ID Q91973_COTCO Unreviewed; 1931 AA.
AC Q91973;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=Myosin-7 {ECO:0000256|ARBA:ARBA00039815};
DE AltName: Full=Myosin heavy chain 7 {ECO:0000256|ARBA:ARBA00041438};
DE AltName: Full=Myosin heavy chain slow isoform {ECO:0000256|ARBA:ARBA00043207};
DE AltName: Full=Myosin heavy chain, cardiac muscle beta isoform {ECO:0000256|ARBA:ARBA00041905};
OS Coturnix coturnix (Common quail) (Tetrao coturnix).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=9091 {ECO:0000313|EMBL:AAC59912.1};
RN [1] {ECO:0000313|EMBL:AAC59912.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8663323; DOI=10.1074/jbc.271.29.17047;
RA Nikovits Jr W., Wang G.F., Feldman J.L., Miller J.B., Wade R., Nelson L.,
RA Stockdale F.E.;
RT "Isolation and characterization of an avian slow myosin heavy chain gene
RT expressed during embryonic skeletal muscle fiber formation.";
RL J. Biol. Chem. 271:17047-17056(1996).
RN [2] {ECO:0000313|EMBL:AAC59912.1}
RP NUCLEOTIDE SEQUENCE.
RA Nikovits W., Wang G.-F., Stockdale F.E., Roberts S.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity
CC essential for muscle contraction. Forms regular bipolar thick filaments
CC that, together with actin thin filaments, constitute the fundamental
CC contractile unit of skeletal and cardiac muscle.
CC {ECO:0000256|ARBA:ARBA00037090}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000256|ARBA:ARBA00004204}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; U53861; AAC59911.1; -; Genomic_DNA.
DR EMBL; U53862; AAC59912.1; -; mRNA.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.10.250.2420; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF1; MYOSIN-7; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 6.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 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|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}.
FT DOMAIN 25..74
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 78..773
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 650..672
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1255..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1931 AA; 221746 MW; D2C15DD6E9BC8DE9 CRC64;
MEALLGAAAP FLRAPEGPHS APPGDTRGLC FVPHPQLEFV RARITARAGN GVTVTTETGE
TLTVPEADVH PQNPPKFDRI EDMAMLTFLH EPAVLYNLKE RYASWMIYTY SGLFCVTVNP
YKWLPVYNAE VVAAYRGKKR TEVPPHIFSI SDNAYQNMLT DRENQSILIT GESGAGKTVN
TKRVIQYFAS IAAIGDRKKE VANSSKGTLE DQIIQANPAL EAFGNAKTVR NDNSSRFGKF
IRIHFGATGK LASADIETYL LEKSRVIFQL KAERNYHIFY QILSNKKPEL LEMLLITNNP
YDYSYVSQGE VTVASIDDSE ELLATDSAFD VLGFTAEEKA GVYKLTGAIM HFGNMKFKQK
QREEQAEPDG TEDADKSAYL MGLNSADLLK GLCHPRVKVG NEYVTKGQSV QQVYYSIGAL
AKAVYEKMFN WMVVRINNSL ETKQPRQYFI GVLDIAGFEI FDFNSFEQLC INFTNEKLQQ
FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL QACIDLIEKP MGIMSILEEE CMFPKASDMT
FKAKLFDNHL GKSANFGKPR NVKGKSEAHF SLIHYAGTVD YNIIGWLEKN KDPLNETVVG
LYQKSALKLL ASLFSNYAGA DAGGDSGKGK GAKKKGSSFQ TVSALHRENL NKLMANLKTT
HPHFVRCLIP NERKEPGVMD NSLVMHQLRC NGVLEGIRIC RKGFPNRILY GDFRQRYRIL
NPTAIPEGQF IDSRKGAEKL LGSLDIDHNQ YKFGHTKVFF KAGLLGLLEE MRDERLSLII
TRIQAQARGQ LMRIEFKKIL ERRDALLVIQ WNIRAFMGVK NWPWMKLYFK IKPLLKSAET
EKEMQTMKEE FGHLKEALEK SEARRKELEE KMVSMLQEKN DLQLQVQAEQ DNLADAEERC
DQLIKNKIQL EAKVKEMTER LEEEEEMNAE LTAKKRKLED ECSELKKDID DLELSLAKVE
KEKHATENKV KNLTEEMAGL DENITKLTKE KKTLQESHQQ ALDDLQAEED KVNTLAKAKV
KLEQQADDLE SSLQQEKKIR MDLERAKRKL EGDLKLAQES VMDLENDKQQ LEERLKKKDF
ELNTLNARIE DEQAIAAQLQ KKLKELQARI EELEEELEAE RTGRAKVEKL RSELLQELEE
TSERLEEAGG ATSVQLELNK KREAEFQKLR RDLEEATLQH EATAAALRKK HADSVAELSE
QLDNMQRVKQ KLEKEKSELK LELDDVSSNM EQLIKAKANL EKMCRSTEDQ MNEHRNKLEE
SQRTVTDLST QRAKLQTENS ELSRQLEEKE AFINQLMRGK LTYTQQLEDL KRQLEEEAKA
KNALAHALQS AQHDCDLLRE QYEEEMEAKA ELQRALSKAN SEVAQWRTKY ETDAIQRTEE
LEEAKKKLAQ RLQEAEEAVE AVNAKCSSLE KTKHRLQNEI EDLMADVERS NAAAAALDKK
QRNFDKILSE WKQKFEESQT ELEASQKEAR SLSTELFKLK NAYEESLEHL ETFKRENKNL
QEEISDLTEQ LGASQKSIHE LEKVRKQLDA EKLELQAALE EAEASLEHEE GKILRAQLEF
NQVKAEYERK LAEKDEEMEQ SKRNHLRVVD SLQTSLDAET RSRNEALRLK KKMEGDLNEM
EIQLSHANRT AAEAQKQVKA LQGYLKDTQL QLDDAVRANE DLKENIAIVE RRNNLLQSEL
EELRAMVEQS ERARKLAEQE LTEASERVQL LHSQNTSLIN QKKKMEADIS QLQTEVEEAI
QECRNAEEKA KKAITDAAMM AEELKKEQDT SAHLERMKKN MEQTVKDLQL RLDEAEQLAL
KGGKKQLQKL EARVRELENE LEAEQKHNAE SIKGLRKSER RVKELSYQTE EDRKNMVRLQ
DLVDKLQLKV KAYKRQAEEA EEQANSNLAK FRKAQHELDE AEERADIAES QVNKLRARSR
DISNKKGLNE E
//
