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
//