ID G3MXE8_BOVIN Unreviewed; 2340 AA.
AC G3MXE8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Myosin IXA {ECO:0000313|Ensembl:ENSBTAP00000054214.2};
GN Name=MYO9A {ECO:0000313|Ensembl:ENSBTAP00000054214.2,
GN ECO:0000313|VGNC:VGNC:97290};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000054214.2, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000054214.2, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000054214.2,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000054214.2}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000054214.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR SMR; G3MXE8; -.
DR STRING; 9913.ENSBTAP00000054214; -.
DR Ensembl; ENSBTAT00000066138.2; ENSBTAP00000054214.2; ENSBTAG00000007433.5.
DR VEuPathDB; HostDB:ENSBTAG00000007433; -.
DR VGNC; VGNC:97290; MYO9A.
DR GeneTree; ENSGT00940000154905; -.
DR HOGENOM; CLU_000192_2_1_1; -.
DR InParanoid; G3MXE8; -.
DR Reactome; R-BTA-8980692; RHOA GTPase cycle.
DR Reactome; R-BTA-9013424; RHOV GTPase cycle.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000007433; Expressed in spermatid and 111 other cell types or tissues.
DR ExpressionAtlas; G3MXE8; baseline and differential.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0044295; C:axonal growth cone; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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; 3.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR046990; RhoGAP_myosin_IX.
DR PANTHER; PTHR46184:SF3; UNCONVENTIONAL MYOSIN-IXA; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 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 PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 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};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 1..750
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1846..2032
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 632..654
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 954..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2158..2183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2196..2236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2261..2320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1223..1276
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2125..2152
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1049..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2167..2183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2202..2216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2217..2236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2288..2302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2340 AA; 268123 MW; 66798DE9AC6BC4E1 CRC64;
MYFSLQGKGR LRRGNYPCPS SPAVVRLPSM SDVTEETLTS EVALETDITE QQQAAMQQEE
RAFGNAKTAH NNNSSSFWQV YSSNYQETGT VLGSYVSSTL RYLICALFQD YNGYPLRQSW
RLDCFTVEGE DLRHDFERLQ LAMEMVGFLP KTRRQIFSLL SAILHLGNIC YKKKTYRDDS
IDICNPEVLP VVSELLEVKE EMLFEALVTR KTVTVGEKLI LPYKLAEAVT VRNSMAKSLY
SALFDWIVFR INHALMNSKD LEQNTKTLSI GVLDIFGFED YENNSFEQFC INFANERLQH
YFNQHIFKLE QEEYRTEGIS WHNIDYIDNT CCINLISKKP TGLLHLLDEE SNFPQATNQT
LLDKFKHQHE ENSYIEFPAV MEPAFIIKHY AGKVKYGVKD FREKNTDHMR PDIVALLRSS
KNAFISGMIG IDPVAIFRWS VLRAFFRAMV AFREAGKRHI QRKTGHDDTA PCAVLKSMDS
ISFLQHPVHQ RSLEILQRCK EEKYNITRKN PRTPLSDLQG MNTLNEKNQH ETFDFAWNGR
TGIRQSKLSS NTSLLDKDGI FANSASSKLL ERAHGILTLN LIFPPVFQHL LEVKSLKHLT
SLTIQDRITK SLLHLHKKKK PPSISAQFQV SLSKLMETLG QAEPYFVKCI RSNAEKLPLR
FNDALVLRQL RYTGMLETVR IRQSGYSCKY SFQDFVSHFH VLLPRNIIPS KFNIQDFFRK
INLNPDNYQV GKSMVFLKEQ ERQHLQDLLH QEVLRRIVLL QRWFRVLLCR QHFLHLRQAS
IVIQQFWRNY VHQKQVRDAA VQKDALLMAS AATLLQASWR AHVQRQRYLE LRTATVVIQR
RWREHCRRRH LAAVCIQARW KGYRESKRYQ EQRNKIILLQ SLCRGFRARQ RFKSLKEQKV
KEAKLELGLA SIKPYGTLEI HGSDPSKWED CSFDSRVKAI EECKSVIESN RISHESSMDC
LNESPNKRQE RARSQSGVDL QENVIVRERP KSLEDLHQKK VSRAKRESRR MRELEQAIFS
LELLKVRSLG GVSPSEERRW STELMPEGLQ SLQGTPDSES SQGSLELLSC EESQKSKPEP
VILDERDLPF VPPEVSHSPD FDPQDYSLSA ASETNYTLTQ RGAPSDSVHL KNGAMKEKLV
CSSESITCKP QLRDPFVSNS LPTFFYIPHQ DPLKMSSQLD TSVKRSKRLE SEETLPSLTL
DISREAGKYH LPGENQVVAS LNIDSSNTVL KKLEKLNTEK EERQKQLQQQ NEKEMMKQIR
RQKDILEKER KAFKTIEKPR TGESFLIPSF HQSKQRIERP SSLLILKTPN KDEEPSMVGT
PSVTIKDSVL APKDSPSAHL PLKDRPVTLF FERKGGPGQS HTVKELSKTD GMSTQLNVAC
KHSHSRISKR EHLRPAHPCS HKSDDPFRDG ATKAIFFTPK ENMSTLNSGN PQLQKQDEPT
WKPVKLTGPG QGEVARPAHK KKARMARTRS DFLTRGTFAD GEGDTEEDDY DDIIEPLLSL
DQASHSELGP APSLGQASHS DSEMTSQRFS SVDEEAKLHK TMSQGEITKL AVRQKASDSD
IRPQRAKMRF WAKGKQGEKK TSRVKPDTHS EVSALFAGSD MIPAHRFPDE LSHNHPTPPL
SPELPGSCRK EFKENKDVKI SSVALESVHW QNDSVQIIAS ASDLKSMDEF LLKKMNDLDN
EDSKKDTLVD VVFKKALKEF RQNIFSFYSS ALAVDDGKSI RYKDLYALFE QILEKTMRLE
QRDWSESPVR VWVNTFKVFL DEYMNEFKTL EYIPTKVPKT ERKKRRKKES DLVEEHNGHI
FKATQYSIPT YCEYCSSLIW IMDRASVCKC KYERSLRNVF ECIWNQKLSS IEDRTVPLVV
EKLINYIEMH GLYTEGIYRK SGSTNKIKEL RQGLDTDAEN VNLDDYNIHV IASVFKQWLR
DLPNPLMTFE LYEEFLRAMG LQERKETIRG VYSVIDQLSR THLNTLERLI FHLVRIALQE
DTNRMSANAL AIVFAPCILR CPDTIDPLQS VQDISKTTTC VELIVVEQMN KYKARLKDIS
SLEFAENKAK TRLSLIRRSM KPVLIAVRFM SITRNSVSGK GRLRRGNYPC PSSPAVVRLP
SMSDVTEETL TSEVALETDI TEQQQAAMQQ EERVLTEQIE NLQKEKEELT FEMLVLEPRA
SDDETLESEA SIGTADSSEN LNIESEERSL ALISMKAAGK SEPSSKLRKQ LKKQQDSLDS
VDSSVSSLCS SGTASSHGTR RRFQIYSKSP FYRASSAGEA LGMEGPSGQT KSLEDKPQFI
SRGTFNPEKG KQKLKNVKNS PQKTKETPEG IVVSSRRKTV DPDCSSAQQL ALFGNNEFMV
//
