ID H3CW18_TETNG Unreviewed; 2042 AA.
AC H3CW18;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Myosin IXA {ECO:0000313|Ensembl:ENSTNIP00000012452.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000012452.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000012452.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, growth cone
CC {ECO:0000256|ARBA:ARBA00004624}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR STRING; 99883.ENSTNIP00000012452; -.
DR Ensembl; ENSTNIT00000012643.1; ENSTNIP00000012452.1; ENSTNIG00000009579.1.
DR GeneTree; ENSGT00940000154905; -.
DR HOGENOM; CLU_000192_2_2_1; -.
DR InParanoid; H3CW18; -.
DR OMA; INDYRSM; -.
DR TreeFam; TF319651; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd20883; C1_Myosin-IXa; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR046987; Myo9.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF3; UNCONVENTIONAL MYOSIN-IXA; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 1.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
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|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000007303};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 24..124
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 158..957
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1649..1698
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1713..1901
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 756..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..861
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1080..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..1985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2008..2042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1971..1985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2020..2042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2042 AA; 232512 MW; 9847BB15DD51F94A CRC64;
SAMSARDGVG GSGTLGRRQR FENSEITVRI YPGALAEGTI YCPISARKTT TAAEAIERVI
DRLQLDRTRC YVLAEVKEFG GEEWVLNPSD CPVQRMMLWP RVALEHRSLS GGEDYRFLLR
QKNLDGSISY QLQMWLQVTE ERRRMVERGL LPQPDAQGDH ADLCHLPQLN ERSLLDNLRS
RFLQEKIYTY VGSILIVINP FRFLPIYNPK YVKMYDNRWG KLEPHIYAVA DVAYHTMLQR
ERNQCIVISG ESGSGKTQST NFLIHHLTAL SQKGFASGVE QIILGAGPVL EAFGNAKTAH
NNNSSRFGKF IQVNYQESGT VRGAYVEKYL LEKSRLVYQE HNERNYHVFY YLLAGASEEE
RKAFHLKKPE EYHYLSQDCF AVEGEDLKHD FERLQLAMEM VGFLPATRKQ IFSLLSAILH
LGNIRYKRKT YRDDSIDICN PEELPVVSEL LEVKEEMLFE ALTTRKTVTV GERLIVPYKL
SEAGTVRDSM AKSLYSALFD WIVFRINHAL LNVKDLVETT KILSIGVLDI FGFEDYENNS
FEQFCINFAN ERLQHYFNQH IFKLEQEEYR AEGISWHNID YIDNTGCIHL ISKKPTALFH
LLDEECNFPQ ATNQTLLDKF KRQHEGNSYI EFPAVMEPAF IIRHYAGKVK YGVKDFREKN
TDHMRPDIVA LLKSSKNAFI CGLMGIDPSA MFRWAVLRAY FRALVAFREA GKRHTQKKKT
AKGMMTLLPV QFPKGSNTIN EKSPRQLHRR RRRHLHQLGQ QQTPGESARH PDTTLKHPSA
LKRNKNYKSK PVLPKHLVNV KSLKYLSNLT LPDRITKSLL HLHKKKKPPS ISAQFQASLN
KLMETLGQSE PYFVKCIRSN AEKLPLRFND NLVLRQLRYT GMLETVRIRQ SGYYIKYSYK
DFVHHFGVLL PEGTAATREE IQLCLDQLDL DSEGYQVGRT MVFLREAARQ RVQALLHREV
LRLIVALQRR FRAQLERRHF VRMRGAAVRI QRAWRSALRR RCSAALVIQA AWRRHRARDA
YLHLCTTVVQ LQALSRGYLS RQTIKNACEM ASKHSEISFK ELLNFPSVFA GCGNGPDWDG
ALRNDPAKTA SGPSGSGGPL LQNGQVSVSE GLPEKIMGLD LSTWEGRSSQ PPERSLSSQE
DERVPAEKTT RAKRENRRMR ELEQAQFSLE LLKVRATGSG GTPSPSEERR WSLELVPSSP
PFRSPQGTPD SQSSKGSFEL LDLEEEPPKA VEEALDSEDL CSPPPEPEVE APPPSQAPVH
PPRAGGPDAG QAQMDPEASS AATHPPKIEN YLPTFYVPKS GGGTDVSRRP AEEPRQNAGA
AVFAGPAVTR PLRERRESAR RPVVVVISMQ KETAVSQVEV PRTGESTPSP QQRKPAPAPA
GPVPTPTSTN LASQVVLEKL ERLNEEKEAD HRRQSGGQTG EHLLLPKRTE SHLQSESWRT
FLRVAESRPS IFIPPFSSSS FQNDAVARDA PAAVSPPTSK ASKASKGREV RDAFFSVVQR
QEWREKGPLN LTNPPTLNIL CPFQIRELEQ EESKTQPMVD LLFKKALKEF PLNIFNFYYN
ALLMEQRKSI PYKDLYPLFE KILEKTMRKE QRNWRESPVN VWVKIFKVLL DEFMTEYKPL
DSTLGKQVAK PEVKKRRKKD SDIVEEHNGH IFKSTQYSIP TYCEFCSSLI WMMDRACVCK
LCRYACHRKC CQKTTNKCSK KFDPELSSRQ FGVEVSRLTT DERAVPLVVE KLINYIEMHG
LYAEGIYRKS GSANKIRELK QGLDTDVDST NLDDYNIHVI GSVFKQWLRD LPNPLLTFEL
YEEFIRAMGL QDKKEMIRGV YSVIDQLSRT HLNTLERLVF HLVRIALQEE TNRMSANALA
IVFAPCILRC PDSIDPLQSV QDIGKTTACV ELIICEQMNK YRVRLKDISS LEFAENKAKC
RLTLIRRSMG KGHLQRVRYN STSPPVSPRL PSVADVVLEE SGDEDGANSL GDVSEHQQAA
MQQEERVLTE QIESLQKEKE ELTFEMLTLE PRASDDETLE SEASIGTADS SENLNLDSEG
TA
//
