-dependent binding to CALM3/CLP.By similarity
The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. It can refold after extension suggesting an in vivo force-dependent function. The isolated SAH domain is monomeric; however, in its distal part seems to form a semirigid helical structure which overlaps with a region shown to mediate antiparallel coiled coil dimerization.By similarity

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation
Contains 3 IQ domains.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated
Contains 1 MyTH4 domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4229. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129697.
InParanoidiD3ZJP6.
OMAiPEDASQW.
OrthoDBiEOG091G006V.
TreeFamiTF316834.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 5 hits.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR000048. IQ_motif_EF-hand-BS.
IPR031971. MYO10_CC.
IPR001609. Myosin_head_motor_dom.
IPR000857. MyTH4_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00612. IQ. 3 hits.
PF16735. MYO10_CC. 1 hit.
PF00063. Myosin_head. 1 hit.
PF00784. MyTH4. 1 hit.
PF00169. PH. 2 hits.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00295. B41. 1 hit.
SM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
SM00139. MyTH4. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 2 hits.
SSF50729. SSF50729. 4 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50057. FERM_3. 1 hit.
PS50096. IQ. 3 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
PS51016. MYTH4. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D3ZJP6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSFFPEGAR VWLRENGQHF PSTVNSCAEG VVVFQTDYGQ VFTYKQSTIT
60 70 80 90 100
NQKVTAMHPL HEEGVDDMAS LTELHGGSIM YNLFQRYKRN QIYTYIGSII
110 120 130 140 150
ASVNPYQPIA GLYERATMEQ YSRCHLGELP PHIFAIANEC YRCLWKRHDN
160 170 180 190 200
QCVLISGESG AGKTESTKLI LKFLSVISQH SLDLCLQEKS SSVEQAILQS
210 220 230 240 250
SPIMEAFGNA KTVYNNNSSR FGKFVQLNIC QKGNIQGGRI VDYLLEKNRV
260 270 280 290 300
VRQNPGERNY HIFYALLAGL DQGEREEFYL SLPENYHYLN QSGCTEDKTI
310 320 330 340 350
SDQESFRQVI EAMEVMQFSK EEVREVLRLL AGILHLGNIE FITAGGAQIS
360 370 380 390 400
FKTALGRSAE LLGLDPTQLT DALTQRSMFL RGEEILTPLS VQQAVDSRDS
410 420 430 440 450
LAMALYARCF EWVIKKINSR IKGKDDFKSI GILDIFGFEN FEVNHFEQFN
460 470 480 490 500
INYANEKLQE YFNKHIFSLE QLEYSREGLV WEDIDWIDNG ECLDLIEKKL
510 520 530 540 550
GLLALINEES HFPQATDSTL LEKLHNQHAN NHFYVKPRVA VNNFGVKHYA
560 570 580 590 600
GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH ISSRNNQDTL
610 620 630 640 650
KCGSKHRRPT VSSQFKDSLH SLMATLSSSN PFFVRCIKPN TQKMPDQFDQ
660 670 680 690 700
AVVLNQLRYS GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RDLALPEDIR
710 720 730 740 750
GKCTVLLQFY DASNSEWQLG KTKVFLRESL EQKLEKRREE EIDRAAMVIR
760 770 780 790 800
AHILGYLARK QYRKVLCGVV TIQKNYRAFL ARKRFLHLKK AAIVFQKQLR
810 820 830 840 850
GRLARKVYRQ LLAEKRELEE RKRLEEEKKR EEEERERKRA QREADLLRAQ
860 870 880 890 900
QEAETRKQQE LEALQKNQRE ADLTRELEKQ RENKQVEEIL RLEKEIEDLQ
910 920 930 940 950
RMKEQQELSL TEASLQKLQQ LRDEELRRLE DEACRAAQEF LESLNFDEID
960 970 980 990 1000
ECVRNIERSL SVGSEISGEL SELAENASGE KPNFNFSQPY PEEEVDEGFE
1010 1020 1030 1040 1050
ADDDAFKDSP NPSEHGHSDQ RTSGIRTSDD SSEEDPYMNY TVVPTSPSAD
1060 1070 1080 1090 1100
STVLLAASVQ DSASLHNSSS GESTYCMPQN NGDLPSPDGD YDYDQDDYED
1110 1120 1130 1140 1150
GAITSGSSVT FSNSYGSQWS PDYRYSVGTY NSSGAYRFSS EGAQSSFEDS
1160 1170 1180 1190 1200
EEDFDSRFDT DDELSYRRDS VYSCVTLPYF HSFLYMKGGL MNSWKRRWCV
1210 1220 1230 1240 1250
LKDETFLWFR SKQEALKQGW LHKKGGGSST LSRRNWKKRW FVLRQSKLMY
1260 1270 1280 1290 1300
FENDSEEKLK GTVEVRSAKE IIDNTNKENG IDIIMADRTF HLIAESPEDA
1310 1320 1330 1340 1350
SQWFSVLSQV HSSTDQEIRE MHDEQANPQN AVGTLDVGLI DSVCASDSPD
1360 1370 1380 1390 1400
RPNSFVIITA NRVLHCNADT PEEMHHWITL LQRSKGDTRV EGQEFIVRGW
1410 1420 1430 1440 1450
LHKEVKNSPK MSSLKLKKRW FVLTHNSLDY YKSSEKNALK LGTLVLNSLC
1460 1470 1480 1490 1500
SVVPPDEKIF KETGYWNVTV YGRKHCYRLY TKLLNEATRW SSAIQNVTDT
1510 1520 1530 1540 1550
KAPIDTPTQQ LIQDIKENCL NSDVVEQIYK RNPILRYTHH PLHSPLLPLP
1560 1570 1580 1590 1600
YGDINLNLLK DKGYTTLQDE AIKIFNSLQQ LESMSDPIPI IQGILQTGHD
1610 1620 1630 1640 1650
LRPLRDELYC QLIKQTNKVP HPGSVGNLYS WQILTCLSCT FLPSRGILKY
1660 1670 1680 1690 1700
LKFHLKRIRE QFPGTEMEKY ALFIYESLKK TKCREFVPSR DEIEALIHRQ
1710 1720 1730 1740 1750
EMTSTVYCHG GGSCKITINS HTTAGEVVEK LIRGLAMEDS RNMFALFEYN
1760 1770 1780 1790 1800
GQVDKAIESR TIVADVLAKF EKLAATSEAG DAPWKFYFKL YCFLDTDSMP
1810 1820 1830 1840 1850
KDSVEFAFMF EQAHEAVIHG HHPAPEESLQ VLAALRLQYL QGDYTLHTSV
1860 1870 1880 1890 1900
PPLEEVYSLQ RLKARISQST KTFTPYERLE KRRTSFLEGT LRRSFRTGTV
1910 1920 1930 1940 1950
ARQKVEEEQM LDMWIKEEIC SARASIIDKW KKLQGVSQEQ AMAKYMALIK
1960 1970 1980 1990 2000
EWPGYGSTLF DVECKEGGFP QELWLGVSAD AVSVYKRGEG KPLEVFQYEH
2010 2020 2030 2040 2050
ILSFGAPLAN TYKIVVDERE LLFETSEVVD VAKLMKAYIS MIVKKRYSTT
2060
RSLSSQGSSR
Length:2,060
Mass (Da):237,262
Last modified:April 20, 2010 - v1
Checksum:i15CA25765D084CE6
GO

Sequence databases

RefSeqiXP_008758990.2. XM_008760768.2.
UniGeneiRn.20775.

Genome annotation databases

EnsembliENSRNOT00000065897; ENSRNOP00000063102; ENSRNOG00000010161.
GeneIDi310178.

Cross-referencesi

Sequence databases

RefSeqiXP_008758990.2. XM_008760768.2.
UniGeneiRn.20775.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TFMX-ray2.53A1178-1385[»]
ProteinModelPortaliD3ZJP6.
SMRiD3ZJP6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063102.

PTM databases

iPTMnetiD3ZJP6.

Proteomic databases

PaxDbiD3ZJP6.
PeptideAtlasiD3ZJP6.
PRIDEiD3ZJP6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000065897; ENSRNOP00000063102; ENSRNOG00000010161.
GeneIDi310178.

Organism-specific databases

RGDi1307193. Myo10.

Phylogenomic databases

eggNOGiKOG4229. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129697.
InParanoidiD3ZJP6.
OMAiPEDASQW.
OrthoDBiEOG091G006V.
TreeFamiTF316834.

Miscellaneous databases

PROiD3ZJP6.

Gene expression databases

BgeeiENSRNOG00000010161.
ExpressionAtlasiD3ZJP6. baseline and differential.
GenevisibleiD3ZJP6. RN.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 5 hits.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR000048. IQ_motif_EF-hand-BS.
IPR031971. MYO10_CC.
IPR001609. Myosin_head_motor_dom.
IPR000857. MyTH4_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00612. IQ. 3 hits.
PF16735. MYO10_CC. 1 hit.
PF00063. Myosin_head. 1 hit.
PF00784. MyTH4. 1 hit.
PF00169. PH. 2 hits.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00295. B41. 1 hit.
SM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
SM00139. MyTH4. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 2 hits.
SSF50729. SSF50729. 4 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50057. FERM_3. 1 hit.
PS50096. IQ. 3 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
PS51016. MYTH4. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMYO10_RAT
AccessioniPrimary (citable) accession number: D3ZJP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: April 20, 2010
Last modified: November 30, 2016
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-10 (MYH10).Curated
Originally predicted to contain a coiled coil domain but shown to contain a stable SAH domain instead.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.