ID A0A3Q7UXZ8_VULVU Unreviewed; 2646 AA.
AC A0A3Q7UXZ8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Unconventional myosin-IXa isoform X2 {ECO:0000313|RefSeq:XP_025872510.1};
GN Name=MYO9A {ECO:0000313|RefSeq:XP_025872510.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025872510.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025872510.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025872510.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025872510.1};
RG RefSeq;
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 RefSeq; XP_025872510.1; XM_026016725.1.
DR STRING; 9627.ENSVVUP00000024451; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd20883; C1_Myosin-IXa; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR CDD; cd17216; RA_Myosin-IXa; 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; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR028558; RA_Myosin-IXa.
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; PF00130; C1_1; 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; 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; 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}; Coiled coil {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:UP000286640};
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 14..112
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 146..1016
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 2079..2128
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 2143..2331
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 898..920
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1220..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1651..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1775..1812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1895..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2379..2421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2457..2478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2499..2541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2574..2633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1495..1534
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2424..2451
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1227..1244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1780..1798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1898..1912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2507..2522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2523..2541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2594..2608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2646 AA; 303645 MW; CA501B5E4CBDD84C CRC64;
MNINDGGRRR FEDNEHTLRI YPGTISEGTI YCPIPARKNS TAAEVIDSLI NRLHLDKTKC
YVLAEVKEFG GEEWILNPTD CPVQRMMLWP RMALENRLSG EDYRFLLREK NLDGSIHYGS
LQSWLRVTEE RRRMMERGFL PQPQQKDFDD LCSLPDLNEK TLLENLRNRF KHEKIYTYVG
SILIVINPFK FLPIYNPKYV KMYDNHQLGK LEPHIYAVAD VAYHAMLQRK KNQCIVISGE
SGSGKTQSTN FLIHHLTALS QKGFASGVEQ IILGAGPVLE AFGNAKTAHN NNSSRFGKFI
QVNYQETGTV LGAYVEKYLL EKSRLVYQEH NERNYHVFYY LLAGASEEER LAFHLKQPEE
YHYLNQITKK PLRQSWDDYC YDSEPDCFSV EGEDLRHDFE RLQLAMEMVG FLPKTRRQIF
SLLSAILHLG NICYKKKTYR DDSIDICNPE VLPIVSELLE VKEEMLFEAL VTRKTVTVGE
KLILPYKLAE AVTVRNSMAK SLYSALFDWI VFRINHALLN SKDLEQNTKT LSIGVLDIFG
FEDYENNSFE QFCINFANER LQHYFNQHIF KLEQEEYRTE GISWHNIDYI DNTCCINLIS
KKPTGLLHLL DEESNFPQAT NQTLLDKFKH QHEENSYIEF PAVMEPAFII KHYAGKVKYG
VKDFREKNTD HMRPDIVALL RSSKSAFISG MIGIDPVAVF RWAVLRAFFR AVIAFREAGK
RHIQRKTGHD DTAPCAILKS MDSFSFLQHP VHQRSLEILQ RCKEEKYSIA RKNPRTPLSD
LQGMNTLNEK NQQDTFDIGW NGRTGIRQSR LSSGTSLLDK DGIFANSASS KLLERAHGIL
MRNKNFKSKP GLPKHLLEVN SLKHLTRLTL QDRITKSLLH LHKKKKPPSI SAQFQASLSK
LMETLGQAEP YFVKCIRSNA EKLPLRFNDA LVLRQLRYTG MLETVRIRQS GYSCKYSFQD
FVSHFHVLLP RNIIPSKFNI QDFFRKISLN SDNYQVGKSM VFLKEQERQH LQDLLHQEVL
RRIILLQRWF RVLLCRQHFL HLRQASIIIQ RFWRNYLNQK QVRNVAVQKD ALVMTSAATL
LQASWRAHLE RQRYLELRTA AIIIQQRWKE HYRRRHMAAV CIQARWKGYR ESKRYQEQRN
KIIFLQSVCR GFRARQRFKV LKEQRLKETK LELGLANTEP YGALEIQGSD PSKWEDCSFD
NRVKAIEECK SVIESNRISQ ESSTDCLKES PNKRQERARS QSGVDLQEEV IVRERPKSLE
DLHQKKVGRA KRESRRMREL EQAIFSLELL KVRSLGGVSP SEERRWSAEL TEGLQSLQGT
PDSESSQGSL ELLSCEESQK SKLESIILDE GDLQFLSPKI PSSPKFDSQD NALSASSETN
YTLIEKGTPS DSVHLKNGTM KEKLVCSSES ITCKPQLRDP FISNSLPTFF YIPQQDPLKT
SSQPDTSIQR NKLLEGKETL SSLTLDINRE ARKYHFSGEN QVVTSLNTDS SNTVLKKLEK
LNIEKEERQK QLQQQNEKEM MEQIRKQTDI LEKERKAFKT IEKPRTEESL LAPSFHPSKQ
RVERSSSLLI LNTPNKEEPS VLGPPSVTVK DAALLSKDSP PAHLSQKDRP VTLFFERKGG
PYQSATNKEF SKTDRMCTQL NVACKLSNNR ISKREHHRPT QSYGHKSDDP SRDGTTSVIF
FTPKDNMNIS LANKEALNSG NPQLRKQDEP TWKPVKLTGL GQGEVARPAH KKKARMARTR
SDFLTRGTFA DGEGDTEEDD YDDIIEPLLS LDQASHSELG PAPSLGQASH SDSEMTSQRF
SSVDEEAKLH KTMSQGEITK LAVRQKDSDS DIRPQRAKMR FWAKGKQGEK KTTRVKAATQ
SEVSAFFAGS DMIPAHQFPD ELVQYHLTPP LSPELPGSCR KEFKENKEPS PKAKRKRSVK
ISNVALESVH WQNDSVQIIA SVSDLKSMDE FLLKKMNDLD NEDSKKDTLV DVVFKKALKE
FRQNIFSFYS SALAIDDGKS IRYKDLYALF EQILEKTMRL EQRDWSESPV RVWVNTFKVF
LDEYMNEFKT LDCIPTKVPK TERKKRRKKE TDLVEEHNGH IFKATQYSIP TYCEYCSSLI
WIMDRASVCK LCKYACHKKC CLKTTAKCSK KYDPELSSRQ FGVELSRLTS EERTVPLVVE
KLINYIEMHG LYTEGIYRKS GSTNKIKELR QGLDTDAESV NLDDYNIHVI ASVFKQWLRD
LPNPLMTFEL YEEFLRAMGL QERKETIRGV YSVIDQLSRT HLNTLERLIF HLVRIALQEE
TNRMSANALA IVFAPCILRC PDTIDPLQSV QDISKTTTCV ELIVVEQMNK YKARLKDISS
LEFAENKAKT RLSLIRRSMK PVLIAVRFMS ITRNSVSGKG RLRRGNYPSP SSPVVVRLPS
VSDVPEETLT SEAAGETDIT EQQQAAMQQE ERVLTEQIEN LQKEKEELTF EMLVLEPRAS
DDETLESEAS IGTADSSENL NIESEGVISE KSERSLALSS LKAAGKSEHS SKLRKQLKKQ
QDSLDSVDSS VSTLCSSNTA SSHGTRKRFQ IYSKSPFYRA ASAGEALGME GPLGQTKSLE
DRPQFISRGT FNPEKGKQKL KNVKNSPQKT KETPEGTVVS GRRKTVDADS SSTQQLALFG
NNEFMV
//