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 11-DEC-2019, entry version 142. 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; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE 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 with RT 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 motor."; RL J. Biol. Chem. 280:15071-15083(2005). RN [6] RP FUNCTION IN REGULATION OF FILOPODIA ASSEMBLY AND REGULATION OF CELL 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 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 linkage RT 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., 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 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 dendritic CC filopodia by trafficking the actin-remodeling protein VASP to the tips CC of filopodia, where it promotes actin elongation (By similarity). CC Myosins are actin-based motor molecules with ATPase activity. CC Unconventional myosins serve in intracellular movements. MYO10 binds to CC actin filaments and actin bundles and functions as plus end-directed CC motor. The tail domain binds to membranous compartments containing CC phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative CC to actin filaments. Stimulates the formation and elongation of CC filopodia. Regulates cell shape, cell spreading and cell adhesion. CC Plays a role in formation of the podosome belt in osteoclasts. CC {ECO:0000250, 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 ECPAS. Interacts CC with NEO 1. Interacts with VASP. Interacts with DCC and ITGB5; the CC presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5 CC or DCC binding inhibits tubulin binding. Interacts strongly with CALM3 CC and weakly with CALM, the CALM3 interaction is essential for function CC in filopodial extension and motility (By similarity). Interacts with CC ITGB1, ITGB3 and ITGB5. {ECO:0000250, ECO:0000269|PubMed:11457842, CC ECO:0000269|PubMed:15156152, ECO:0000269|PubMed:20364131, CC ECO:0000269|PubMed:21666676}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection, CC lamellipodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Cell CC projection, filopodium tip. Cytoplasm, cell cortex. Cell projection, CC filopodium membrane; Peripheral membrane protein. Note=May be in an CC inactive, monomeric conformation in the cytosol. Detected in CC cytoplasmic punctae and in cell projections. Colocalizes with actin CC fibers. Interacts with microtubules. Undergoes forward and rearward CC movements within filopodia. Interaction with membranes containing CC phosphatidylinositol 3,4,5-trisphosphate mediates localization at CC 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 an CC inactive, monomeric conformation. Phospholipid binding via the PH CC domains leads to the formation of the active, dimeric form of the CC protein and strongly increases actin-dependent ATPase activity and CC motor activity. CC -!- DOMAIN: Interacts with membranes containing phosphatidylinositol-3,4,5- CC trisphosphate via the PH domains. CC -!- DOMAIN: IQ 3 domain mediates high-affinity calcium-dependent binding to CC CALM3/CLP. {ECO:0000250}. CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high CC content of charged residues which are predicted to stabilize the alpha- CC helical structure by ionic bonds. It can refold after extension CC suggesting an in vivo force-dependent function. The isolated SAH domain CC is monomeric; however, in its distal part seems to form a semirigid CC helical structure which overlaps with a region shown to mediate CC antiparallel coiled coil-mediated dimerization (PubMed:25122759). CC {ECO:0000305|PubMed:25122759}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {ECO:0000305}. CC -!- CAUTION: Represents an unconventional myosin. This protein should not CC be confused with the conventional myosin-10 (MYH10). {ECO:0000305}. CC -!- CAUTION: Originally predicted to contain a coiled coil domain but shown CC 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 PDB; 2N9B; NMR; -; A/B=884-921. DR PDB; 5HMO; X-ray; 3.49 A; A/C=796-929. DR PDBsum; 2N9B; -. DR PDBsum; 5HMO; -. DR SMR; P79114; -. DR DIP; DIP-46150N; -. DR IntAct; P79114; 8. 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 InParanoid; P79114; -. DR KO; K12559; -. DR OrthoDB; 16113at2759; -. 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:0005516; F:calmodulin 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 CDD; cd14473; FERM_B-lobe; 1. DR CDD; cd13202; FERM_C_MyoX; 1. DR CDD; cd14873; MYSc_Myo10; 1. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 1.25.40.530; -; 1. DR Gene3D; 2.30.29.30; -; 4. DR Gene3D; 3.40.850.10; -; 1. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf. DR InterPro; IPR035963; FERM_2. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR031971; MYO10_CC. DR InterPro; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR041797; MyoX_FERM_C. DR InterPro; IPR040640; MyoX_N_SH3. DR InterPro; IPR036124; MYSc_Myo10. DR InterPro; IPR000857; MyTH4_dom. DR InterPro; IPR038185; MyTH4_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011993; PH-like_dom_sf. 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 Pfam; PF18597; SH3_19; 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; 1. 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; Calmodulin-binding; KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Membrane; KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; Transport. FT CHAIN 1..2052 FT /note="Unconventional myosin-X" FT /id="PRO_0000123472" FT DOMAIN 63..739 FT /note="Myosin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT DOMAIN 742..763 FT /note="IQ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 764..787 FT /note="IQ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 788..817 FT /note="IQ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 1206..1304 FT /note="PH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 1386..1491 FT /note="PH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 1541..1689 FT /note="MyTH4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359" FT DOMAIN 1694..2038 FT /note="FERM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084" FT NP_BIND 157..164 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT REGION 619..641 FT /note="Actin-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT REGION 815..909 FT /note="SAH" FT /evidence="ECO:0000305|PubMed:25122759" FT REGION 884..934 FT /note="Mediates antiparallel dimerization" FT /evidence="ECO:0000250|UniProtKB:Q9HD67" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q9HD67" FT MOD_RES 963 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:D3ZJP6" FT MOD_RES 966 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9HD67" FT MOD_RES 1152 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:D3ZJP6" FT HELIX 801..861 FT /evidence="ECO:0000244|PDB:5HMO" FT HELIX 864..872 FT /evidence="ECO:0000244|PDB:5HMO" FT TURN 873..878 FT /evidence="ECO:0000244|PDB:5HMO" FT HELIX 879..910 FT /evidence="ECO:0000244|PDB:5HMO" FT HELIX 914..925 FT /evidence="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 //