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Database: UniProt
Entry: W5N4L7_LEPOC
LinkDB: W5N4L7_LEPOC
Original site: W5N4L7_LEPOC 
ID   W5N4L7_LEPOC            Unreviewed;      2047 AA.
AC   W5N4L7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Myosin X {ECO:0000313|Ensembl:ENSLOCP00000015576.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000015576.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000015576.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; AHAT01002485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01002486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7918.ENSLOCP00000015576; -.
DR   Ensembl; ENSLOCT00000015605.1; ENSLOCP00000015576.1; ENSLOCG00000012650.1.
DR   eggNOG; KOG4229; Eukaryota.
DR   GeneTree; ENSGT00940000155469; -.
DR   HOGENOM; CLU_001626_1_0_1; -.
DR   InParanoid; W5N4L7; -.
DR   OMA; HYDVRGI; -.
DR   Proteomes; UP000018468; Linkage group LG9.
DR   Bgee; ENSLOCG00000012650; Expressed in zone of skin and 12 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030175; C:filopodium; IBA:GO_Central.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IBA:GO_Central.
DR   GO; GO:0060002; F:plus-end directed microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   GO; GO:0051489; P:regulation of filopodium assembly; IBA:GO_Central.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13202; FERM_C_MyoX; 1.
DR   CDD; cd17206; FERM_F1_Myosin-X; 1.
DR   CDD; cd13296; PH2_MyoX; 1.
DR   CDD; cd13297; PH3_MyoX-like; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 6.20.240.20; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 1.25.40.530; MyTH4 domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
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; 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   PANTHER; PTHR46049; AGAP003327-PA; 1.
DR   PANTHER; PTHR46049:SF2; UNCONVENTIONAL MYOSIN-X; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF16735; MYO10_CC; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00784; MyTH4; 1.
DR   Pfam; PF00169; PH; 2.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 4.
DR   SUPFAM; SSF47031; Second domain of FERM; 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   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          62..741
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1197..1295
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1377..1481
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1531..1679
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          1684..2030
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          822..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..1022
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..981
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        982..1013
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         156..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2047 AA;  235063 MW;  569F600C131041F2 CRC64;
     MAFVLQGARV WLRENDQHLP CTVSSCSGGV VVFTTDYGQV YTYKQNTLTR QKVMPMHSSS
     SEGVEDMAGL ADLHDGAIMY NLFLRYRQNK IYTYIGSILA AVNPYQFIPN LYDHPAVELY
     SRHRLGEISP HIFAVANECY RSLWKRLENQ CVLISGESGA GKTESTKLIL KFLSAMSQHS
     LEVTSKEKTS HVEQALLESS PIMEAFGNAK TVYNNNSSRF GKFVQLNFCQ KGNIQGGKIV
     DCILFYNRVV RHNPGERNYH IFYALLAGTN AEQREAFYLS QPDSYYYLKQ SGCIEDKTIN
     DKNTFHEVLN AMKTMQFSAE NIQEILRLLA GILHIGNVEF MTAGGAQVSS KSALGRAAEL
     LGLDSGQLAE VLTHRSMILR GEEISTPLTV EQAVDSRDSM AMALYSQCFT WIIRKLNSRI
     RGKEDFKSIG ILDIFGFENF EVNRFEQFNI NYANEKLQEY FNKHIFSLEQ LEYNNCGLCV
     IFITIPMPGM LLGLEEHPHL ESKQSNSYLQ RSVDNCTVDK EGSSYLRNWS FPMETSDREL
     VHYSYTKHWL GLIYYTEKDT LERNNRDFVR LNCILEVKKK KLSFFFCLFL NTHPNSGTVS
     LRQSEARQYR PIASFPLPCG AYKCPTQISL SMGRFLKILL CSTHLMPERF DQPVVLNQLR
     YSGMLETVRI RRAGFPVRRP FQDFYFRYKV LMKDVTLPED MKGKCACLLH LYDSTKTEWQ
     LGKTKVFLRE SLENKLEKQR EVEVYKAAMI IQAHIVGYVA RKQYQRLLQC IVVIQKNYRA
     FYWRRRFLHL RWAALTLQTR ARGHLARKTY YRLLEERRKR EEEERRQREE EEERERQRLE
     AERLAQEAEA SRRAEEEEEE ERARAKGAGV REQRCPDSTQ VEEILRLERE IQELQRKKEQ
     QELSLTQASL LRLQLLRDEE LRRLEDEACR AAQEFLASLN FDEIDECVRD IESSLSAGGQ
     PYPREEEEGE GEEEVDEGFG ADDDAFKDSP NPSEHGHSDV RTSGIRTSDD SSEEDPYMND
     TVVPTISGAA DALALPAAPG CQSGSNSGDS AYCMPENLGL MAQDSVELIP PNEDSDYDQD
     DYDEGAIVSG SSVAFSNPHS GQWSSDYRCS VGTYNSSGAY RFSSEGAQSS YEDSEDDFDR
     FDTDDELSYR RDSVYSCVTL PYFHSFLYIK GGLMNTWKRR WCVLKDETFL WFRSKQEALK
     QGWLHKKGGG SSTLSRRNWK RRWFVLRQSK LMYFDSDGEE KLKGTLDVRS AKEIIDNTGK
     ENGIDVVMPE RTYHLIAESA EDASQWFSVL SQVHGSTEQE IREMHDEQAN PQNAVGTLDV
     GLIDSVCASD NPERPNSFVI ITANRVLHCN ADTPEEMHHW ITLLQRSKGD TRVEGQEFIV
     RGWLHKEMKN STKASLKLKK RWFLLTHNSL DYYKSSERNA VKLGTLVLNS LCSVVPPDEK
     VFKETGYWNV TVYGRKHCYR LYTKLLNEAT RWSSTIQNVI DTKAPIDTPT QQLIQDIKEN
     CLNADVVEQI YKRNPILRYT HHPLHSPLLP LPYGDISLNL LQDKGYTTLQ DEAVKVFNSL
     QHLESAGDPI PITQGILQTG HDLRPLRDEL YCQLIKQTTR PAQPGGVGNL RAWHILACMS
     CTFTPSRGIL KYLKFHLKRT RELFPGTDME KYAAFTYESL KKTKTREFVP SQEEIKAIIS
     RQEMTTTVYC HGGGSCKITI NSHTTAGEVV EKLIRGLAME DSRNMFALFE HNATIDKAII
     VREKLSARYM VYGEKLSGNQ EESNKGWKFY FKLYCFLDTD NVPKDSVEFA FMFEQAHEAV
     IRGHYPAPEE TLQFLAALRL QYLLGDFNAQ ASVPEMEQVY PMSRLRARIH QSTKTFAPAA
     ERAEKKRASF LEGTLRRSFR SGSVSRQRLE EEQMLEMWVK EEIVAARTNV LEKWKKLQSM
     TQEQAMVKYM ALVKEWPGYG STLFEVESRE GGFPSELWLG VSAEAISLYK RGEPRPLEVF
     QYEHILSFGA PLPNMYKIAV EDRELLFETS QVVDVAKLMK AYISMIVKKR YSTTRSVSSQ
     GSQCSSR
//
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