GenomeNet

Database: UniProt
Entry: F6SBJ8_MACMU
LinkDB: F6SBJ8_MACMU
Original site: F6SBJ8_MACMU 
ID   F6SBJ8_MACMU            Unreviewed;      2566 AA.
AC   F6SBJ8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Myosin IXA {ECO:0000313|Ensembl:ENSMMUP00000025335.4};
GN   Name=MYO9A {ECO:0000313|Ensembl:ENSMMUP00000025335.4,
GN   ECO:0000313|VGNC:VGNC:75120};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000025335.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000025335.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000025335.4};
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|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   SMR; F6SBJ8; -.
DR   PaxDb; 9544-ENSMMUP00000025335; -.
DR   Ensembl; ENSMMUT00000027079.4; ENSMMUP00000025335.4; ENSMMUG00000019278.4.
DR   VEuPathDB; HostDB:ENSMMUG00000019278; -.
DR   VGNC; VGNC:75120; MYO9A.
DR   eggNOG; KOG1453; Eukaryota.
DR   eggNOG; KOG4229; Eukaryota.
DR   GeneTree; ENSGT00940000154905; -.
DR   HOGENOM; CLU_000192_2_1_1; -.
DR   TreeFam; TF316834; -.
DR   Proteomes; UP000006718; Chromosome 7.
DR   Bgee; ENSMMUG00000019278; Expressed in spermatocyte and 22 other cell types or tissues.
DR   ExpressionAtlas; F6SBJ8; baseline.
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   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProt.
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:UP000006718};
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          1999..2048
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          2063..2251
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..1275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1297..1380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1801..1836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2377..2442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2507..2549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1487..1526
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2344..2371
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1248..1275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1319..1342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1362..1380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1817..1831
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2386..2406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2413..2427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2428..2442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2514..2528
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   2566 AA;  295087 MW;  71085328A29FD182 CRC64;
     MNINDGGRRR FEDNEHTLRI YPGTISEGTI YCPIPARKNS TAAEVIESLI NKLHLDKTKC
     YVLAEVKEFG GEEWILNPTD CPVQRMMLWP RMALENRLSG EDYRFLLREK NLDGSIHYGS
     LQSWLRVTEE RRRMMERGFL PQPQQKDFDD LCSLPDLNEK TLLENLRNRF KHEKIYTYVG
     SILIVINPFK FLPIYNPKYV KMYDNHQLGK LEPHIYAVAD VAYHAMLQRK KNQCIVISGE
     SGSGKTQSTN FLIHHLTALS QKGFVSGVEQ IILGAGPVLE AFGNAKTAHN NNSSRFGKFI
     QVNYQETGTV LGAYVEKYLL EKSRLVYQEH NERNYHVFYY LLAGASEDER SAFHLKQPEE
     YHYLNQITKK PLRQSWDDYC YDSEPDCFMV EGEDLRHDFE RLQLAMEMVG FLPKTRRQIF
     SLLSAILHLG NICYKKKTYR DDSIDICNPE VLPIVSELLE VKEEMLFEAL VTRKTVTVGE
     KLILPYKLAE AVTVRNSMAK SLYSALFDWI VFRINHALLN SKDLEHNTKT LSIGVLDIFG
     FEDYENNSFE QFCINFANER LQHYFNQHIF KLEQEEYRTE GISWHNIDYI DNTCCINLIS
     KKPTGLLHLL DEESNFPQAT NQTLLDKFKH QHEDNSYIEF PAVMEPAFII KHYAGKVKYG
     VKDFREKNTD HMRPDIVALL RSSKNAFISG MIGIDPVAVF RWAILRAFFR AMVAFREAGK
     RHIHRKAGHD DTAPCAILKS MDSFSFLQHP VHQRSLEILQ RCKEEKYSIT RKNPRTPLSD
     LQGMNALNEK NQHDTFDIAW NGRTGIRQSR LSSSTSLLDK DGIFANSTSS KLLERAHGIL
     TRNKNFKPKP ALPKHLLEVN SLKHLTRLTL QDRITKSLLH LHKKKKPPSI SAQFQTSLSK
     LMETLGQAEP YFVKCIRSNA EKLPLRFNDA LVLRQLRYTG MLETVRIRQS GYSSKYSFQD
     FVSHFHVLLP RNIIPSKFNI QDFFRKINLN PDNYQVGKTM VFLKEQERQH LQDLLHQEVL
     RRIILLQRWF RVLLCRQHFL HLRQASVIIQ RFWRNYLNRK QVRDAAVQKD AFVMASAAAL
     LQASWRAHLE RQRYLELRAA AIVIQQKWRD HYRRRHMAAI CIQARWKAYR ESKRYQEQRK
     KIILLQSTCR GFRARQRFKA LKEQRLRETK PELGLVNIKG YGSLEIQGSD PSEWEDCSFD
     NRIKAIEECK SVTESNRISH ESSVDCLKKS PNKQQERAQS PSGVDLQEDV LVRERPRSLE
     DLHQKKVGRA KRESRRMREL EQAIFSLELL KVRSLGGVSP SEDRRWSTEL VPEGLQSPRG
     TPDSESSQGS LELLSSEESQ KSKLESVISD EGDLLFPSPK ISSSPKFDSR DNALSASNET
     SYAEHLKDGT MKEKVVCSSE SITCKPQLKD SFISNSLPTF FYIPQQDPQK TNSQLDTSIQ
     RNKLLENEDT PGEALTLDIN RETRRYHCSG EDQIVPPLNT ESSNPMLKKL EKLNTEKEER
     QKQLQQQNEK EMMEQIRQQT DILEKERKAF KTIEKPRIGE CLVAPSSYQS KQRVERPSSL
     LSLNTSNKGE LNVLGSLSVK DAALAQKDSS SARLLPKDRP VTVFFERKGS PCQSSTVKEL
     SKTDRMGAQL NVACKLSNNR ISKREHFMPT QSYSHNSDDL SREGNTRPIF FTPKDNMNIP
     LVSKEALNSK NPQLRKEDEP AWKPVKLAGP GQRETSQRFS SVDEQAKLHK TMSQGEITKL
     AVRQKASDSD IRPQRAKMRF WAKGKQGEKK TTRVKPTTQS EVSPVFTGAD VIPAHQFPDE
     LAQYHPTPPL SPELPGSCRK EFKENKEPSP KAKRKRSVKI SNVALDSMHW QNDSVQIIAS
     VSDLKSMDEF LLKKMNDLDN EDSKKDTLVD VVFKKALKEF RQNIFSFYSS ALAMDDGKSI
     RYKDLYALFE QILEKTMRLE QRDSLGESPV RVWVNTFKVF LDEYMNEFKT SDYTATKVPK
     TERKKRRKKE TDLVEEHNGH IFKATQYSIP TYCEYCSSLI WIMDRASVCK LCKYACHKKC
     CLKTTAKCSK KYDPELSSRQ FGVELSRLTS EDRTVPLVVE KLINYIEMHG LYTEGIYRKS
     GSTNKIKELR QGLDTDAENV NLDDYNIHVI ASVFKQWLRD LPNPLMTFEL YEEFLRAMGL
     QERKETIRGV YSVIDQLSRT HLNTLERLIF HLVRIALQED TNRMSANALA IVFAPCILRC
     PDTTDPLQSV QDISKTTTCV ELIVVEQMNK YKARLKDISS LEFAENKAKT RLSLIRRSMK
     PVLIAVRFMN ITRNSVSGKG RIRRGNYPGP SSPVVVRLPS VSDVSEETLT SEAAMETDIT
     EQQQAAMQQE ERVLTEQIEN LQKEKEELTF EMLVLEPRAS DDETLESEAS IGTADSSENL
     NMESECAISE KSERSLALSS LKTAGKSEPS SKLRKQLKKQ QDSLDVVDSS VSSLCLSNTA
     SSHGTRKLFQ IYSKSPFYRA ASANEALGME GPLGQTKSLE DRPQFISRGT FNPEKGKQKL
     KNVKNSPQKT KETPEGTVMS GRRKTVDPDC TSNQQLALFG NNEFMV
//
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