ID A0A3P9AS45_9CICH Unreviewed; 2048 AA.
AC A0A3P9AS45;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Myosin X {ECO:0000313|Ensembl:ENSMZEP00005000438.1};
GN Name=MYO10 {ECO:0000313|Ensembl:ENSMZEP00005000438.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005000438.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005000438.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005000438.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR Ensembl; ENSMZET00005000499.1; ENSMZEP00005000438.1; ENSMZEG00005000207.1.
DR GeneTree; ENSGT00940000155469; -.
DR Proteomes; UP000265160; LG18.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; cd14873; MYSc_Myo10; 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; 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 PANTHER; PTHR46049; AGAP003327-PA; 1.
DR PANTHER; PTHR46049:SF2; UNCONVENTIONAL MYOSIN-X; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 1.
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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000265160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 63..739
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1194..1292
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1374..1478
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1516..1674
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 1679..2031
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 619..641
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 947..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 809..921
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 947..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2048 AA; 235435 MW; 8CC39F1C7AA884C2 CRC64;
FSSFFPTGDR VWLREDEQFL PSTVSSCSGG VVVFATDYGQ VYTYKQNTLT RQKVQPMHRS
SIRGVEDMAS LEDLHEGAIM HNLYLRYKQK YIYTYIGSIL AAVNPYQPLP GLYDRPAVEM
YSQHHLGEIS PHIFAIANEC YRSLWKRLQN QCVLISGESG AGKTESTKLI LKFLSAMSQH
SLEVSSRDKT SHVEEALLES SPIMEAFGNA KTVYNNNSSR FGKFVQLHVS QKGNIQGGKI
VDYLLEKNRV VRQNPGERNY HIFYAILAGT NNQQREAFGL THPDSYHYLR QSSCQDDKTI
NDKGTFQDVL NAMRTMQFTE ENINEILRLL AGILHTGNIE FVTAGGAQIS SKSALSWTSE
LLGLNSDQVA EVLTHRSMIL RGEEISTPLT VEQAVDSRDS MAMALYSQCF NWIIRKLNTR
IKGKEDFKSV SILDIFGFEN FEVNRFEQFN INYANEKLQE YFNKHIFSLE QLEYNKEGLV
WVDIDWMDNG ECLDLIEKKL GLLALMNEES HFPKATDDTL LEKLHSQHSK NPFYVKPRVA
VHYFGVKHYA GEVVYDVRGM LEKNRDTFRD DILNMLRESR LDFVYDLFEH VLSRNKQDTL
KSSIKHRRPT VSTQFKDSLH SLMATLSTSN PYFIRCIKPN THKMPDHFDQ TVVLNQLRYS
GMLETVKIRR TGFPVRRTIQ DFCSRYKVLM RGLLNSEDPR GCCVQLLCQY DSSSAEWQLG
KTKVFLRESL EHRLEKQREV EVLKAAMIIQ AYVTGYMARK QYKKLLRCIV VIQKNYRAFY
WRRKFLLLRW AALTFQKCLR GQLARQTCSR MLEERRKKEE EERRRWMEEM ERERQRLEAE
RLTREELESA ETFVEASAEE EEAIRPHEAS QVEEILRLER EIQVLQRQKE RQELSLTEAS
LNRLQQLRDQ ELRRLEDEAC KAAQQFLDSL NFDEIDECVR NIESSLGVGE EDEKKEDDQR
RGNEEEEVDE GFGADDDAFK DSPNPSEHGH SDGQRTSGIR TSDDSSEEDP YANDAVIPSL
PPTTVLHHSL PAMPSACHSA SSSGDSAYCH PQASSEAQSD ELVELIPPDE DSDYDQDDYD
EGAIVSSGSM AFSNPRSGQW SPDYRGSVGT YNSSGAYRFS SEGAQSSFED SEDDFERFDT
DDELSYRRDS VYSCVTLPYF HSFLYIKGGL MNTWKRRWCV LKDETFLWFR TKQEALKQGW
LHKKGGGSST LSRRNWKRRW FVLRQSKLMY FENDGEEKMK GVLDMHNAKE IIDNTGKENG
INIVMPERTY HLIAESAEDA SQWFSVLSQV HGSTEQEIRE MHDEQANPQN AVGTLDVGMI
DSVCASDNPE RPNSFVMITA NRVLHCNADT PEEMHHWITL LQRSKGDTRV DGQEFIIRGW
LHKEMKNSTK ASLKLKKRWF LLTHNSLDYY KSSERNALKL GTLVLNSLCS VVQPDEKVFK
ETGYWNVIVY GRKHSYRLYC KLLTEATRWA NSVQNVIDTK APIDTPTQQL IQDIKENCLN
LEVVEQIYKR NPILRYSHHP LHSPLLPLPY GDIHLTSDRS YTTLQDEALK VFSSLQHLEG
VADPVPIIQG ILQTGQELKP LRDELYCQLI KQTTRPPQPG SPGNLCNWKI LACMSCTFVP
TRSILRYLKF HLKRTHELFP GSEMDRYAAF AADSLRKTRA RENVPSQEEI RCIVARQDMS
TTVHCHGGGS CKITINSHTT AGEVVEKLIR GLAMEDSRNM FALFEHNDTT EKAIESRTVV
ADVLAKFEKL SASPDEGSTG WKFYFKLYCF LDTDNVPKDS VEFAFMFEQA HEAVIRGQYP
APEETLQFLA ALRLQYLLGD HNSQSTIPEM SQVFPMSRLR ARVQNSAKTF APGTGSVADR
SGTAERKRSS FLEGTLRRSF RSSSLSRQKL EEENSLEAWM REEAAAVRTS VMDKWKKLQG
MNQEQAMVKY MALVKEWQGY GSTLFNVECR DGMFPSELWL GVSREAISVY KRGEPWPLEV
FPYEQILSFG APLSNTYKIT VEGRELVFET QMVMDIAKLM KAYISMIVKK RYSNCQSVSS
HGSHCSTW
//