ID A0A1S2ZJY5_ERIEU Unreviewed; 2052 AA.
AC A0A1S2ZJY5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Unconventional myosin-XVIIIa isoform X2 {ECO:0000313|RefSeq:XP_007520514.1};
GN Name=MYO18A {ECO:0000313|RefSeq:XP_007520514.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007520514.1};
RN [1] {ECO:0000313|RefSeq:XP_007520514.1}
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_007520514.1; XM_007520452.2.
DR CTD; 399687; -.
DR eggNOG; KOG0161; Eukaryota.
DR OrthoDB; 3687088at2759; -.
DR Proteomes; UP000079721; 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; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 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};
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:UP000079721}.
FT DOMAIN 218..309
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 347..399
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 403..1183
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1448..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1958..2052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1247..1344
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1958..1983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1997..2014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2029..2052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 496..503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2052 AA; 233067 MW; 6012699381398293 CRC64;
MFNLMKKDKD KDGGRKEKKD KKDKKERMSA AELRSLEEIS MRRGFFNLNR SSKRESKTRL
EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAASPQVEVR TLEGQLMQHP
GIPRPGPRSR VPELVTKRFP ADLRLPPVLS PPAPALRQLE LQRRPTGDFG FSLRRTTMLD
RGPEGQVCRK VVHFAEPGAG TKDLALGLVP GDRLVEINGH NVESKSRDEI VEMIRQSGDC
VRLKVQPIPE LSELSRSWLR SSKGTHREPA DVKTEEQIAA EEAWYETEKV WLVHKDGFSL
ASQLRSEELS LPEGKVRVKL DHDGTVLDVD EDDVEKANAP SCDRLEDLAS LVYLSESSVL
HTLRQRYGAS LLHTYAGPSL LVLSPRGAPA VYSEKVMHMF KGCRREDMAP HIYAVAQSAY
RAMLMSRQDQ SIVLLGSSGS GKTTSCQHLV QYLATIAGTS GNKVFSVEKW QALYTLLEAF
GNSPTIMNGN ATRFSQILSL DFDQAGQVAS ASIQTMLLEK LRVVRRPASE ATFNVFYYLL
ACGDGTLRTE LHLNHLAENN VFGIVPLAKP EEKQKAAQQF SKLQAAMKVL GISPDEQKAC
WLILAATYHL GAAGATKEAA EAGRKQFARH EWAQKAAYLL GCSLEELSSA IFKHQHKGGT
LQRSTSFRQG PEESSLGDGT GPKLSALECL EGMASGLYSE LFTLLISLIN RALKSNQHSL
CSMMIVDTPG FQNPEQGGSA RGASFEELCH NYAQDRLQRL FHERTFVQEL ERYKEENIEL
AFDDLEPAMD NSVAVVDQAS HQSLVRSLAR TDEARGLLWL LEEETLVPGA TEDSLLERLF
SYYGPQEGDK KGQSPLLRSS KPHHFLLGHS HNTNWVEYNM AGWLSYTKQN PATQNAPRLL
QDSQKKIISN LFLGRAGSTT VLSGSIAGLE GGSQLALRRA TSMRKTFTTG MAAVKKKSLC
IQIKLQVDAL IDTIKKSKLH FVHCFLPVAE GWGGEPRSAS SRRVSSSSEL DLPPGDHCEA
GLLQLDVPLL RAQLRGSRLL DAMRMYRQGY PDHMVFSEFR RRFDVLAPHL TKKHGRNYIV
VDERRAVEEL LESLDLEKSS CCMGLSRVFF RAGTLVRLEE QRDEQTSRNL TLFQAACKGY
LARQHFKKRK IQDLAIRCVQ KNIKKNKGVK DWPWWKLFTT VRPLIEVQLS EEQIRNKDEE
IQQLRSKLEK VEKERNELRL HSDRLETRIS ELTSELTDER NTGESASQLL DAETAERLRA
EKEMKELQTQ YDAMKKQMEV MEIEVMEARL IRAAEINGEV DDDDTGGEWR LKYERAVREV
DFTKKRLQQE FEDKLEVEQQ NKRQLERRLG DLQADSEESQ RALQQLKKKC QRLTAELQDT
KLHLEGQQVR NHELEKKQRR FDSELSQAHE ETQREKLQRE KLQREKDMLL AEAFSLKQQL
EEKDMDIAGF TQKVVSLEAE LQDISSQESK DEASLAKVKK QLRDLEAKVK DQEEELDEQA
GTIQMLEQAK LRLEMEMERM RQTHSKEMES RDEEVEEVRQ SCQKKLKQME VQLEEEYEDK
QKVLREKREL EGKFTTLSDQ VNQRDFESEK RLRKDLKRTK ALLADAQIML DHLKNSAPSK
REIAQLKNQL EESEFTCAAA VKARKAMEVE IEDLHLQIDD IAKAKTALEE QLSRLQREKN
EVQNRLEEDQ EDMNELMKKH KAAVAQATRD LAQMTDLQAQ LEEANKEKQE LQEKLQALQS
QVEFLEQSMV DKSLVSRQEA KIRELETRLE FERTQVKRLE SLASRLKENM EKLTEERDQR
AAAENREKEQ NKRLQRQLRD TKEEMGELSR KEAEASRKKH ELEMDLESLE AANQSLQADL
KLAFKRIGDL QAAIEDEMES DENEDLINSL QDMVTKYQKR KNKLEGDSDV DSELEDRVDG
VKSWLSKNKG PSKAASDDGS LKSSSPTSCW KSPAPDQSDD EHDLPDNTSR PQYSHNYLSD
SDTEAKSTEA NA
//
