ID A0A2K6AI46_MANLE Unreviewed; 2054 AA.
AC A0A2K6AI46;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Myosin XVIIIA {ECO:0000313|Ensembl:ENSMLEP00000039713.1};
GN Name=MYO18A {ECO:0000313|Ensembl:ENSMLEP00000039713.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000039713.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000039713.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011845751.1; XM_011990361.1.
DR STRING; 9568.ENSMLEP00000039713; -.
DR Ensembl; ENSMLET00000063332.1; ENSMLEP00000039713.1; ENSMLEG00000043771.1.
DR GeneID; 105547005; -.
DR KEGG; mleu:105547005; -.
DR CTD; 399687; -.
DR GeneTree; ENSGT00940000155768; -.
DR OrthoDB; 3687088at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0042641; C:actomyosin; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
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:0031032; P:actomyosin structure organization; IEA:Ensembl.
DR GO; GO:0090164; P:asymmetric Golgi ribbon formation; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0006259; P:DNA metabolic process; IEA:InterPro.
DR GO; GO:0048194; P:Golgi vesicle budding; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1903028; P:positive regulation of opsonization; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0043030; P:regulation of macrophage activation; IEA:Ensembl.
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:UP000233140}.
FT DOMAIN 220..311
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 349..401
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 405..1185
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 542..607
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..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1451..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1852..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1962..2054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1249..1353
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1962..1985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1999..2014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2016..2031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2054 AA; 233216 MW; A34818A972A91E31 CRC64;
MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS LRRGFFNLNR SSKRESKTRL
EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLVQHS
GPGIPRPGHR SRAPELVTKK FPVDLRLPPV VPLPPPALRE LELQRRPTGD FGFSLRRTTM
LDRGPEGQAY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GHNVENKSRD EIVEMIRQSG
DSVRLKVQPI PELSELSRSW LRSGEGPRRE PSDAKTEEQI AAEEAWNETE KVWLVHRDGF
SLASQLKSEE LSLPEGKVRV KLDHDGAILD VDEDDVEKAN APSCDRLEDL ASLVYLNESS
VLHTLRQRYG ASLLHTYAGP SLLVLGPRGA PAVYSEKVMH MFKGCRREDM APHIYAVAQT
AYRAMLMSRQ DQSIILLGSS GSGKTTSCQH LVQYLATIAG ISGNKVFSVE KWQALYTLLE
AFGNSPTIMN GNATRFSQIL SLDFDQAGQV ASASIQTMLL EKLRVARRPA SEATFNIFYY
LLACGDGTLR TELHLNHLAE NNVFGIVPLA KPEEKQKAAQ QFSKLQAAMK VLGISPDEQK
ACWLILAAIY HLGAAGATKE AAEAGRKQFA RHEWAQKAAY LLGCSLEELS SAIFKHQHKG
GTLQRSTSFR QGPEESGLGD GTGPKLSALE CLEGMAAGLY SELFTLLVSL VNRALKSSQH
SLCSMMIVDT PGFQNPEQGG SARGASFEEL CHNYTQDRLQ RLFHERTFVQ ELERYKEENI
ELAFDDLESP TDDSVAAVDQ ASHQSLVRSL ARTDEARGLL WLLEEEALVP GASEDTLLER
LFSYYGPQEG DKKGQSPLLR SSKPHHFLLG HSHGTNWVEY NVTGWLNYTK QNPATQNAPR
LLQDSQKKII SNLFLGRAGS ATVLSGSIAG LEGGSQLALR RATSMRKTFT TGMAAVKKKS
LCIQMKLQVD ALIDTIKKSK LHFVHCFLPV AEGWAGEPRS ASSCRVSSSS ELDLPSGDHC
EAGLLQLDVP LLRTQLRGSR LLDAMRMYRQ GYPDHMVFSE FRRRFDVLAP HLTKKHGRNY
IVVDERRAVE ELLECLDLEK SSCCMGLSRV FFRAGTLARL EEQRDEQTSR NLTLFQAACR
GYLARQHFKK RKIQDLAIRC VQKNIKKNKG VKDWPWWKLF TTVRPLIEVQ LSEEQIRNKD
EEIQQLRSKL EKVEKERNEL RLNSDRLESR ISELTSELTD ERNTGESASQ LLDAETAERL
RAEKEMKELQ TQYDALKKQM EVMEMEVMEA RLIRAAEING EVDDDDAGGE WRLKYERAVR
EVDFTKKRLQ QEFEDKLEVE QQNKRQLERR LGDLQADSEE SQRALQQLKK KCQRLTAELQ
DTKLHLEGQQ VRNHELEKKQ RRFDSELSQA HEEAQREKLQ REKLQREKDM LLAEAFSLKQ
QLEEKDMDIA GFTQKVVSLE AELQDISSQE SKDEASLAKV KKQLRDLEAK VKDQEEELDE
QAGTIQMLEQ AKLRLEMEME RMRQTHSKEM ESRDEEVEEA RQSCQKKLKQ MEVQLEEEYE
DKQKVLREKR ELEGKLATLS DQVNRRDFES EKRLRKDLKR TKALLADAQL MLDHLKNSAP
SKREIAQLKN QLEESEFTCA AAVKARKAME VEIEDLHLQI DDIAKAKTVL EEQLSRLQRE
KNEIQNRLEE DQEDMNELMK KHKAAVAQAS RDLAQINDLQ AQLEEANKEK QELQEKLQAL
QSQVEFLEQS MVDKSLVSRQ EAKIRELETR LEFERTQVKR LESLASRLKE NMEKLTEERD
QRIAAENREK EQNKRLQRQL RDTKEEMGEL ARKEAEASRK KHELEMDLES LEAANQSLQA
DLKLAFKRIG DLQAAIEDEM ESDENEDLIN SLQDMVTKYQ KRKNKLEGDS DVDSELEDRV
DGVKSWLSKN KGPSKAASDD GSLKSSSPTS YWKSLAPDRS DDEHDPLDNT SRPRYSHSYL
SDSDTEAKLT ETNK
//
