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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

Enzyme and pathway databases

ReactomeiR-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20602060Unconventional myosin-XPRO_0000416245Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei961 – 9611PhosphoserineCombined sources
Modified residuei964 – 9641PhosphoserineCombined sources
Modified residuei967 – 9671PhosphoserineCombined sources
Modified residuei1160 – 11601PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiD3ZJP6.

Expressioni

Gene expression databases

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

1
2060
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1180 – 11867Combined sources
Turni1189 – 11913Combined sources
Beta strandi1195 – 12028Combined sources
Beta strandi1205 – 12117Combined sources
Beta strandi1215 – 12239Combined sources
Helixi1225 – 12273Combined sources
Beta strandi1229 – 12313Combined sources
Helixi1233 – 12353Combined sources
Beta strandi1237 – 12437Combined sources
Beta strandi1245 – 12539Combined sources
Beta strandi1258 – 12647Combined sources
Helixi1265 – 12673Combined sources
Beta strandi1269 – 12735Combined sources
Turni1275 – 12773Combined sources
Beta strandi1278 – 12847Combined sources
Beta strandi1289 – 12935Combined sources
Helixi1297 – 131115Combined sources
Helixi1315 – 13184Combined sources
Turni1328 – 13303Combined sources
Beta strandi1332 – 13365Combined sources
Helixi1337 – 13393Combined sources
Beta strandi1340 – 13456Combined sources
Beta strandi1354 – 13596Combined sources
Beta strandi1362 – 13676Combined sources
Helixi1371 – 138111Combined sources

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 739677Myosin motorAdd
BLAST
Domaini742 – 77130IQ 1PROSITE-ProRule annotationAdd
BLAST
Domaini765 – 79430IQ 2PROSITE-ProRule annotationAdd
BLAST
Domaini788 – 81730IQ 3PROSITE-ProRule annotationAdd
BLAST
Domaini1214 – 131299PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini1394 – 1499106PH 2PROSITE-ProRule annotationAdd
BLAST
Domaini1549 – 1697149MyTH4PROSITE-ProRule annotationAdd
BLAST
Domaini1702 – 2046345FERMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni815 – 90793SAHBy similarityAdd
BLAST
Regioni882 – 93251Mediates antiparallel dimerizationBy similarityAdd
BLAST

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.
GeneTreeiENSGT00840000129687.
InParanoidiD3ZJP6.
OMAiPEDASQW.
OrthoDBiEOG7Q5HC9.
TreeFamiTF316834.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 4 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

UniGeneiRn.20775.

Genome annotation databases

EnsembliENSRNOT00000065897; ENSRNOP00000063102; ENSRNOG00000010161.

Cross-referencesi

Sequence databases

UniGeneiRn.20775.

3D structure databases

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063102.

Proteomic databases

PaxDbiD3ZJP6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000065897; ENSRNOP00000063102; ENSRNOG00000010161.

Organism-specific databases

RGDi1307193. Myo10.

Phylogenomic databases

eggNOGiKOG4229. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129687.
InParanoidiD3ZJP6.
OMAiPEDASQW.
OrthoDBiEOG7Q5HC9.
TreeFamiTF316834.

Enzyme and pathway databases

ReactomeiR-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

PROiD3ZJP6.

Gene expression databases

ExpressionAtlasiD3ZJP6. baseline and differential.
GenevisibleiD3ZJP6. RN.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 4 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...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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-961; SER-964; SER-967 AND THR-1160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "Structural basis of the myosin X PH1(N)-PH2-PH1(C) tandem as a specific and acute cellular PI(3,4,5)P(3) sensor."
    Lu Q., Yu J., Yan J., Wei Z., Zhang M.
    Mol. Biol. Cell 22:4268-4278(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) OF 1178-1385, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH PHOSPHATIDYLINOSITOL-3,4,5-TRISPHOSPHATE.

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: May 11, 2016
This is version 57 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.