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Database: UniProt
Entry: Q9U487_DORPE
LinkDB: Q9U487_DORPE
Original site: Q9U487_DORPE 
ID   Q9U487_DORPE            Unreviewed;      1849 AA.
AC   Q9U487;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Myosin heavy chain V {ECO:0000313|EMBL:AAF12809.2};
GN   Name=MyoV {ECO:0000313|EMBL:AAF12809.2};
OS   Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Myopsida; Loliginidae; Doryteuthis.
OX   NCBI_TaxID=1051067 {ECO:0000313|EMBL:AAF12809.2};
RN   [1] {ECO:0000313|EMBL:AAF12809.2}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:AAF12809.2};
RX   PubMed=9390390;
RA   Molyneaux B.J., Langford G.M.;
RT   "Characterization of antibodies to the head and tail domains of squid brain
RT   myosin V.";
RL   Biol. Bull. 193:222-223(1997).
RN   [2] {ECO:0000313|EMBL:AAF12809.2}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:AAF12809.2};
RA   Molyneaux B.J., Mulcahey M.K., Stafford P., Langford G.M.;
RT   "Sequence and phylogenetic analysis of squid myosin V, a vesicle motor in
RT   nerve cells.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; AF197336; AAF12809.2; -; mRNA.
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; cd15470; Myo5_CBD; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 3.
DR   Gene3D; 1.20.58.530; -; 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   InterPro; IPR002710; Dilute_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 6.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 4.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {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}.
FT   DOMAIN          111..752
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1529..1806
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          631..653
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1084..1164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          966..1025
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1169..1237
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1303..1362
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1389..1416
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1087..1101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1129..1164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1849 AA;  215422 MW;  BA7ED44A2C025278 CRC64;
     MAVSHLYTKN AKIWVRDEEI VWRTAELGED YKNQKELQVL VFAKGDQLKE EKITIKAKSD
     LPHLRDPTSS KIRLASLNYL MTRSLTPYNL QVRFIDKTYS THIVELFWGD QPLPRWDIYD
     ETTLEIYRYQ RILKNLDPHI YAVAAEPFNQ MTRFNRNQSI IVSGESGAGK TVSAKHTMHY
     FARVGGSTET AIHDKVLASN PIMESFGNAK TIRNDNSSRF GKYIQIAFGT RNYIIGANMK
     TYLLEKSRVV FQAPNERNYH IFYQLCASSK CAELKSFQLT HQDKFLYTNQ GESPHIQEID
     DADLFIKTRS AFTELGISED DQMKMFGIVS AILHLGNIAF ESGEDESTCC VSKKNSHFDI
     VCDLLSLNKD EMQMWLCNRQ ITSGSERIIK PLTAKEAGYG KDALAKHIYA RVFDWIVAKI
     NRNLLTHEDT QNFIGVLDIY GFETFRINSF EQFCINYANE RLQLQFNTRV FTLEQQEYRK
     EGLEWHEISH YDNTPCIDLI ESSQGILASL DDECKMMSGN DANWCTSLFK KLSGTKCFEK
     PRTSQTSFTV CHFAEKVTYM CHGFMEKNMD TVSDLQIETL KGSTNPLVME LFQEKKLERK
     MSTMSEESYL NQPKKSKKHK QTVGISVQRI LEQFDEDSLR HQPSLRRCIK PNDEKKPFRF
     NCKRVVEQLR ACGVLETIRI SAAGFPARET YENIFNMFQQ LLDVIEVDKS DPKLSCEKLM
     QKYIEDPDKY RFGKTKIFFR AGQLALLDKL LSDRRIRWSV MVQKQVRTFL CKRRFNKIRR
     SIFLLQVYGR GYLARLAFQE RRRKFAAIRI QAYFRGYLCR KIYQQKKLAA IVVQRYARKA
     LAQRLFRQLV EDHKATVIQT RVRAYLARRK FEKVRRGMVL LQSHVRRRAA KKVFKELKRK
     AKDSDELKLS NRRLCNKIIE LSNILKEKEG DLKKFRAIQS STSQVQEQYE KLVSEHDNCR
     VLKVKIQEYE FMIERLEGDI KHKTEEFTVL MAEKNKMKTS YDDDKQTMEK KNQELHQQLL
     DAQSLIKTNE ETIANYVKKE EDHSALDNQK EREIEKAHHN KILHDYEVLK NHYDNLRHEM
     TVLKQTHRRT PSDNSTVSFE SAEGEPVAAE PEGEEDEERQ AAHVVAQVVA EPDDKEDQGY
     GTGKRQERPI PAERKSRTVQ RQATLDEPEK VDLALIMKLQ NRIKELEKEI KRLNTERERE
     EEENKDKEHT VYNSLKMQEL ENDNDRMKRE INNLMTAISK SPKYEEGITD AGKAFKEKYD
     TMVEELERRR AEILYIKAIW LETGIEKKDD LHAKHGGEDV SEEEELKTAL QFHQKLNRLL
     ENQLQETEKK SKHTEQDLLT QIEELTKENE RQKQVISQLN SIATNLSSKT GDEISVTMGQ
     DIIRITTENL ELRETVSKQT EQIRKLKKTL KVYARKLKDG EGPFRRFQSL VSATSLSPTS
     AAEIAAELDR DEQESSGVMA AVKHQEREYL GMLEYNKVDE SALIKNLVHD LQPYVAESML
     PGLPAYIIFM CIRHTDHIND DEKVCALLTG VVNGIKRVVK KSNNDVERMT LWLANSCRLL
     HNLKQYSGEK RYQTSNTPKQ NEHCLRNFDL SEYRPVFNDL CVYNYRQLIK VMKDNIEKLI
     VPAILEHEAI AGLNKDDRRG RVPTNETEPD ALDNLQKIMS QYLRVLRNHA VDPEVITLIV
     KQLFYDMSVK ALNNLLLRRD MCNWHKGTQI RYNISHLEQW LREYHLQDAG AFSTMEPLIQ
     ASQLLQARKT DADVDSVCQM CPKLKTAQII KILNQYTPVR GYEDDTVAIS FIRKVQEKLS
     QTRETDMGTN LLMDTQYAFP VTFPFNPSNI ALERITVPDK LHLGFIKRV
//
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