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Database: UniProt
Entry: F6RJH8_MACMU
LinkDB: F6RJH8_MACMU
Original site: F6RJH8_MACMU 
ID   F6RJH8_MACMU            Unreviewed;      2066 AA.
AC   F6RJH8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   24-JAN-2024, entry version 81.
DE   SubName: Full=Myosin XVIIIA {ECO:0000313|Ensembl:ENSMMUP00000013005.4};
GN   Name=MYO18A {ECO:0000313|Ensembl:ENSMMUP00000013005.4,
GN   ECO:0000313|VGNC:VGNC:75058};
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:ENSMMUP00000013005.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000013005.4, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000013005.4,
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:ENSMMUP00000013005.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000013005.4};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   PaxDb; 9544-ENSMMUP00000013005; -.
DR   Ensembl; ENSMMUT00000013881.4; ENSMMUP00000013005.4; ENSMMUG00000009938.4.
DR   VEuPathDB; HostDB:ENSMMUG00000009938; -.
DR   VGNC; VGNC:75058; MYO18A.
DR   eggNOG; KOG0161; Eukaryota.
DR   GeneTree; ENSGT00940000155768; -.
DR   HOGENOM; CLU_000192_1_0_1; -.
DR   TreeFam; TF339614; -.
DR   Proteomes; UP000006718; Chromosome 16.
DR   Bgee; ENSMMUG00000009938; Expressed in hindlimb stylopod muscle and 20 other cell types or tissues.
DR   ExpressionAtlas; F6RJH8; 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:0008094; F:ATP-dependent activity, acting on DNA; IEA:InterPro.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006259; P:DNA metabolic process; IEA:InterPro.
DR   CDD; cd01386; MYSc_Myo18; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR036064; MYSc_Myo18.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF13; UNCONVENTIONAL MYOSIN-XVIIIA; 1.
DR   Pfam; PF00063; Myosin_head; 2.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50163; RECA_3; 1.
DR   PROSITE; PS51844; SH3_LIKE; 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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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}.
FT   DOMAIN          220..311
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          361..413
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          417..1197
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          554..619
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1467..1492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1864..1913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1974..2066
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1261..1365
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        140..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1974..1997
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2011..2026
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2028..2043
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2044..2058
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         510..517
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2066 AA;  234563 MW;  39DB40B4E472EC22 CRC64;
     MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS LRRGFFNLNR SSKRESKTRL
     EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
     AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLVQHP
     GPGIPRPGHR SRAPELVTKK FPVDLRLPPV VPLPPPALRE LELQRRPTGD FGFSLRRTTM
     LDRGPEGQAY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GHNVENKSRD EIVEMIRQSG
     DSVRLKVQPI PELSELSRSW LRSGEGPRRE PSDLDSEAAS RAHSQAKTEE QIAAEEAWNE
     TEKVWLVHRD GFSLASQLKS EELSLPEGKV RVKLDHDGAI LDVDEDDVEK ANAPSCDRLE
     DLASLVYLNE SSVLHTLRQR YGASLLHTYA GPSLLVLGPR GAPAVYSEKV MHMFKGCRRE
     DMAPHIYAVA QTAYRAMLMS RQDQSIILLG SSGSGKTTSC QHLVQYLATI AGISGNKVFS
     VEKWQALYTL LEAFGNSPTI MNGNATRFSQ ILSLDFDQAG QVASASIQTM LLEKLRVARR
     PASEATFNIF YYLLACGDGT LRTELHLNHL AENNVFGIVP LAKPEEKQKA AQQFSKLQAA
     MKVLGISPDE QKACWLILAA IYHLGAAGAT KEAAEAGRKQ FARHEWAQKA AYLLGCSLEE
     LSSAIFKHQH KGGTLQRSTS FRQGPEESGL GDGTGPKLSA LECLEGMAAG LYSELFTLLV
     SLVNRALKSS QHSLCSMMIV DTPGFQNPEQ GGSARGASFE ELCHNYTQDR LQRLFHERTF
     VQELERYKEE NIELAFDDLE SPTDDSVAAV DQASHQSLVR SLARTDEARG LLWLLEEEAL
     VPGASEDTLL ERLFSYYGPQ EGDKKGQSPL LRSSKPHHFL LGHSHGTNWV EYNVTGWLNY
     TKQNPATQNA PRLLQDSQKK IISNLFLGRA GSATVLSGSI AGLEGGSQLA LRRATSMRKT
     FTTGMAAVKK KSLCIQMKLQ VDALIDTIKK SKLHFVHCFL PVAEGWAGEP RSASSRRVSS
     SSELDLPSGD HCEAGLLQLD VPLLRTQLRG SRLLDAMRMY RQGYPDHMVF SEFRRRFDVL
     APHLTKKHGR NYIVVDERRA VEELLECLDL EKSSCCMGLS RVFFRAGTLA RLEEQRDEQT
     SRNLTLFQAA CRGYLARQHF KKRKIQDLAI RCVQKNIKKN KGVKDWPWWK LFTTVRPLIE
     VQLSEEQIRN KDEEIQQLRS KLEKVEKERN ELRLNSDRLE SRISELTSEL TDERNTGESA
     SQLLDAETAE RLRAEKEMKE LQTQYDALKK QMEVMEMEVM EARLIRAAEI NGEVDDDDAG
     GEWRLKYERA VREVDFTKKR LQQEFEDKLE VEQQNKRQLE RRLGDLQADS EESQRALQQL
     KKKCQRLTAE LQDTKLHLEG QQVRNHELEK KQRRFDSELS QAHEEAQREK LQREKLQREK
     DMLLAEAFSL KQQLEEKDMD IAGFTQKVVS LEAELQDISS QESKDEASLA KVKKQLRDLE
     AKVKDQEEEL DEQAGTIQML EQAKLRLEME MERMRQTHSK EMESRDEEVE EARQSCQKKL
     KQMEVQLEEE YEDKQKVLRE KRELEGKLAT LSDQVNRRDF ESEKRLRKDL KRTKALLADA
     QLMLDHLKNS APSKREIAQL KNQLEESEFT CAAAVKARKA MEVEIEDLHL QIDDIAKAKT
     VLEEQLSRLQ REKNEIQNRL EEDQEDMNEL MKKHKAAVAQ ASRDLAQIND LQAQLEEANK
     EKQELQEKLQ ALQSQVEFLE QSMVDKSLVS RQEAKIRELE TRLEFERTQV KRLESLASRL
     KENMEKLTEE RDQRIAAENR EKEQNKRLQR QLRDTKEEMG ELARKEAEAS RKKHELEMDL
     ESLEAANQSL QADLKLAFKR IGDLQAAIED EMESDENEDL INSLQDMVTK YQKRKNKLEG
     DSDVDSELED RVDGVKSWLS KNKGPSKAAS DDGSLKSSSP TSYWKSLAPD RSDDEHDPLD
     NTSRPRYSHS YLSDSDTEAK LMETNK
//
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