MYH2_HORSE
ID MYH2_HORSE Reviewed; 1937 AA.
AC Q8MJV1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Myosin-2;
DE AltName: Full=Myosin heavy chain 2;
DE AltName: Full=Myosin heavy chain 2a;
DE Short=MyHC-2a;
DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 2;
GN Name=MYH2;
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. Required for cytoskeleton organization
CC (By similarity). {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). Interacts with GCSAM.
CC {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-2 (MYO2). {ECO:0000305}.
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DR EMBL; AB088365; BAC05679.1; -; mRNA.
DR RefSeq; NP_001075229.1; NM_001081760.1.
DR AlphaFoldDB; Q8MJV1; -.
DR SMR; Q8MJV1; -.
DR STRING; 9796.ENSECAP00000025956; -.
DR PaxDb; Q8MJV1; -.
DR ABCD; Q8MJV1; 1 sequenced antibody.
DR GeneID; 791236; -.
DR KEGG; ecb:791236; -.
DR CTD; 4620; -.
DR InParanoid; Q8MJV1; -.
DR OrthoDB; 47111at2759; -.
DR Proteomes; UP000002281; Unplaced.
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; 2.
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..1937
FT /note="Myosin-2"
FT /id="PRO_0000274167"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..780
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 783..812
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 657..679
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 759..773
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1124..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1883..1913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 841..1937
FT /evidence="ECO:0000255"
FT COMPBIAS 1899..1913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 387
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 755
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 1094
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1253
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1284
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1462
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1465
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1490
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1499
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1515
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1728
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1734
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
SQ SEQUENCE 1937 AA; 222748 MW; 4B00FA4246B41271 CRC64;
MSSDQEMAIF GEAAPYLRKS EKERIEAQNR PFDAKTSVFV AEPKESFVKG TIQSREGGKV
TVKTDAGATL TVKEDQVFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEP GKMQGTLEDQ IISANPLLEA FGNAKTVRND
NSSRFGKFIR IHFGTTGKLA SADIETYLLE KSRVTFQLKA ERSYHIFYQI TSNRKPELIE
MLLITTNPYD YPYVSQGEIS VASIDDQEEL IATDSAIDIL GFTNDEKVSI YKLTGAVMHY
GNLKFKQKQR EEQAEPDGTE VADKAAYLQG LNSADLLKAL CYPRVKVGNE FVTKGQTVEQ
VTNAVGALAK AVYDKMFLWM VARINQQLDT KQPRQYFIGV LDIAGFEIFD FNSLEQLCIN
FTNEKLQQFF NHHMFVLEQE EYKKEGIEWT FIDFGMDLAA CIELIEKPMG IFSILEEECM
FPKATDTSFK NKLYEQHLGK SSNFQKPKVV KGKAEAHFSL IHYAGVVDYN ITGWLDKNKD
PLNETVVGLY QKSSVKTLAL LFSGAQTADA EAGGVKKGGK KKGSSFQTVS ALFRENLNKL
MTNLRSTHPH FVRCIIPNET KTPGAMEHEL VLHQLRCNGV LEGIRICRKG FPSRILYADF
KQRYKVLNAS AIPEGQFIDS KKASEKLLAS IDIDHTQYKF GHTKVFFKAG LLGLLEEMRD
DKLAQIITRT QARCRGFLAR VEYQKMVERR ESIFCIQYNI RAFMNVKHWP WMKLFFRIKP
LLKSAETEKE MATMKEEFQK TKDELAKSEA KRKELEEKMV SLLKEKNDLQ LQVQSEAEGL
ADAEERCDQL IKTKIQLEAK IKEVTERAED EEEINAELTA KKRKLEDECS ELKKDIDDLE
LTLAKVEKEK HATENKVKNL TEEMAGLDET IAKLTKEKKA LQEAHQQTLD DLQAEEDKVN
TLTKAKTKLE QQVDDLEGSL EQEKKLRMDL ERAKRKLEGD LKLAQESIMD IENEKQQLDE
KLKKKEFEIG NLQSKIEDEQ ALGIQLQKKI KELQARIEEL EEEIEAERAS RAKAEKQRSD
LSRELEEISE RLEEAGGATS AQIEMNKKRE AEFQKMRRDL EEATLQHEAT AAALRKKHAD
SVAELGEQID NLQRVKQKLE KEKSEMKMEI DDLASNVETV SKAKGNLEKM CRTLEDQVSE
LKSKEEEQQR LINDLTAQRG RLQTEAGEFS RQLDEKEALV SQLSRGKQAF TQQIEELKRQ
LEEEIKAKNA LAHALQSSRH DCDLLREQYE EEQESKAELQ RALSKANSEV AQWRTKYETD
AIQRTEELEE AKKKLAQRLQ AAEEHVEAVN AKCASLEKTK QRLQNEVEDL MLDVERTNAA
CAALDKKQRN FDKILAEWKQ KYEETHAELE ASQKEARSLG TELFKMKNAY EESLDQLETL
KRENKNLQQE ISDLTEQIAE GGKRIHELEK IKKQVEQEKS ELQAALEEAE ASLEHEEGKI
LRIQLELNQV KSEIDRKIAE KDEEIDQLKR NHVRVVETMQ TMLDAEIRSR NDAIRIKKKM
EGDLNEMEIQ LNHANRMAAE ALRNYRNTQG ILKDTQLHLD DALRGQEDLK EQLAMVERRA
NLLQAEIEEL RATLEQTERS RKIAEQELLD ASERVQLLHT QNTSLINTKK KLETDISQLQ
GEMEDILQEA RNAEEKAKKA ITDAAMMAEE LKKEQDTSAH LERMKKNLEQ TVKDLQQRLD
EAEQLALKGG KKQIQKLEAR VRELEGEVES EQKRSAEAIK GLRKHERRVK ELTYQTEEDR
KNILRLQDLV DKLQAKVKSY KRQAEEAEEQ SNTNLSKFRK LQHELEEAEE RADIAESQVN
KLRVKSREVH TKIISEE
