MYH1_HORSE
ID MYH1_HORSE Reviewed; 1938 AA.
AC Q8MJV0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Myosin-1;
DE AltName: Full=Myosin heavy chain 1;
DE AltName: Full=Myosin heavy chain 2x;
DE Short=MyHC-2x;
DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 1;
GN Name=MYH1;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Thoroughbred; TISSUE=Skeletal muscle;
RA Chikuni K., Nakajima I., Muroya S.;
RT "Sequencing of the horse myosin heavy chain isoforms.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Muscle contraction. {ECO:0000250}.
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril {ECO:0000250}. Note=Thick
CC filaments of the myofibrils. {ECO:0000250}.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
CC meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
CC cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment
CC (S2). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents a conventional myosin. This protein should not be
CC confused with the unconventional myosin-1 (MYO1). {ECO:0000305}.
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DR EMBL; AB088366; BAC05680.1; -; mRNA.
DR RefSeq; NP_001075228.1; NM_001081759.1.
DR RefSeq; XP_005597093.1; XM_005597036.2.
DR AlphaFoldDB; Q8MJV0; -.
DR SMR; Q8MJV0; -.
DR STRING; 9796.ENSECAP00000031274; -.
DR PaxDb; Q8MJV0; -.
DR PRIDE; Q8MJV0; -.
DR Ensembl; ENSECAT00000026554; ENSECAP00000022162; ENSECAG00000022909.
DR GeneID; 791235; -.
DR KEGG; ecb:791235; -.
DR CTD; 4619; -.
DR VGNC; VGNC:56450; MYH1.
DR GeneTree; ENSGT00940000154760; -.
DR HOGENOM; CLU_000192_8_1_1; -.
DR InParanoid; Q8MJV0; -.
DR OMA; TWDWFLL; -.
DR OrthoDB; 47111at2759; -.
DR Proteomes; UP000002281; Chromosome 11.
DR Bgee; ENSECAG00000022909; Expressed in triceps brachii and 6 other tissues.
DR ExpressionAtlas; Q8MJV0; baseline.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR Gene3D; 1.20.5.370; -; 4.
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 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Methylation; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Thick filament.
FT CHAIN 1..1938
FT /note="Myosin-1"
FT /id="PRO_0000274163"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..781
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 784..813
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 658..680
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 760..774
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1124..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 842..1938
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 130
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT MOD_RES 389
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 424
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 756
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1285
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1463
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1491
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1500
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1729
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1735
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
SQ SEQUENCE 1938 AA; 222941 MW; 049A535E6D438341 CRC64;
MSSDQEMAIF GEAAPYLRKS EKERIEAQNK PFDAKTSVFV ADPKESFVKA TVQSREGGKV
TAKTEAGATV TVKEDQCFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNAEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEP TSGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPDL
IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELMATDSAIE ILGFTSDERV SIYKLTGAVM
HYGNLKFKQK QREEQAEPDG TEVADKAAYL QGLNSADLLK ALCYPRVKVG NEFVTKGQTV
EQVYNAVGAL AKAVYDKMFL WMVARINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PVKGKPEAHF SLIHYAGTVD YNITGWLDKN
KDPLNETVVG LYQKSSVKTL ALLFSGPASA DAEAGGKKGG KKKGSSFQTV SALFRENLNK
LMTNLRSTHP HFVRCIIPNE TKTPGAMEHE LVLHQLRCNG VLEGIRICRK GFPSRILYAD
FKQRYKVLNA SAIPEGQFID SKKASEKLLG SIDIDHTQYK FGHTKVFFKA GLLGLLEEMR
DDKLAQIITR TQARCRGFLA RVEYQRMVER RESIFCIQYN VRAFMNVKHW PWMKLYFKIK
PLLKSAETEK EMANMKEEFE KTKESLAKAE AKRKELEEKM VALMQEKNDL QLQVQAEADS
LADAEERCDQ LIKTKIQLEA KIKEATERAE DEEEINAELT AKKRKLEDEC SELKKDIDDL
ELTLAKVEKE KHATENKVKN LTEEMAGLDE TIAKLTKEKK ALQEAHQQTL DDLQAEEDKV
NTLTKAKTKL EQQVDDLEGS LEQEKKLRMD LERAKRKLEG DLKLAQESTM DIENDKQQLD
EKLKKKEFEM SNLQSKIEDE QALAMQLQKK IKELQARIEE LEEEIEAERA SRAKAEKQRS
DLSRELEEIS ERLEEAGGAT SAQIEMNKKR EAEFQKMRRD LEEATLQHEA TAAALRKKHA
DSVAELGEQI DNLQRVKQKL EKEKSEMKME IDDLASNMET VSKAKGNLEK MCRTLEDQLS
ELKSKEEEQQ RLVNDLTGQR ARLQTEAGEY SRQLDEKDSL VSQLSRGKQA FTQQIEELKR
QLEEEIKAKS ALAHALQSAR HDCDLLREQY EEEQEAKAEL QRAMSKANSE VAQWRTKYET
DAIQRTEELE EAKKKLAQRL QDAEEHVEAV NAKCASLEKT KQRLQNEVED LMIDVERTNA
ACAALDKKQR NFDKILSEWK HKYEETHAEL EASQKESRSL STELFKVKNA YEESLDQLET
LKRENKNLQQ EISDLTEQIA EGGKRIHELE KVKKQIEQEK SEIQAALEEA EASLEHEEGK
ILRIQLELNQ VKSEIDRKIA EKDEEIDQLK RNHVRVVETM QTMLDAEIRS RNDAIRIKKK
MEGDLNEMEI QLNHANRMAA EALRNYRNTQ GILKDTQLHL DDALRGQEDL KEQLAMVERR
ANLLQAEIEE LRATLEQTER SRKIAEQELL DASERVQLLH TQNTSLINTK KKLETDISQL
QGEMEDIVQE AHNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNLE QTVKDLQHRL
DEAEQLALKG GKKQIQKLEA RVRDLEGEVE SEQKRNVEAV KGLRKHERRV KELTYQTEED
RKNILRLQDL VDKLQSKVKA YKRQAEEAEE QSNVNLSKFR KIQHELEEAE ERADIAESQV
NKLRVKSREV HTKIISEE
