MYH1_BOVIN
ID MYH1_BOVIN Reviewed; 1938 AA.
AC Q9BE40;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein; TISSUE=Skeletal muscle;
RX AGRICOLA=IND43619651; DOI=10.1016/j.meatsci.2003.09.011;
RA Chikuni K., Muroya S., Nakajima I.;
RT "Myosin heavy chain isoforms expressed in bovine skeletal muscles.";
RL Meat Sci. 67:87-94(2004).
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; AB059399; BAB40921.2; -; mRNA.
DR RefSeq; NP_776542.1; NM_174117.1.
DR RefSeq; XP_010814282.1; XM_010815980.2.
DR AlphaFoldDB; Q9BE40; -.
DR SMR; Q9BE40; -.
DR STRING; 9913.ENSBTAP00000009327; -.
DR PaxDb; Q9BE40; -.
DR PRIDE; Q9BE40; -.
DR Ensembl; ENSBTAT00000009327; ENSBTAP00000009327; ENSBTAG00000018204.
DR GeneID; 281337; -.
DR KEGG; bta:281337; -.
DR CTD; 4619; -.
DR VEuPathDB; HostDB:ENSBTAG00000018204; -.
DR VGNC; VGNC:55851; MYH1.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000163211; -.
DR HOGENOM; CLU_000192_8_1_1; -.
DR InParanoid; Q9BE40; -.
DR OMA; TWDWFLL; -.
DR OrthoDB; 47111at2759; -.
DR TreeFam; TF314375; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000018204; Expressed in biceps femoris and 69 other tissues.
DR ExpressionAtlas; Q9BE40; baseline and differential.
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:0003725; F:double-stranded RNA binding; IEA:Ensembl.
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_0000274161"
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 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1264
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1285
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1287
FT /note="Phosphoserine"
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 1599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1602
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"
SQ SEQUENCE 1938 AA; 222990 MW; 2E965FDA6FF50DC6 CRC64;
MSSDQEMAVF GEAAPYLRKS EKERIEAQNK PFDAKTSVFV ADPKESFVKA TVQSREGGKV
TAKTEAGATV TVKEDQVFPM NPPKFDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNAEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEP TSGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPEL
IEMLLITTNP YDYAYVSQGE ITVPSIDDQE ELMATDSAIE ILGFTSDERV SIYKLTGAVM
HYGNLKFKQK QREEQAEPDG TEVADKAAYL QGLNSADLLK ALCYPRVKVG NEFVTKGQTV
EQVYNAVGAL AKAVYDKMFL WMVARINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDMS FKNKLYEQHL GKSNNFQKPK PAKGKAEAHF SLIHYAGTVD YNITGWLDKN
KDPLNETVVG LYQKSSVKTL ALLFSGPASG EAEGGPKKGG KKKGSSFQTV SALFRENLNK
LMTNLRSTHP HFVRCIIPNE TKTPGAMEHE LVLHQLRCNG VLEGIRICRK GFPSRILYAD
FKQRYKVLNA SAIPEGQFID SKKASEKLLA SIDVDHTQYK FGHTKVFFKA GLLGLLEEMR
DEKLAQLITR TQARCRGFLA RVEYQKMVER RESIFCIQYN VRAFMNVKHW PWMKLYFKIK
PLLKSAETEK EMANMKEEFE KTKEELAKSE AKRKELEEKM VTLTQEKNDL QLQVQSEADA
LADAEERCDQ LIKTKIQLEA KIKEVTERAE 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 MCRALEDQLS
ELKTKEDEQQ RLINDLTTQR ARLQTESGEF SRQLDEKDAL VSQLSRGKQA FTQQIEELKR
QLEEEIKAKS ALAHALQSAR HDCDLLREQY EEEQEGKAEL QRAMSKANSE VAQWRTKYET
DAIQRTEELE EAKKKLAQRL QDAEEHVEAV NAKCASLEKT KQRLQNEVED LMIDVERTNA
ACAALDKKQR NFDKILSEWK QKYEETHAEL EASQKESRSL STELFKIKNA YEESLDQLET
LKRENKNLQQ EISDLTEQIA EGGKRIHELE KVKKQVEQEK SEIQAALEEA EASLEHEEGK
ILRIQLELNQ VKSEIDRKIA EKDEEIDQLK RNHIRIVESM QSTLDAEIRS RNDAIRLKKK
MEGDLNEMEI QLNHANRMAA EALKNYRSTQ AILKDTQIHL DDALRGQEDL KEQLAMVERR
ANLLQAEIEE LRATLEQTER SRKIAEQELL DASERVQLLH TQNTSLINTK KKLETDITQI
QGEMEDIIQE ARNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNLE QTVKDLQHRL
DEAEQLALKG GKKQIQKLEA RVRELEGEVE SEQKRNVEAV KGLRKHERRV KELTYQTEED
RKNILRLQDL VDKLQAKVKS YKRQAEEAEE QSNVNLSKFR KLQHELEEAE ERADIAESQV
NKLRVKSREV HTKIISEE
