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Database: UniProt
Entry: W5L610_ASTMX
LinkDB: W5L610_ASTMX
Original site: W5L610_ASTMX 
ID   W5L610_ASTMX            Unreviewed;      2396 AA.
AC   W5L610;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Myosin IXAb {ECO:0000313|Ensembl:ENSAMXP00000015272.2};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000015272.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000015272.2}
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|PROSITE-ProRule:PRU00782}.
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DR   STRING; 7994.ENSAMXP00000015272; -.
DR   Ensembl; ENSAMXT00000015272.2; ENSAMXP00000015272.2; ENSAMXG00000014841.2.
DR   eggNOG; KOG1453; Eukaryota.
DR   eggNOG; KOG4229; Eukaryota.
DR   GeneTree; ENSGT00940000154905; -.
DR   HOGENOM; CLU_000192_2_2_1; -.
DR   InParanoid; W5L610; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000014841; Expressed in brain and 14 other cell types or tissues.
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: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; cd01385; MYSc_Myo9; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 3.
DR   Gene3D; 1.20.58.530; -; 2.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 6.20.240.20; -; 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; 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; 2.
DR   Pfam; PF00063; Myosin_head; 2.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 4.
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; 3.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 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:ARBA00022771};
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:UP000018467};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          16..114
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          149..1018
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1933..2121
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          780..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..922
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1163..1184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1201..1246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1323..1385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1463..1482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1539..1569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1598..1717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2145..2199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2226..2384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..814
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1163..1180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1544..1568
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1644..1660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1697..1717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2185..2199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2239..2264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2265..2286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2290..2320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2349..2377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         242..249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2396 AA;  273886 MW;  C71708FD714A6C0C CRC64;
     IMSCHDAGGR RRFEDTEFTL HIYPGTLSEG TIYCPVSARK VTSAAEVIEQ VIERLRLDRA
     RLYVLAEVKE FGGEEWILNP GDCPVQRMML WPRMALENRI SGEDYRFLLR EKNVDGSIHY
     GSLQMWLRVT EERRRLVERG LLPQPPAGQL ASDLCALPDL NERTLLENLR GRFRQEKIYT
     YVGGILIVVN PFKFLPIYNP KYVKMYDNHQ LGKLEPHIYA VADVAYHAML QRRRNQCIVI
     SGESGSGKTQ STNFLIHHLT ALSQKGFASG VEQIILGAGP VLEAFGNAKT AHNNNSSRFG
     KFIQVNYQES GTVRGAYVEK YLLEKSRLVY QEHNERNYHV FYYLLAGASE EERKAFHLLR
     PEEYHYLNQM TKKAHRLHWE NYCESELDCF SVEGEDLKHD FERLQLAMEM VGFLPATRKQ
     ILSLLSAILL LGNIQYKKKT YRDDSIDICN PEVLPTISEL LEVKEEMLFE ALTTRKTVTV
     GERLIVPYKL AEAGTVRDSM AKSLYGALFD WIVFRTNHAL LNNKDLEDSA KILSIGVLDI
     FGFEDYENNS FEQFCINFAN ERLQHYFNQH IFKLEQEEYR AEGISWHMID YIDNTSCINL
     ISKKPTALLH LLDEECNFPQ ASNQTLLDKF KRQHDGNSYI EFPAVMEPAF IIHHYAGKVK
     YSVKDFREKN TDHMRPDIVA LLKSSKSAFI CGLMGIDPVA TFRWAVLRAY FRAVVAFRGA
     GKWHREKKSG SDSAVQCTVI KSVDSFSFLH HPVHQRSLEI LQRCKDDKYN SCITRRNPRS
     PLSDLQGTNT LNEKSTRDGF SGCNGRSSRP GRLATTGSAH EEDGIFVNAM SNRLLERAQG
     ILMRNKNYKA KPSLPKHLLD VKSLKHLSSL TLHDRITKSL LHLHKKKKPP SISAQFQASL
     NKLMETLGQS EPYFVKCIRS NAEKLPLRFN DALVLRQLRY TGMLETVRIR QSGYSVKYTF
     QDFAHHFHVL LPDGTGASQA GIREFLKRAD LDPDGYQVGK TMVFLREVQR QRLQDLLHQE
     VLRRIVMLQR KFRALLERKL FINQRQAALV IQHWWRKCML CHSRDRADAS ELRHGAAVCL
     QAAWRGYKER KLYLLQRDAV LLLQRGWRRC MQRRWRAAGL IQATWRAHRQ RQRYLQLCRA
     IITLQAACRG HQARQRCRCL REEQKTHSEN NKEQSTTPED LQDFQKRTSA QITDLHLEEL
     HQSSETSQEE HRMEFSESLS SEHCKTLDDS TLKSRAKRES RRKRELEQAT FSLELLKVRS
     NNVPLSDQPV PLKTAPPYSS PQSSFDSHGS FELLIVDDAK LEELDHHHPD LVPIDQSISV
     EDNKREHKTV SEVKTTPVKR LEPSSPIQPA GQRTSKALFY ISDEGSSPVS PEPQTPSRSK
     AARDRKESVV VLISMQKESP VDPSSLEALE RLEQEAECKP NIAQQESTCS SIRFGQAPLN
     QPTVQPSQAP LDLRLNLELS SGAATLPSGS ATREASSEAR KEEGMGLMQA QKKAVMHSIS
     ISMKEKATNL AFSPKRSRLT FSKSDKDLAN QERSLALQRE RTSGFRSLKS REVARGGRPK
     KARMARTRSD FLTRACSTEA DSDDEDDDDY EYRRVLSHTL PLPEPPGSPT TDQAFHSDSE
     MPSQKEQKRL QKTMSSGDLG KVDSLRKSSS HTDSSRVRGK MRFWGKGKHS EKKMSTRGRS
     AEGDLTKAGN DSPPRSPERS GGRDHGRDSK ENREPEVKMM MMTMRRRRSL KISSITQEPT
     PWQSDSLVIL TCTADYRSMN DFLMKKINDL ETEDSKKDSP VDVVFKKALK EFRLNIFNSY
     STALAMDDGR SIRYKDLYAL FEHILEKSMR LEQRDWSESP VKVWVNTFKV FLDEFMTEYK
     PMDNTIGRAP KPERKKRRKK ETDIVEEHMG HIFKSTQYSI PTYCEYCSSL IWMMDRACVC
     KRELLHIGMQ FGVELSRLTS DERAVPLVVE KLINYIEMHG LYTEGIYRKS GSTNKIKELK
     LGLDTDANTV NLDDYNIHVI ASVLKQWLRD LPNPLMTFEL YDEFLRATGL QDKREVVKGV
     YTVIDQLSRT HLGTLERLIF HLVRISLQEE TNRMSANALA IVFAPCILRC PDSTDPLQSV
     QDIGKTTACV EMIICQQMNK YKARLKDINT LEFAESKAKN RLTHIRRSMG KARIRRSSHH
     TPSPPMSPRS PVVAEPEVPE DEGVESSLSD QQQAAMQQEE TVLTQQIESL QKEKEELTYE
     MLALEPRASD DEMLESEASI GTADSSENLM AEQEGATSET WEKNCSTLRS RKTDSKSRRA
     LRRQPESLDS VDSAVASLSS TSSTPHYRFR SSSSGPLFSS ASGLDHPHLA EQEASEQPVL
     NTRCASSSEK TRPRTRGNRS CPPKPRESGE GGGRRRDTEF GSVQPLVLYG SNEFMV
//
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