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Database: UniProt
Entry: F7GPY6_MACMU
LinkDB: F7GPY6_MACMU
Original site: F7GPY6_MACMU 
ID   F7GPY6_MACMU            Unreviewed;      2592 AA.
AC   F7GPY6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   24-JAN-2024, entry version 73.
DE   SubName: Full=Myosin IXA {ECO:0000313|Ensembl:ENSMMUP00000033455.3};
GN   Name=MYO9A {ECO:0000313|Ensembl:ENSMMUP00000033455.3,
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:ENSMMUP00000033455.3, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000033455.3, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000033455.3,
RC   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:ENSMMUP00000033455.3}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000033455.3};
RG   Ensembl;
RL   Submitted (JUL-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; ENSMMUT00000040390.3; ENSMMUP00000033455.3; ENSMMUG00000019278.4.
DR   VEuPathDB; HostDB:ENSMMUG00000019278; -.
DR   VGNC; VGNC:75120; MYO9A.
DR   GeneTree; ENSGT00940000154905; -.
DR   HOGENOM; CLU_140117_0_0_1; -.
DR   Proteomes; UP000006718; Chromosome 7.
DR   Bgee; ENSMMUG00000019278; Expressed in spermatocyte and 22 other cell types or tissues.
DR   ExpressionAtlas; F7GPY6; baseline.
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          2043..2092
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          2107..2295
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          1738..1762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1846..1880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2403..2468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2533..2575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1487..1526
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2370..2397
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        1745..1762
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1861..1875
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2412..2432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2439..2453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2454..2468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2540..2554
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   2592 AA;  297920 MW;  086A357C51EAD5A0 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 GQREVARPAH KKKARMARTR SDFLTRASHC
     ELGPTPSLDQ ASHSDSEMTS QRFSSVDEQA KLHKTMSQGE ITKLAVRQKA SDSDIRPQRA
     KMRFWAKGKQ GEKKTTRVKP TTQSEVSPVF TGADVIPAHQ FPDELAQYHP TPPLSPELPG
     SCRKEFKENK EPSPKAKRKR SVKISNVALD SMHWQNDSVQ IIASVSDLKS MDEFLLKKMN
     DLDNEDSKKD TLVDVVFKKA LKEFRQNIFS FYSSALAMDD GKSIRYKDLY ALFEQILEKT
     MRLEQRDSLG ESPVRVWVNT FKVFLDEYMN EFKTSDYTAT KVPKTERKKR RKKETDLVEE
     HNGHIFKATQ YSIPTYCEYC SSLIWIMDRA SVCKLCKYAC HKKCCLKTTA KCSKKYDPEL
     SSRQFGVELS RLTSEDRTVP LVVEKLINYI EMHGLYTEGI YRKSGSTNKI KELRQGLDTD
     AENVNLDDYN IHVIASVFKQ WLRDLPNPLM TFELYEEFLR AMGLQERKET IRGVYSVIDQ
     LSRTHLNTLE RLIFHLVRIA LQEDTNRMSA NALAIVFAPC ILRCPDTTDP LQSVQDISKT
     TTCVELIVVE QMNKYKARLK DISSLEFAEN KAKTRLSLIR RSMGKGRIRR GNYPGPSSPV
     VVRLPSVSDV SEETLTSEAA METDITEQQQ AAMQQEERVL TEQIENLQKE KEELTFEMLV
     LEPRASDDET LESEASIGTA DSSENLNMES ECAISEKSER SLALSSLKTA GKSEPSSKLR
     KQLKKQQDSL DVVDSSVSSL CLSNTASSHG TRKLFQIYSK SPFYRAASAN EALGMEGPLG
     QTKSLEDRPQ FISRGTFNPE KGKQKLKNVK NSPQKTKETP EGTVMSGRRK TVDPDCTSNQ
     QLALFGNNEF MV
//
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