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Database: UniProt
Entry: A0A3Q0D2R8_MESAU
LinkDB: A0A3Q0D2R8_MESAU
Original site: A0A3Q0D2R8_MESAU 
ID   A0A3Q0D2R8_MESAU        Unreviewed;      2333 AA.
AC   A0A3Q0D2R8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Unconventional myosin-XVIIIa isoform X6 {ECO:0000313|RefSeq:XP_021086839.1};
GN   Name=Myo18a {ECO:0000313|RefSeq:XP_021086839.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021086839.1};
RN   [1] {ECO:0000313|RefSeq:XP_021086839.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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_021086839.1; XM_021231180.1.
DR   Proteomes; UP000189706; Unplaced.
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:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
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   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; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000189706}.
FT   DOMAIN          220..311
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          643..695
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          699..1479
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..110
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          321..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1018..1037
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1349..1369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1744..1772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2146..2197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2231..2333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..476
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2231..2255
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2278..2293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2295..2310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2311..2333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         792..799
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2333 AA;  261688 MW;  99BF80118DDFB441 CRC64;
     MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS MRRGFFNLNR SSKRESKTRL
     EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
     AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLMQHP
     GLGIPRPGPR SRVPELVTKR FPADLRLPAV VPPPPPALRE LELQRRPTGD FGFSLRRTTM
     LDRAPEGQAY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GQNVENKSRD EIVEMIRQSG
     DSVRLKVQPI PELSELSRSW LRTGEGHRRE PADVKEEDKT LPKPGSPGKE EGALEGSSKD
     SSGPPTSPQP ATSPVPSETS QRAKSPEATL TMNGLGAAST ANEEAPGLSR KRVANAMRKV
     VSKVLPGDEE PGNAKEPPGR GAKSPEHPPR GKKGEKAASS PKPPPPPPPP PAPPKPEAKK
     EAVKDELSMG LRSLMSRGRG KDHKSRSKQP PGRGEKAPSQ EPGSPEKPGS PDVVDAPKKA
     GSPAKPETPN KQCSPAPAQE LVDPDSAGPK SNASGEQQAN SPALGVRQET GADPEVRLSP
     AEEAHQRLER IFTASLDPEA ASPAHSQAKT EDQIAAEEAW YETEKVWLVH KDGFSLASQL
     KSEQLSLPEG KVRVKLDHDG AILDVDEDDI EKANAPSCDR LEDLASLVYL NESSVLHTLR
     QRYGASLLHT YAGTSLLVLS PRGAPAVYSE KVMHMFKGCR REDMAPHIYA VAQTAYRAML
     MSRQDQSIVL LGSSGSGKTT SFQHLVQYLA TIAGTSGSKV FSVEKWQALY TLLEAFGNSP
     TIMNGSATRF SQILSLDFDQ AGQVASASIQ TMLLEKLRVA RRPASEATFN VFYYLLACGD
     STLRTELHLN HLAENNVFGI VPLAKPEEKQ KAAQQFSKLQ TAMKVLAISP EEQKACWLIL
     ASIYHLGAAG ATKEAAEAGR KQFARHEWAQ KAAYLLGCSL EELSSAIFKH QLKGGTLQRS
     TSFRQGPEES GLGDGTGPKL SAMECLEGMA SGLYSELFTL LISLVNRALK SSQHSLCSMM
     IVDTPGFQNP ERGGSARGAS FEELCHNYAQ DRLQRLFHER TFLQELERYK EENIELAFED
     LEPATDDSVA AVDQASHQSL VRSLAHADEA RGLLWLLEEE ALVPGATEDT LLDRLFSYYG
     PQEGDKKGQS PLLRSSKPRH FLLGHSHGTN WVEYNVSGWL NYTKQNPATQ NASQLLQDSQ
     KKIISNLFLG RAGSATVLSG SIAGLEGGSQ LALRRATSMR KTFTTGMAAV KKKSLCIQIK
     LQVDALIDTI KRSKMHFVHC FLPVAEGWPG EPRSASSRRV SSSSELDLPP GDPCEAGLLQ
     LDVSLLRAQL RGSRLLDAMR MYRQGYPDHM VFSEFRRRFD VLAPHLTKKH GRNYIVMDEK
     RAVEELLESL DLEKSSCCMG LSRVFFRAGT LARLEEQRDE QTSRHLTLFQ AACRGYLARQ
     HFKKRKIQDL AIRCVQKNIK KNKGVKDWPW WKLFTTVRPL IQVQLSEEQI RNKDEEIQQL
     RSKLEKVEKE RNELRLNSDR LETRISELTS ELTDERNTGE SASQLLDAET AERLRAEKEM
     KELQTQYDAL KKQMEVMEME VMEARLIRAA EINGDVEDDD AGGEWRLKYE RAVREVDFTK
     KRLQQELEDK MEVEQQSRRQ LERRLGDLQA DSDESQRTLQ QLKKKCQRLT AELQDTKLHL
     EGQQVRNHEL EKKQRRFDSE LSQAQEETQR EKLQREKLQR EKDMLLAEAF GLKQQLEEKD
     MDIAGFTQKV VSLEAELQDI SSQESKDEAS LAKVKKQLRD LEAKVKDQEE ELDEQAGSIQ
     MLEQAKLRLE MEMERMRQTH SKEMESRDEE IEEARQSCQK KLKQMEVQLE EEYEDKQKAL
     REKRELESKL STLSDQVNQR DYESEKRLRK DLKRTKALLA DAQIMLDHLK NNAPSKREIA
     QLKNQLEESE FTCAAAVKAR KAMEVEMEDL HLQIDDIAKA KTALEEQLSR LQREKNEIQN
     RLEEDQEDMN ELMKKHKAAV AQASRDMVQM NDLQTQLEES NKEKQELQEK LQALQSQVEF
     LEQSMVDKSL VSRQEAKIRE LETRLEFEKT QVKRLESLAS RLKENMEKLT EDRDQRAAAE
     NREKEQNKRL QRQLRDTKEE MSELARKEAE ASRKKHELEM DLESLEAANQ SLQADLKLAF
     KRIGDLQAAI EDEMESDENE DLINSEGDSD VDSELEDRVD GVKSWLSKNK GPSKAASDDG
     SLKSSSPTSH WKSLAPDPSD DERDPADSTS RPRFSHNYLS DSDTEAKPTE TSA
//
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