ID A0A3P9AKM9_ESOLU Unreviewed; 2341 AA.
AC A0A3P9AKM9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Unconventional myosin-IXa {ECO:0000313|Ensembl:ENSELUP00000041327.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000041327.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000041327.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000041327.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSELUT00000034405.2; ENSELUP00000041327.2; ENSELUG00000022255.2.
DR GeneTree; ENSGT00940000154905; -.
DR Proteomes; UP000265140; LG02.
DR Bgee; ENSELUG00000022255; Expressed in camera-type eye 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: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; -; 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; 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; 2.
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; 6.
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; 4.
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};
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: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:UP000265140};
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 7..108
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 145..1012
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1789..1838
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1853..2041
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 767..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..916
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1151..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2151..2245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2287..2328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1465..1518
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2120..2147
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 802..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2162..2181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2217..2245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2297..2322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 238..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2341 AA; 267571 MW; 597BE84ACDA24658 CRC64;
LNVNLDSEFT LRIYPGALAE GTIYCPVSAR KSTTAAEVIE RCLERLRLDR ERCYVLAEVK
EFGGEEWILN PTDCPVQRMM LWPRGALEQR SGGGGGEDYR FLLRQKNLDG SIHYGGSLQM
WLRVTEERRL MMERGLLPPR EEARGDYADL CRLPELTERS LLDNLRSRFR QERIYTYVGS
ILVVINPFQF LPIYNPKYVK MYDNHALGEL EPHVYAVADV AYHAMLQRRR NQCIVISGES
GSGKTQSTNF LIHHLTALSQ KGFASGVEQI ILGAGPVLEA FGNAKTAHNN NSSRFGKFIQ
VNYQESGTVR GAYVEKYLLE KSRLVYQEHN ERNYHVFYYL LAGASDEERS VFHLKKPEEY
HYLNQMTKKV LRPNWENYYE SEPDCFTVEG EDLKHDFERL QLAMEMVGFL PATRKQIFSL
LSAILHLGNI RYKKKTYRDD SIDICNPEVL PVVSELLEVK EEMLFEALTT RKTVTVGERL
IVPYKLAEAG TVRDSMAKSL YSALFDWIVF RINHALLNNR DLEESAKIFS IGVLDIFGFE
DYENNSFEQF CINFANERLQ HYFNQHIFKL EQEEYRAEGI SWHNIDYIDN TGCINLISKK
PTALLHLLDE ECNFPQATNQ TLLDKFKRQH EGNNYIEFPA VMEPAFIICH YAGKVKYGVK
DFREKNTDHM RPDIVALLKS SKNAFICGLM GIDPPATFRW AVLRAYFRAT VAFREAGRRL
ARRKSGHADA APCAGFKSVD SFSFLHHPVH QRSLEILQRC KEEKYSVTRR SPRMPLSDLQ
GSNMLNDKPP GEGVGWNGRA GRQGRLSSSG SNTDEDGGIF VNSTSSKLLE RAHGILMRNK
NFKLKPSLPK HLLDVKSLKY LSKLTLHDRI TKSLLHLHKK KKPPSISAQF QASLNKLMET
LGQSEPYFVK CIRSNAEKQP LRFNDSLVLR QLRYTGMLET VRIRQSGYSI KYTFQDFVRL
FRVLLPEGTR PVQEDIGQYL RKVELVPDGY QVGKTMVFLR EVERQRLQAL LHKEVLDRIV
TLQRRFRALL ERKHFLRMRL AATTIQQWWR AYGSKQEDEH TPRQEQAALL LQTAWRRYRE
RRRFGLWRRA ALLLQREWRA WLRRREQEAA ARAIQTAWRR HAAREAYLRL RGATVMLQAL
VRGYLARQSL KDKEQREKKN QPTQKLQNGQ RSPSPDPQEQ AARIMGLDLS TWEDRSYNER
ETALRRLNSQ EERIKEGGGG GGEIGGGEMR ATESQIRTHS PVLSASTTGV VVRERTRTLD
EPGQRTTRAK RESRRMRELE QAKFSLELLK VRSTGGGGAS PPSEERRWSA ELAHATTPPP
RSPQGPSTPD SQSSRGSFEL LSVDDEIPRE RPPLADVEEL GSSVASEAQV VLESTPEVFP
ISLMSKEPPS DSQSKAKSQA KPEKAGPSAH PHKIENCLPT FYVPSTDSSL VITRLLPPPA
AVLMDPTPVT SVIPAPGPTP VPAANQFVLE KLERLNEEKE ERQRHQQQQK EREMMEQIRQ
QKEVLERQRR HFAQYEKELF EKQRGKALVR IQQSRQVGAA QDESGTPAAS MRFWGKTKQG
EKKLSREKLI CGGDSMDGDY GDTGPLLGEA GQEYMSPPRS PDLTLEHGAK EFKENKEPSP
KVKRRRSVKI SNVALEPAQW GNDALQILTC ANDYRSMNDF LMKKINDLEA EDGGKKDTMV
DVVFKKALKE FRLNIFNSYS TALAMDDGKS IRYKDLYALF EQILEKTMRL EQRDWSESPV
KVWVNTFKIF LDEFMTEYKP MDNTISKVPK PERKKRRKKD ADIVEEHNGH IFKATQYSIP
TYCEYCSSLI WMMDKACVCK LCRYACHRKC CLRMTTKCSK KYNPELSSRQ FGVEVSRLTN
EERTVPLVVE KLINYIEMHG LYTEGIYRKS GSTNKIKELK QGLDTDVNSM NLDDYNIHVI
ASVFKQWLRD LPNPLMTFEL YEEFLRAMCM QDKKEVIRGV YSIIDQLSRT HLNTLERLFF
HLVRIAGQED TNRMSANALA IVFAPCILRC PDTIDPLQSV QDIGKTTACV ELIIVEQMNK
YKARLKDINS LEFAENKAKC RLTLIRRSMG KGHVRRFSYH HTPSPPVSPR LPLAADVATC
EGGVEEALAG LEPEVPEHQQ VAMQQEERVL TEQIESLQKE KEELTFEMLT LEPRASDDET
LDSEASIGSS ENLNVDSEGA TSDFSERCGP VPSAATRPKK SEGKSYRRHN LRRQADSLDS
VDSGSTISSH SSSAHLHPPT SSAVTARRFK SPALVTPGFP GTQPPRCDSV DCASAAELEG
LFEERSQFTS RGTFNPEKGK QKLKGSKIAP LRHSRDSAGH SRDPPDLSQQ LVLYGNNEFM
V
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