ID A0A3Q7UXR1_VULVU Unreviewed; 2647 AA.
AC A0A3Q7UXR1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Unconventional myosin-IXa isoform X1 {ECO:0000313|RefSeq:XP_025872440.1};
GN Name=MYO9A {ECO:0000313|RefSeq:XP_025872440.1};
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_025872440.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025872440.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025872440.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025872440.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_025872440.1; XM_026016655.1.
DR KEGG; vvp:112933463; -.
DR OrthoDB; 1094820at2759; -.
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 2080..2129
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 2144..2332
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 1776..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1896..1918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2380..2424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2458..2479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2500..2542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2575..2634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1495..1534
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2425..2452
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 1781..1799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1800..1814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1823..1837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1899..1913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2508..2523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2524..2542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2595..2609
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 2647 AA; 303773 MW; B3F58D21A442DD80 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 GQGEQVARPA HKKKARMART
RSDFLTRGTF ADGEGDTEED DYDDIIEPLL SLDQASHSEL GPAPSLGQAS HSDSEMTSQR
FSSVDEEAKL HKTMSQGEIT KLAVRQKDSD SDIRPQRAKM RFWAKGKQGE KKTTRVKAAT
QSEVSAFFAG SDMIPAHQFP DELVQYHLTP PLSPELPGSC RKEFKENKEP SPKAKRKRSV
KISNVALESV HWQNDSVQII ASVSDLKSMD EFLLKKMNDL DNEDSKKDTL VDVVFKKALK
EFRQNIFSFY SSALAIDDGK SIRYKDLYAL FEQILEKTMR LEQRDWSESP VRVWVNTFKV
FLDEYMNEFK TLDCIPTKVP KTERKKRRKK ETDLVEEHNG HIFKATQYSI PTYCEYCSSL
IWIMDRASVC KLCKYACHKK CCLKTTAKCS KKYDPELSSR QFGVELSRLT SEERTVPLVV
EKLINYIEMH GLYTEGIYRK SGSTNKIKEL RQGLDTDAES VNLDDYNIHV IASVFKQWLR
DLPNPLMTFE LYEEFLRAMG LQERKETIRG VYSVIDQLSR THLNTLERLI FHLVRIALQE
ETNRMSANAL AIVFAPCILR CPDTIDPLQS VQDISKTTTC VELIVVEQMN KYKARLKDIS
SLEFAENKAK TRLSLIRRSM KPVLIAVRFM SITRNSVSGK GRLRRGNYPS PSSPVVVRLP
SVSDVPEETL TSEAAGETDI TEQQQAAMQQ EERVLTEQIE NLQKEKEELT FEMLVLEPRA
SDDETLESEA SIGTADSSEN LNIESEGVIS EKSERSLALS SLKAAGKSEH SSKLRKQLKK
QQDSLDSVDS SVSTLCSSNT ASSHGTRKRF QIYSKSPFYR AASAGEALGM EGPLGQTKSL
EDRPQFISRG TFNPEKGKQK LKNVKNSPQK TKETPEGTVV SGRRKTVDAD SSSTQQLALF
GNNEFMV
//
