MYS_ARGIR
ID MYS_ARGIR Reviewed; 1938 AA.
AC P24733;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Myosin heavy chain, striated muscle;
OS Argopecten irradians (Bay scallop) (Aequipecten irradians).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC Argopecten.
OX NCBI_TaxID=31199;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adductor muscle;
RX PubMed=1917970; DOI=10.1016/s0021-9258(18)55085-7;
RA Nyitray L., Goodwin E.B., Szent-Gyorgyi A.G.;
RT "Complete primary structure of a scallop striated muscle myosin heavy
RT chain. Sequence comparison with other heavy chains reveals regions that
RT might be critical for regulation.";
RL J. Biol. Chem. 266:18469-18476(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adductor muscle;
RX PubMed=2263488; DOI=10.1093/nar/18.23.7158;
RA Nyitray L., Goodwin E.B., Szent-Gyorgyi A.G.;
RT "Nucleotide sequence of full length cDNA for a scallop striated muscle
RT myosin heavy chain.";
RL Nucleic Acids Res. 18:7158-7158(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 777-836.
RX PubMed=8127365; DOI=10.1038/368306a0;
RA Xie X., Harrison D.H., Schlichting I., Sweet R.M., Kalabokis V.N.,
RA Szent-Gyorgyi A.G., Cohen C.;
RT "Structure of the regulatory domain of scallop myosin at 2.8-A
RT resolution.";
RL Nature 368:306-312(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 777-836.
RX PubMed=8805510; DOI=10.1016/s0969-2126(96)00006-8;
RA Houdusse A., Cohen C.;
RT "Structure of the regulatory domain of scallop myosin at 2-A resolution:
RT implications for regulation.";
RL Structure 4:21-32(1996).
CC -!- FUNCTION: Muscle contraction.
CC -!- FUNCTION: Myosin is a protein that binds to F-actin and has ATPase
CC activity that is activated by F-actin.
CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; X55714; CAA39247.1; -; mRNA.
DR PIR; A40997; A40997.
DR PDB; 1B7T; X-ray; 2.50 A; A=1-835.
DR PDB; 1DFK; X-ray; 4.20 A; A=6-835.
DR PDB; 1DFL; X-ray; 4.20 A; A/B=5-835.
DR PDB; 1KK7; X-ray; 3.20 A; A=1-837.
DR PDB; 1KK8; X-ray; 2.30 A; A=1-837.
DR PDB; 1KQM; X-ray; 3.00 A; A=1-835.
DR PDB; 1KWO; X-ray; 3.80 A; A=1-835.
DR PDB; 1L2O; X-ray; 2.80 A; A=1-835.
DR PDB; 1QVI; X-ray; 2.54 A; A=1-840.
DR PDB; 1S5G; X-ray; 3.10 A; A=1-840.
DR PDB; 1SCM; X-ray; 2.80 A; A=777-836.
DR PDB; 1SR6; X-ray; 2.75 A; A=1-840.
DR PDB; 1WDC; X-ray; 2.00 A; A=774-837.
DR PDB; 2W4T; EM; 35.00 A; C=5-835.
DR PDB; 2W4V; EM; 35.00 A; C=5-835.
DR PDB; 2W4W; EM; 35.00 A; C=5-835.
DR PDB; 3BAS; X-ray; 2.30 A; A/B=835-885.
DR PDB; 3BAT; X-ray; 2.30 A; A/B/C/D=835-885.
DR PDB; 3JTD; X-ray; 2.57 A; A=773-836.
DR PDB; 3JVT; X-ray; 2.10 A; A=773-837.
DR PDBsum; 1B7T; -.
DR PDBsum; 1DFK; -.
DR PDBsum; 1DFL; -.
DR PDBsum; 1KK7; -.
DR PDBsum; 1KK8; -.
DR PDBsum; 1KQM; -.
DR PDBsum; 1KWO; -.
DR PDBsum; 1L2O; -.
DR PDBsum; 1QVI; -.
DR PDBsum; 1S5G; -.
DR PDBsum; 1SCM; -.
DR PDBsum; 1SR6; -.
DR PDBsum; 1WDC; -.
DR PDBsum; 2W4T; -.
DR PDBsum; 2W4V; -.
DR PDBsum; 2W4W; -.
DR PDBsum; 3BAS; -.
DR PDBsum; 3BAT; -.
DR PDBsum; 3JTD; -.
DR PDBsum; 3JVT; -.
DR AlphaFoldDB; P24733; -.
DR SMR; P24733; -.
DR PRIDE; P24733; -.
DR EvolutionaryTrace; P24733; -.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR Gene3D; 1.20.5.370; -; 3.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 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 Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
KW Cytoplasm; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW Thick filament.
FT CHAIN 1..1938
FT /note="Myosin heavy chain, striated muscle"
FT /id="PRO_0000123384"
FT DOMAIN 29..79
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 83..775
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 778..805
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 653..675
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 836..1938
FT /note="Rodlike tail (S2 and LMM domains)"
FT REGION 1041..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1898..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 836..1938
FT /evidence="ECO:0000255"
FT COMPBIAS 1206..1233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1898..1915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1916..1938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1KK8"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1QVI"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1KK8"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1KK8"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1KK7"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1SR6"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1L2O"
FT HELIX 182..196
FT /evidence="ECO:0007829|PDB:1KK8"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:1KK7"
FT HELIX 215..230
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:1L2O"
FT STRAND 240..251
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:1KK8"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1KK7"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1KK8"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1SR6"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 342..358
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:1QVI"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:1QVI"
FT HELIX 416..446
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 472..502
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 514..524
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 529..536
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 544..555
FT /evidence="ECO:0007829|PDB:1KK8"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:1QVI"
FT STRAND 577..582
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 585..589
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 594..598
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 604..611
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 616..621
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 645..660
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 663..671
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 684..691
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 694..696
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 700..704
FT /evidence="ECO:0007829|PDB:1KK7"
FT STRAND 709..712
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 713..720
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 721..723
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 725..727
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 735..746
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 750..752
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:1KK8"
FT STRAND 757..762
FT /evidence="ECO:0007829|PDB:1KK8"
FT HELIX 776..822
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 825..833
FT /evidence="ECO:0007829|PDB:1WDC"
FT TURN 834..836
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 841..885
FT /evidence="ECO:0007829|PDB:3BAS"
SQ SEQUENCE 1938 AA; 222822 MW; A5CCE4127D1A4896 CRC64;
MNIDFSDPDF QYLAVDRKKL MKEQTAAFDG KKNCWVPDEK EGFASAEIQS SKGDEITVKI
VADSSTRTVK KDDIQSMNPP KFEKLEDMAN MTYLNEASVL YNLRSRYTSG LIYTYSGLFC
IAVNPYRRLP IYTDSVIAKY RGKRKTEIPP HLFSVADNAY QNMVTDRENQ SCLITGESGA
GKTENTKKVI MYLAKVACAV KKKDEEASDK KEGSLEDQII QANPVLEAYG NAKTTRNNNS
SRFGKFIRIH FGPTGKIAGA DIETYLLEKS RVTYQQSAER NYHIFYQICS NAIPELNDVM
LVTPDSGLYS FINQGCLTVD NIDDVEEFKL CDEAFDILGF TKEEKQSMFK CTASILHMGE
MKFKQRPREE QAESDGTAEA EKVAFLCGIN AGDLLKALLK PKVKVGTEMV TKGQNMNQVV
NSVGALAKSL YDRMFNWLVR RVNKTLDTKA KRNYYIGVLD IAGFEIFDFN SFEQLCINYT
NERLQQFFNH HMFILEQEEY KKEGIAWEFI DFGMDLQMCI DLIEKPMGIL SILEEECMFP
KADDKSFQDK LYQNHMGKNR MFTKPGKPTR PNQGPAHFEL HHYAGNVPYS ITGWLEKNKD
PINENVVALL GASKEPLVAE LFKAPEEPAG GGKKKKGKSS AFQTISAVHR ESLNKLMKNL
YSTHPHFVRC IIPNELKQPG LVDAELVLHQ LQCNGVLEGI RICRKGFPSR LIYSEFKQRY
SILAPNAIPQ GFVDGKTVSE KILAGLQMDP AEYRLGTTKV FFKAGVLGNL EEMRDERLSK
IISMFQAHIR GYLIRKAYKK LQDQRIGLSV IQRNIRKWLV LRNWQWWKLY SKVKPLLSIA
RQEEEMKEQL KQMDKMKEDL AKTERIKKEL EEQNVTLLEQ KNDLFLQLQT LEDSMGDQEE
RVEKLIMQKA DFESQIKELE ERLLDEEDAA ADLEGIKKKM EADNANLKKD IGDLENTLQK
AEQDKAHKDN QISTLQGEIS QQDEHIGKLN KEKKALEEAN KKTSDSLQAE EDKCNHLNKL
KAKLEQALDE LEDNLEREKK VRGDVEKAKR KVEQDLKSTQ ENVEDLERVK RELEENVRRK
EAEISSLNSK LEDEQNLVSQ LQRKIKELQA RIEELEEELE AERNARAKVE KQRAELNREL
EELGERLDEA GGATSAQIEL NKKREAELLK IRRDLEEASL QHEAQISALR KKHQDAANEM
ADQVDQLQKV KSKLEKDKKD LKREMDDLES QMTHNMKNKG CSEKVMKQFE SQMSDLNARL
EDSQRSINEL QSQKSRLQAE NSDLTRQLED AEHRVSVLSK EKSQLSSQLE DARRSLEEET
RARSKLQNEV RNMHADMDAI REQLEEEQES KSDVQRQLSK ANNEIQQWRS KFESEGANRT
EELEDQKRKL LGKLSEAEQT TEAANAKCSA LEKAKSRLQQ ELEDMSIEVD RANASVNQME
KKQRAFDKTT AEWQAKVNSL QSELENSQKE SRGYSAELYR IKASIEEYQD SIGALRRENK
NLADEIHDLT DQLSEGGRST HELDKARRRL EMEKEELQAA LEEAEGALEQ EEAKVMRAQL
EIATVRNEID KRIQEKEEEF DNTRRNHQRA LESMQASLEA EAKGKADAMR IKKKLEQDIN
ELEVALDASN RGKAEMEKTV KRYQQQIREM QTSIEEEQRQ RDEARESYNM AERRCTLMSG
EVEELRAALE QAERARKASD NELADANDRV NELTSQVSSV QGQKRKLEGD INAMQTDLDE
MHGELKGADE RCKKAMADAA RLADELRAEQ DHSNQVEKVR KNLESQVKEF QIRLDEAEAS
SLKGGKKMIQ KLESRVHELE AELDNEQRRH AETQKNMRKA DRRLKELAFQ ADEDRKNQER
LQELIDKLNA KIKTFKRQVE EAEEIAAINL AKYRKAQHEL EEAEERADTA DSTLQKFRAK
SRSSVSVQRS SVSVSASN
