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 19-MAR-2014, entry version 107. 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). CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase CC activity. Unconventional myosins serve in intracellular movements. CC MYO10 binds to actin filaments and actin bundles and functions as CC plus end-directed motor. The tail domain binds to membranous CC compartments containing phosphatidylinositol 3,4,5-trisphosphate, CC which are then moved relative to actin filaments. Stimulates the CC formation and elongation of filopodia. Regulates cell shape, cell CC spreading and cell adhesion. Plays a role in formation of the CC podosome belt in osteoclasts. CC -!- SUBUNIT: Monomer, when in an inactive confomation in the cytosol. CC Homodimer in its active, membrane-bound conformation. Interacts CC with ECM29. Interacts with NEO1. Interacts with DCC and ITGB5; the CC presence of DCC inhibits ITGB5 binding. Interacts with tubulin; CC ITGB5 or DCC binding inhibits tubulin binding (By similarity). CC Interacts with CALM. Interacts with ITGB1, ITGB3 and ITGB5. 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 -!- 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 -!- SIMILARITY: Contains 1 FERM domain. CC -!- SIMILARITY: Contains 3 IQ domains. CC -!- SIMILARITY: Contains 1 myosin head-like domain. CC -!- SIMILARITY: Contains 1 MyTH4 domain. CC -!- SIMILARITY: Contains 2 PH domains. CC -!- CAUTION: Represents an unconventional myosin. This protein should CC not be confused with the conventional myosin-10 (MYH10). 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 ProteinModelPortal; P79114; -. DR DIP; DIP-46150N; -. DR IntAct; P79114; 6. DR STRING; 9913.ENSBTAP00000026812; -. DR PRIDE; P79114; -. DR GeneID; 281935; -. DR KEGG; bta:281935; -. DR CTD; 4651; -. DR eggNOG; COG5022; -. DR HOGENOM; HOG000007044; -. DR HOVERGEN; HBG052553; -. DR InParanoid; P79114; -. DR KO; K12559; -. DR NextBio; 20805812; -. 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 Gene3D; 1.20.80.10; -; 2. DR Gene3D; 2.30.29.30; -; 4. 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; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR000857; MyTH4_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011993; PH_like_dom. DR InterPro; IPR001849; Pleckstrin_homology. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF00612; IQ; 3. DR Pfam; PF00063; Myosin_head; 1. DR Pfam; PF00784; MyTH4; 1. DR Pfam; PF00169; PH; 2. 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; SSF52540; SSF52540; 1. DR PROSITE; PS50057; FERM_3; 1. DR PROSITE; PS50096; IQ; 2. DR PROSITE; PS51016; MYTH4; 1. DR PROSITE; PS50003; PH_DOMAIN; 2. PE 1: Evidence at protein level; KW Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; KW Cell membrane; Cell projection; Coiled coil; 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 1 727 Myosin head-like. FT DOMAIN 742 763 IQ 1. FT DOMAIN 764 787 IQ 2. FT DOMAIN 788 817 IQ 3. FT DOMAIN 1206 1304 PH 1. FT DOMAIN 1386 1491 PH 2. FT DOMAIN 1541 1689 MyTH4. FT DOMAIN 1694 2038 FERM. FT COILED 800 941 Potential. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 966 966 Phosphoserine (By similarity). 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 //