ID MYO10_BOVIN Reviewed; 2052 AA. AC P79114; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 30-NOV-2016, entry version 125. DE RecName: Full=Unconventional myosin-X; DE AltName: Full=Unconventional myosin-10; GN Name=MYO10; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Aorta; RX PubMed=10984435; RA Berg J.S., Derfler B.H., Pennisi C.M., Corey D.P., Cheney R.E.; RT "Myosin-X, a novel myosin with pleckstrin homology domains, associates RT with regions of dynamic actin."; RL J. Cell Sci. 113:3439-3451(2000). RN [2] RP FUNCTION, AND INTERACTION WITH CALM. RX PubMed=11457842; DOI=10.1074/jbc.M104785200; RA Homma K., Saito J., Ikebe R., Ikebe M.; RT "Motor function and regulation of myosin X."; RL J. Biol. Chem. 276:34348-34354(2001). RN [3] RP SUBCELLULAR LOCATION. RX PubMed=11854753; DOI=10.1038/ncb762; RA Berg J.S., Cheney R.E.; RT "Myosin-X is an unconventional myosin that undergoes intrafilopodial RT motility."; RL Nat. Cell Biol. 4:246-250(2002). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ITGB1; ITGB3 AND RP ITGB5. RX PubMed=15156152; DOI=10.1038/ncb1136; RA Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A., RA Cheney R.E., Stromblad S.; RT "Myosin-X provides a motor-based link between integrins and the RT cytoskeleton."; RL Nat. Cell Biol. 6:523-531(2004). RN [5] RP FUNCTION IN ACTIN BINDING AND ATP HYDROLYSIS. RX PubMed=15705568; DOI=10.1074/jbc.M500616200; RA Kovacs M., Wang F., Sellers J.R.; RT "Mechanism of action of myosin X, a membrane-associated molecular RT motor."; RL J. Biol. Chem. 280:15071-15083(2005). RN [6] RP FUNCTION IN REGULATION OF FILOPODIA ASSEMBLY AND REGULATION OF CELL RP SHAPE. RX PubMed=16894163; DOI=10.1073/pnas.0602443103; RA Bohil A.B., Robertson B.W., Cheney R.E.; RT "Myosin-X is a molecular motor that functions in filopodia RT formation."; RL Proc. Natl. Acad. Sci. U.S.A. 103:12411-12416(2006). RN [7] RP FUNCTION. RX PubMed=20081229; DOI=10.1074/jbc.M109.017269; RA McMichael B.K., Cheney R.E., Lee B.S.; RT "Myosin X regulates sealing zone patterning in osteoclasts through RT linkage of podosomes and microtubules."; RL J. Biol. Chem. 285:9506-9515(2010). RN [8] RP FUNCTION. RX PubMed=20392702; DOI=10.1074/jbc.M109.093864; RA Watanabe T.M., Tokuo H., Gonda K., Higuchi H., Ikebe M.; RT "Myosin-X induces filopodia by multiple elongation mechanism."; RL J. Biol. Chem. 285:19605-19614(2010). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND RP PHOSPHATIDYLINOSITOL-3,4,5-TRISPHOSPHATE BINDING. RX PubMed=20930142; DOI=10.1242/jcs.069609; RA Plantard L., Arjonen A., Lock J.G., Nurani G., Ivaska J., RA Stromblad S.; RT "PtdIns(3,4,5)P is a regulator of myosin-X localization and filopodia RT formation."; RL J. Cell Sci. 123:3525-3534(2010). RN [10] RP FUNCTION, AND INTERACTION WITH CALM. RX PubMed=20364131; DOI=10.1038/nsmb.1785; RA Sun Y., Sato O., Ruhnow F., Arsenault M.E., Ikebe M., Goldman Y.E.; RT "Single-molecule stepping and structural dynamics of myosin X."; RL Nat. Struct. Mol. Biol. 17:485-491(2010). RN [11] RP FUNCTION, DOMAIN, INTERACTION WITH CALM, AND SUBUNIT. RX PubMed=21666676; DOI=10.1038/nsmb.2065; RA Umeki N., Jung H.S., Sakai T., Sato O., Ikebe R., Ikebe M.; RT "Phospholipid-dependent regulation of the motor activity of myosin RT X."; RL Nat. Struct. Mol. Biol. 18:783-788(2011). RN [12] RP SAH DOMAIN. RX PubMed=25122759; DOI=10.1074/jbc.M114.585679; RA Wolny M., Batchelor M., Knight P.J., Paci E., Dougan L., Peckham M.; RT "Stable single alpha-helices are constant force springs in proteins."; RL J. Biol. Chem. 289:27825-27835(2014). CC -!- FUNCTION: In hippocampal neurons it induces the formation of CC dendritic filopodia by trafficking the actin-remodeling protein CC VASP to the tips of filopodia, where it promotes actin elongation CC (By similarity). Myosins are actin-based motor molecules with CC ATPase activity. Unconventional myosins serve in intracellular CC movements. MYO10 binds to actin filaments and actin bundles and CC functions as plus end-directed motor. The tail domain binds to CC membranous compartments containing phosphatidylinositol 3,4,5- CC trisphosphate, which are then moved relative to actin filaments. CC Stimulates the formation and elongation of filopodia. Regulates CC cell shape, cell spreading and cell adhesion. Plays a role in CC formation of the podosome belt in osteoclasts. {ECO:0000250, CC ECO:0000269|PubMed:11457842, ECO:0000269|PubMed:15156152, CC ECO:0000269|PubMed:15705568, ECO:0000269|PubMed:16894163, CC ECO:0000269|PubMed:20081229, ECO:0000269|PubMed:20364131, CC ECO:0000269|PubMed:20392702, ECO:0000269|PubMed:20930142, CC ECO:0000269|PubMed:21666676}. CC -!- SUBUNIT: Monomer, when in an inactive confomation in the cytosol. CC Homodimer in its active, membrane-bound conformation; antiparallel CC coiled coil-mediated dimer formation. Interacts with ECM29. CC Interacts with NEO 1. Interacts with VASP. Interacts with DCC and CC ITGB5; the presence of DCC inhibits ITGB5 binding. Interacts with CC tubulin; ITGB5 or DCC binding inhibits tubulin binding. Interacts CC strongly with CALM3 and weakly with CALM, the CALM3 interaction is CC essential for function in filopodial extension and motility (By CC similarity). Interacts with ITGB1, ITGB3 and ITGB5. {ECO:0000250, CC ECO:0000269|PubMed:11457842, ECO:0000269|PubMed:15156152, CC ECO:0000269|PubMed:20364131, ECO:0000269|PubMed:21666676}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection, CC lamellipodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. CC Cell projection, filopodium tip. Cytoplasm, cell cortex. Cell CC projection, filopodium membrane; Peripheral membrane protein. CC Note=May be in an inactive, monomeric conformation in the cytosol. CC Detected in cytoplasmic punctae and in cell projections. CC Colocalizes with actin fibers. Interacts with microtubules. CC Undergoes forward and rearward movements within filopodia. CC Interaction with membranes containing phosphatidylinositol 3,4,5- CC trisphosphate mediates localization at filopodium membranes. CC -!- TISSUE SPECIFICITY: Detected in kidney, testis, liver, kidney, CC cerebellum and brain cortex (at protein level). CC {ECO:0000269|PubMed:10984435}. CC -!- DOMAIN: Interaction between the motor domain and the tail leads to CC an inactive, monomeric conformation. Phospholipid binding via the CC PH domains leads to the formation of the active, dimeric form of CC the protein and strongly increases actin-dependent ATPase activity CC and motor activity. CC -!- DOMAIN: Interacts with membranes containing phosphatidylinositol- CC 3,4,5-trisphosphate via the PH domains. CC -!- DOMAIN: IQ 3 domain mediates high-affinity calcium-dependent CC binding to CALM3/CLP. {ECO:0000250}. CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a CC high content of charged residues which are predicted to stabilize CC the alpha-helical structure by ionic bonds. It can refold after CC extension suggesting an in vivo force-dependent function. The CC isolated SAH domain is monomeric; however, in its distal part CC seems to form a semirigid helical structure which overlaps with a CC region shown to mediate antiparallel coiled coil-mediated CC dimerization (PubMed:25122759). {ECO:0000305|PubMed:25122759}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FERM domain. {ECO:0000255|PROSITE- CC ProRule:PRU00084}. CC -!- SIMILARITY: Contains 3 IQ domains. {ECO:0000255|PROSITE- CC ProRule:PRU00116}. CC -!- SIMILARITY: Contains 1 myosin motor domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 MyTH4 domain. {ECO:0000255|PROSITE- CC ProRule:PRU00359}. CC -!- SIMILARITY: Contains 2 PH domains. {ECO:0000255|PROSITE- CC ProRule:PRU00145}. CC -!- CAUTION: Represents an unconventional myosin. This protein should CC not be confused with the conventional myosin-10 (MYH10). CC {ECO:0000305}. CC -!- CAUTION: Originally predicted to contain a coiled coil domain but CC shown to contain a stable SAH domain instead. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U55042; AAB39486.1; -; mRNA. DR PIR; T18519; T18519. DR RefSeq; NP_776819.1; NM_174394.2. DR UniGene; Bt.103339; -. DR PDB; 2N9B; NMR; -; A/B=884-921, A/B=934-951. DR PDB; 5HMO; X-ray; 3.49 A; A/C=796-929. DR PDBsum; 2N9B; -. DR PDBsum; 5HMO; -. DR ProteinModelPortal; P79114; -. DR SMR; P79114; -. DR DIP; DIP-46150N; -. DR IntAct; P79114; 6. DR STRING; 9913.ENSBTAP00000026812; -. DR PaxDb; P79114; -. DR PRIDE; P79114; -. DR GeneID; 281935; -. DR KEGG; bta:281935; -. DR CTD; 4651; -. DR eggNOG; KOG4229; Eukaryota. DR eggNOG; COG5022; LUCA. DR HOGENOM; HOG000007044; -. DR HOVERGEN; HBG052553; -. DR InParanoid; P79114; -. DR KO; K12559; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:UniProtKB. DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032433; C:filopodium tip; IDA:UniProtKB. DR GO; GO:0030027; C:lamellipodium; IDA:MGI. DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW. DR GO; GO:0001726; C:ruffle; IDA:MGI. DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB. DR GO; GO:0030898; F:actin-dependent ATPase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB. DR GO; GO:0060002; F:plus-end directed microfilament motor activity; IDA:UniProtKB. DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IDA:UniProtKB. DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB. DR GO; GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR Gene3D; 1.20.80.10; -; 2. DR Gene3D; 2.30.29.30; -; 5. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR031971; MYO10_CC. DR InterPro; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR000857; MyTH4_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011993; PH_dom-like. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR000159; RA_dom. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF00612; IQ; 3. DR Pfam; PF16735; MYO10_CC; 1. DR Pfam; PF00063; Myosin_head; 1. DR Pfam; PF00784; MyTH4; 1. DR Pfam; PF00169; PH; 2. DR Pfam; PF00788; RA; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR SMART; SM00295; B41; 1. DR SMART; SM00015; IQ; 3. DR SMART; SM00242; MYSc; 1. DR SMART; SM00139; MyTH4; 1. DR SMART; SM00233; PH; 2. DR SUPFAM; SSF47031; SSF47031; 2. DR SUPFAM; SSF50729; SSF50729; 4. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50057; FERM_3; 1. DR PROSITE; PS50096; IQ; 2. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. DR PROSITE; PS51016; MYTH4; 1. DR PROSITE; PS50003; PH_DOMAIN; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; ATP-binding; KW Calmodulin-binding; Cell membrane; Cell projection; Complete proteome; KW Cytoplasm; Cytoskeleton; Membrane; Motor protein; Myosin; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; KW Transport. FT CHAIN 1 2052 Unconventional myosin-X. FT /FTId=PRO_0000123472. FT DOMAIN 63 739 Myosin motor. FT DOMAIN 742 763 IQ 1. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 764 787 IQ 2. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 788 817 IQ 3. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 1206 1304 PH 1. {ECO:0000255|PROSITE- FT ProRule:PRU00145}. FT DOMAIN 1386 1491 PH 2. {ECO:0000255|PROSITE- FT ProRule:PRU00145}. FT DOMAIN 1541 1689 MyTH4. {ECO:0000255|PROSITE- FT ProRule:PRU00359}. FT DOMAIN 1694 2038 FERM. {ECO:0000255|PROSITE- FT ProRule:PRU00084}. FT REGION 815 909 SAH. {ECO:0000305|PubMed:25122759}. FT REGION 884 934 Mediates antiparallel dimerization. FT {ECO:0000250|UniProtKB:Q9HD67}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000250|UniProtKB:Q9HD67}. FT MOD_RES 963 963 Phosphoserine. FT {ECO:0000250|UniProtKB:D3ZJP6}. FT MOD_RES 966 966 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9HD67}. FT MOD_RES 1152 1152 Phosphothreonine. FT {ECO:0000250|UniProtKB:D3ZJP6}. FT HELIX 801 861 {ECO:0000244|PDB:5HMO}. FT HELIX 864 872 {ECO:0000244|PDB:5HMO}. FT TURN 873 878 {ECO:0000244|PDB:5HMO}. FT HELIX 879 910 {ECO:0000244|PDB:5HMO}. FT HELIX 914 925 {ECO:0000244|PDB:5HMO}. SQ SEQUENCE 2052 AA; 235839 MW; 43DF13424B4B2D28 CRC64; MDNFFPEGTR VWLRENGQHF PSTVNSCAEG VVVFQTDYGQ VFTYKQSTIT HQKVMPMQPT DEEGVDDMAT LTELHGGAIM HNLYQRYKRN QIYTYIGSII ASVNPYKTIT GLYSRDAVDR YSRCHLGELP PHVFAIANEC YRCLWKRHDN QCVLISGESG AGKTESTKLI LKFLSAISQQ SVDLSSKEKT SSVEQAILES SPIMEAFGNA KTVYNNNSSR FGKFVQLNIG QKGNIQGGRI VDYLLEKNRV VRQNPGERNY HIFYALLAGL GHEEREEFYL SVPENYHYLN QSGCVTDRTI SDQESFREVI MAMEVMQFSK EEVREVLRLL AGILHLGNIE FITAGGAQVS FKTALGRSAE LLGLDPAQLT DALTQRSMFL RGEEILTPLN VQQAADSRDS LAMALYARCF EWVIKKINSR IKGKDDFKSI GILDIFGFEN FEVNHFEQFN INYANEKLQE YFNKHIFSLE QLEYSREGLV WEDIDWIDNG ECLDLIEKKL GLLALINEES HFPQATDSTL LEKLHNQHAN NHFYVKPRVA VNNFGVKHYA GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH VSSRNNQDTL KCGSKHRRPT VSSQFKDSLH SLMATLSASN PFFVRCIKPN MQKMPDQFDQ AVVVNQLRYS GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RNVALPEDIR GKCTALLQLY DASNSEWQLG KTKVFLRESL EQKLEKRQEE EVTRAAMVIR AHVLGYLARK QYKKVLDCVV IIQKNYRAFL LRRRFLHLKK AAVVFQKQLR GQIARRVYRQ LLAEKRAEEE KRKREEEEKR KREEEERERE RERREAELRA QQEEAARKQR ELEALQQESQ RAAELSRELE KQKENKQVEE ILRLEKEIED LQRMKERQEL SLTEASLQKL QQLRDEELRR LEDEACRAAQ EFLESLNFDE IDECVRNIER SLSVGSGCTG EQGAGAEKPS FNFSQPYPEE EEVDEGFEAD DDAFKDSPNP SEHGHSDQRT SGIRTSDESS EEDPYMNDTV VPTSPSADST VLLAPSEHDS SAGEPTYCLP QTPGALPAPE GDYDYDQDDY EDGAITSGSS VTFSNSCSSQ WSPDYRCSVG TYNSSGAYRF SSEGAQSSFE DSEEDFDSRF DTDDELSYRR DSVYSCVTLP YFHSFLYMKG GLMNSWKRRW CVLKDETFLW FRSKQEALKQ GWLHKKGGGS STLSRRNWKK RWFVLRQAKL MYFENDSEEK LKGTVEVRAA KEIIDNTSKE NGIDIIMADR TFHLIAESPE DASQWFSVLS QVHASTDQEI REMHDEQANP QNAVGTLDVG LIDSVCASDS PDRPNSFVII TANRVLHCNA DTPEEMHHWI TLLQRSKGDT RVEGQEFIVR GWLHKEVKNS PKMSSLKLKK RWFVLTHNSL DYYKSSEKNA LKLGTLVLNS LCSVVPPDEK IFKETGYWNV TVYGRKHCYR LYTKLLNEAT RWSSAIQNVT DTKAPIDTPT QQLIQDIKEN CLNSDVVEQI YKRNPILRHT HHPLHSPLLP LPYGDINLNL LKDKGYTTLQ DEAIKIFNSL QQLESMSDPI PIIQGILQTG HDLRPLRDEL YCQLIKQTNK VPHPGSVGNL CSWQILTCLS CTFLPSRGIL KYLKFHLRRI REQFPGTEME KYALFIYESL KKTKCREFVP SRDEIEALIH RQEMTSTVHC HGGGSCKITV NSHTTAGEVV EKLIRGLAME DSRNMFALFE YNGHVDKAIE SRTIVADVLA KFEKLAATSE VGEQPWKFYF KLYCFLDTDN VPKDSVEFAF MFEQAHEAVI HGHYPAPEEN LQVLAALRLQ YLQGDYAPHA PVPPLEEVYS LQRLKARISQ STKSFTPGER LEKRRTSFLE GTLRRSFRTG SAIRQKAEEE QMVDMWVKEE VCSARASILD KWKKFQGMSQ EQAMAKYMAL IKEWPGYGST LFDVECKEGG FPQDLWLGVS ADAVSVYKRG EGRPLEVFQY EHILSFGAPL ANTYKIVVDE RELLFETSEV VDVAKLMKAY ISMIVKKRYS TSRSVSSQGS SR //