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Database: UniProt
Entry: M4ACZ9_XIPMA
LinkDB: M4ACZ9_XIPMA
Original site: M4ACZ9_XIPMA 
ID   M4ACZ9_XIPMA            Unreviewed;      2449 AA.
AC   M4ACZ9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   24-JAN-2024, entry version 75.
DE   SubName: Full=Unconventional myosin-IXa-like {ECO:0000313|Ensembl:ENSXMAP00000012343.2};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000012343.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000012343.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000012343.2};
RG   Ensembl;
RL   Submitted (JUL-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; 8083.ENSXMAP00000041425; -.
DR   Ensembl; ENSXMAT00000012359.2; ENSXMAP00000012343.2; ENSXMAG00000012266.2.
DR   Ensembl; ENSXMAT00000036846.1; ENSXMAP00000041425.1; ENSXMAG00000012266.2.
DR   eggNOG; KOG1453; Eukaryota.
DR   eggNOG; KOG4229; Eukaryota.
DR   GeneTree; ENSGT00940000154905; -.
DR   HOGENOM; CLU_000192_2_2_1; -.
DR   OMA; DAMAKCI; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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:0048675; P:axon extension; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0098529; P:neuromuscular junction development, skeletal muscle fiber; IEA:Ensembl.
DR   GO; GO:0036269; P:swimming behavior; IEA:Ensembl.
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; -; 2.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 2.
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; PF00130; C1_1; 1.
DR   Pfam; PF00612; IQ; 3.
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; 5.
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; 2.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50096; IQ; 3.
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}; 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:UP000002852};
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          30..131
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          167..1037
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1905..1954
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1969..2157
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          919..941
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1182..1254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1275..1306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1325..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1400..1745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2203..2258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2284..2449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1291..1306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1405..1419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1430..1444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1471..1485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1510..1529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1539..1590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1633..1655
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1686..1703
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1720..1738
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2203..2217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2294..2314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2322..2343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2344..2388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2428..2449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         260..267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2449 AA;  278362 MW;  8788D776EE18D339 CRC64;
     MSLQDGGCSY ASSANLATIT GSMRRRLEDQ EFTLRVYPGS LAEGTIYCPV AARKITTAAE
     AIECLIERLR LDRTKCYVLA EVKEFGGEEW ILNPGDCPVQ RMMLWPRTAL ENRSGLGSGE
     DYRFLLREKN LDGSIHYGGS LQMWLRVTEE RRRMVERGFL PQPAGNDPPS DLCALPELTE
     RALLESLRAR FRQEKIYTYV GSILIVINPF QFLPIYNPKY VKLYDNHTLG KLEPHIYAVA
     DVAYHAMLQR RKNQCIVISG ESGSGKTQST NFLIHHLTAL SQKGFASGVE QIILGAGPVL
     EAFGNAKTAH NNNSSRFGKF IQVNYQESGT VRGAYVEKYL LEKSRLVYQE HNERNYHVFY
     YLLAGASEEE RKAFHLLKPE EYHYLNQMTK RPHKLHWDNF YESELQDCFT VEGEDLKHDF
     ERLQLAMEMV GFLPSTRKQI FSLLSAILHL GNIRYKKKTY RDDSIDICNP EGLPIVSELL
     EVKEEMLLEA LTTRKTVTVG ERLIVPYKLA EANTVRDSMA KSLYSALFDW IVFRTNHALL
     NNKDLEDSSK ILSIGVLDIF GFEDYENNSF EQFCINFANE RLQHYFNQHI FKLEQEEYRA
     EGISWHNIDY SDNSGCLNLI SKKPTALFHL LDEECNFPQA SNQTLLDKFK RQHEGNSYIE
     FPAVMEPAFI IRHYAGKVKY GVKDFREKNT DHMRPDIVAL LKSSKNAFIC GLMGIDPVAT
     FRWAVLRAYF RAVVAFREAG RRHTHKNTGN DAAVPCPVVK TVDSFSFIHH PVHQRSLEIL
     QRCKDEKYSI ARKNPRTPLS ALQGTNALNE KASWDGYGVG CNGRGSRSGC VSSSGSPALE
     EEGIFLNSGS SKLLERAQGI LLRNKNCKSK PSLPKHLLDV KSLRYLSSVT LHDRITKSLL
     HLHKKKKPPS ISAQFQASLT KLMETLDQSE PYFVKCIRSN AEKLPLRFND SLVLRQLRYT
     GMLETVRIRQ SGYSIKHTFQ EFVRHFHVLL PRGTSPTKSG IREFFRRIHL PPAGYQVGHT
     MVFLREAERQ RLQTLLHQEV LRRIVMLQRR FRAVLERRHF VSMRRAARFI QRWWRSWLFS
     QSGVDSSVEE AAVVCLQSAW RGYRERRRFL QQRASAVTIQ RSWRSCRRRH CTQAAVVIQT
     AWRRVRERNR FCRARSSVTQ LQAIGRGYLA RVRFKLLREQ SERLSRRPRP DTGTDVGNLE
     DLVPSGLDVS VSADSSEEPD PTKTDRDDDS ERSRSTDEMS HKSRSKRESR RMRELEQAQF
     SLELLKVRTT SIGGSLLEDA TPDSSLAQTD DRHQRLSPQG SLASHGSFEM LSVDEMEMEG
     RPLEILRDSN HNEKPVKELR PEGPRATFYI PSEQSPANLG SPSRSVKDRK ESVSRRPVVV
     LISMQKESPV EEGELLAAHT LEGASQTGPF DSSTAPSEGV GAPTHKEQPT EVFPHAKRDV
     AGAEKPSKLP TQALRGENPE EPALCPPKVD VQISQKSSVS TVLPGKQERK TVRPAQEAPS
     PILDTKPPKA QKKSSAQTVI VNMVEKPSST VFSPPRRKLP FSKSDKDLVN QERSLSLSMH
     RDDSKSAGSR NREQVSRPGP KKKARMSRTR SDFLTRCNSE GATQSDDDDE YYIPAHSCTL
     PLSLSPSRAH PNTDCHSDSE MSHKEQKKIH KTMSSGDLGK VEILRKSSNQ DGSRMRGKMR
     FWSKTKHSEK KLSREKQTSR SEAGETHESA SPPRSPDLEV VPSRETRDTK ENKEPSPKMK
     RRRSLKISSI AVEPAQWQND SLHILTSAHD YRTMNEFLMK KIADLDSEDS KKDTMVDVVF
     KKALKEFRIN IFNSYSTALA MDDGRSIRYK DLHALFEHIL EKTMRLEQRD WSESPVKVWV
     NTFKVFLDEF MTEYKPMEGT IGRTLKRERK KSRKKETDIV EEHNGHIFKS TQYSIPTYCE
     YCSSLIWMMD RACVCKLCRY ACHRKCCSKM TTKCSKKYDP ELSSRQFGVE LSRLTSDERA
     VPQLVEKLIN YIEMHGLYTE GIYRKSGSTN KIKELRQGLD TDVSSVILDD YNIHVIASVL
     KQWLRDLPSP LMTFELYEEF LRAMGQPDKR EVIQGVYSVI DQLSRTHLST LERLIFHLVR
     ISLQEETNRM SVNALAIVFA PCILRCPDTI DPLQSVQDIS KTTACVELII NEQMSKYKAR
     LKDISSLEFA ESKAKSRLTH IRRSLKPVLI AVRFMSITRS TTPNKVRVRQ SGSHIPSPPL
     SPKAEGDGVG GAGGGGGGEE AAGETEINEQ QQQAMQQEER ILTEQIESLQ KEKEELTYEM
     LVLEPRASDD ETPESEASIG TADSSENITM EMEGATSDPS ERGTYRSRKS EAKTRRTLRR
     QPDSQDSVDS TSTASSSYQP SSSLSSIASG SPSPHYRFRS SSSGPLLTSC GLGAPLAEPE
     DGQRTGKTRL RLRLSRSSPR DSSGSHQRES DFGPGPQQLV LYSNNEFMV
//
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