ID I3JEA8_ORENI Unreviewed; 2268 AA.
AC I3JEA8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Myosin IXAa {ECO:0000313|Ensembl:ENSONIP00000007199.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000007199.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000007199.2}
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; 8128.ENSONIP00000007199; -.
DR Ensembl; ENSONIT00000007204.2; ENSONIP00000007199.2; ENSONIG00000005713.2.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000154905; -.
DR HOGENOM; CLU_000192_2_2_1; -.
DR InParanoid; I3JEA8; -.
DR TreeFam; TF319651; -.
DR Proteomes; UP000005207; Linkage group LG1.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd01385; MYSc_Myo9; 1.
DR CDD; cd04377; RhoGAP_myosin_IX; 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; IPR046990; RhoGAP_myosin_IX.
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; 4.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
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; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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:UP000005207};
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 22..122
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 158..1027
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1856..2041
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 780..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..931
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1177..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1788..1807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2053..2079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2115..2268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2085..2112
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 784..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2127..2147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2148..2174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2178..2207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2224..2250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 251..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2268 AA; 258426 MW; DC109C9EC87B7406 CRC64;
MSARDGVGGM GTLGRRQRFE NSEFTVRIYP GALAEGTIYC PISARKTTTA AEAIERVIER
LKLDRSKFYV LAEVKEFGGE EWILNPNDCP VQRMMLWPRI ALEHRPLSGG EDYRFLLREK
NLDGSIHYGG SLQMWLQVTE ERRRLMERGL LPQPESQGDH ADLCCLPELN ERTLLDNLRS
RFRQEKIYTY VGSILIVINP FKFLPIYNPK YVKMYDNHTL GDLEPHIYAV ADVAYHAMLQ
RQRNQCIVIS GESGSGKTQS TNFLIHHLTA LSQKGFASGV EQIILGAGPV LEAFGNAKTA
HNNNSSRFGK FIQVNYQESG AVRGAYVEKY LLEKSRLVYQ EHNERNYHVF YYLLAGASEE
ERKAFHLKKP EEYHYLSQMS KTSHQRQWES YCESEPDCFN VEGEDLKHDF ERLQLAMEMV
GFLPATRKQI FSLLSAILHL GNIRYKKKTY RDDSIDIVNP EVLPVVSELL QVKEEMLFEA
LTTRKTVTVG EKLIVPYKLA EAGTVRDSMA KSLYSALFDW IVFRINHALL NIKDLMETTK
ILSIGVLDIF GFEDYENNSF EQFCINFANE RLQHYFNQHI FKLEQEEYRA EGISWRNIDY
IDNTGCINLI SKKPTALFHL LDEECNFPQA TNQTLLDKFK RQHEGNSYIE FPAVMEPAFI
IRHYAGKVKY GVKDFREKNT DHMRPDIVAL LKSSKNAFIC GLIGIDPSAT FRWAVLRAYF
RAMVAFRQAG KRHKHKKHTG HDDAAPCAVL KSTDSFSFLH HPVHQRSLEI LQRCKEEKYS
VTRKSPRTPL SDLQGSNTIN EKSPRGSPGL GWNGRLGRQS RLSSSSSTAE DDGIFLNSTS
SKLLERAHDI LMRNKNYKSK PVLPKHLLNV KSLKYLNNLT LHDRITKSLL HLHKKKKPPS
ISAQFQASLN KLMETLGQSE PYFVKCIRSN AEKLPLRFND NLVLRQLRYT GMLETVHIRQ
SGYNIKYTFK DFVHHFSVLL PEGTSATREG IQQCLDQLDL QADGYQVGKT KVFLREAERQ
QLQAFLHKEV LRLIVMLQRR FRARLERKQF VRMREAAVCI QRWWRSVRSI DEEEEEDDDD
SDLSVQEGAA LCLQKHWRGY RERQRFRLWR EAALVLQRAW RFWLCRRCTA ALVIQAAWRC
HRAREAYLRL YAAVIQLQAV CKGFLTRQSL QEVVKEAGGE DAATKESPSK TQTEATTSVP
APSVTVRERA RTADEPSQRT TRAKRESRRM RELEQAQFSL KLLEVRANSG GAASPCEDRR
WSLELVLPAS PPLRSPQGTP DSQSSKGSFE LLMMDEEPPK ATEEVTDTED PFSPLPPVSP
VSEPNVDVVS TSPKPTEPYR TELSDTSQQS KDAAVSTATS AINKPLRDRR ESTRRPVVVV
ISMQKETPLS EELSNAVRPS VEVRDSTAQT ADLTPSSKKP DRPAVPAPTT VPQADQGWAP
KLTLEIAQPY AKNSAAHQHE DHNALKLRLL KATFKHAVIT SGKLQVGRAG QKKKARMART
RSDFLTRTPI LSVGGDSDEE DYDGDSLHSP RHYTLPLSKQ STTEACLRES CFSDSDMVTG
KKKLHKTMSS GDLVKEDSLR KNSQDGSSSN ILIKNNIVAS EASLIGVLFL VAGQENMSPP
CSPDLTLNQS LRDSKENREP SPKVKRRRSV KISSVAVESA QRQNDTLQIL TSIGDYRSMN
DFLVKKISDL DAEDSKKDTL VDIVFKKALK EFRLNIFNSY STALAMDDGK SIRYKDLYAL
FEQILEKIMR LEQRDWRESP VKVWGNTFKI FLDEFMIEYK PTHCTLSKPL PKPERKKRRK
KDTDNVEEHN GHIFKSTQYS IPTYCEYCSS LIWMMDRACV CKCEYARMYV CLQFGVEVSR
LTNDERTVPL VVEKLINYIE MHGLYTEGIY RKSGSTNKIK ELKLGLDTDV EHMILDDYNI
HVIASVFKQW LRDLPNPLMT FELYGEFIRV MGLQDKKELI RGVYSVIDQL SRTHLNTLER
LIFHLVRIAL EEETNRMSPN ALAIVFAPCI LRCPDTTDPL QSVQDINKTT APLLPAQRAV
MYISAYHIPS PPVSPRLQPM ADAATEESGG EEGAESLPDI PEHQRAAMQQ EERVLTEEIE
SLQKEKEELT FEMLSLEPRA SDDETLESEA SIGTADSSEN LNVDSEETIS DFSERGPLKS
DAKSPRRRVL RRQPASLDSV DIGSSYTSSS HFHPSSLDNS STGDQEAIYD ERPQFTSRGT
YNPDKGKQKL KGARHTAPRP SREGGGHGRD PSDMPQRVVV YGSNEFMV
//
