MYH2_BOVIN
ID MYH2_BOVIN Reviewed; 1940 AA.
AC Q9BE41;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 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. 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB059398; BAB40920.1; -; mRNA.
DR AlphaFoldDB; Q9BE41; -.
DR SMR; Q9BE41; -.
DR STRING; 9913.ENSBTAP00000012797; -.
DR BindingDB; Q9BE41; -.
DR ChEMBL; CHEMBL4680039; -.
DR PaxDb; Q9BE41; -.
DR PRIDE; Q9BE41; -.
DR ABCD; Q9BE41; 1 sequenced antibody.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; Q9BE41; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; IDA:CAFA.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0030017; C:sarcomere; IDA:CAFA.
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; -; 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; 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..1940
FT /note="Myosin-2"
FT /id="PRO_0000274165"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..783
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 786..815
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 660..682
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 762..776
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1886..1905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..1940
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 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 758
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1242
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1256
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1293
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 1307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1465
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1468
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1493
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1502
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1518
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1731
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1737
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
SQ SEQUENCE 1940 AA; 223319 MW; EE2642E1E29FDDC2 CRC64;
MSSDQEMAIF GEAAPYLRKS EKERIEAQNK PFDAKTSVFV AEPKESFVKG TIQSREGGKV
TVKTEGGATL TVKEDQVFPM NPPKFDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGDKKKEEI TSGKIQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QITSNRKPEL
IEMLLITTNP YDYPFISQGE ISVASIDDQE ELIATDSAID ILGFTNEEKV SIYKLTGAVM
HYGNLKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
EQVTNAVGAL AKAVYEKMFL WMVARINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKREGIE WTFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDMS FKNKLYDQHL GKSANFQKPK VVKGKPEAHF ALIHYAGVVD YNITGWLEKN
KDPLNDTVVG LYQKSALKTL AFLFSGTPTG DSEASGGTKK GGKKKGSSFQ TVSALFRENL
NKLMTNLRST HPHFVRCIIP NETKTPGAME HELVLHQLRC NGVLEGIRIC RKGFPSRILY
ADFKQRYKVL NASAIPEGQY IDSKKASEKL LASIDIDHTQ YKFGHTKVFF KAGLLGLLEE
MRDEKLAQLM TRTQARCRGF LARVEYQKMV ERRESIFCIQ YNIRAFMNVK HWPWMKLFFR
IKPLLKSAET EKEMATMKEE FQKTKDELAK SEAKRKELEE KMVTLLKEKN DLQLQVQSEA
EGLADAEERC DQLIKTKIQL EAKIKEVTER AEDEEEINAE LTAKKRKLED ECSELKKDID
DLELTLAKVE KEKHATENKV KNLTEEMAGL DETIAKLTKE KKALQEAHQQ TLDDLQAEED
KVNTLTKAKT KLEQQVDDLE GSLEQEKKLR MDLERAKRKL EGDLKLAQES IMDIENEKQQ
LDEKLKKKEF EISNLQSKIE DEQALGIQLQ KKIKELQARI EELEEEIEAE RASRAKAEKQ
RSDLSRELEE ISERLEEAGG ATSAQIEMNK KREAEFQKMR RDLEEATLQH EATAAALRKK
HADSVAELGE QIDNLQRVKQ KLEKEKSEMK MEIDDLASNV ETISKAKGNL EKMCRTLEDQ
VNELKSKEEE QQRLINDLTT QRGRLQTESG EFSRQLDEKE ALVSQLSRGK QAFTQQIEEL
KRQLEEEIKA KNALAHGLQS ARHDCDLLRE QYEEEQESKA ELQRALSKAN TEVAQWRTKY
ETDAIQRTEE LEEAKKKLAQ RLQAAEEHVE AVNAKCASLE KTKQRLQNEV EDLMLDVERT
NAACAALDKK QRNFDKILAE WKQKYEETHA ELEAAQKEAR SLGTELFKMK NAYEESLDQL
ETLKRENKNL QQEISDLTEQ IAEGGKRMHE LEKIKKQVEQ EKSEIQAALE EAEASLEHEE
GKILRIQLEL NQVKSEIDRK IAEKDEEIDQ LKRNHIRVVE SMQTMLDAEI RSRNDAIRLK
KKMEGDLNEM EIQLNHANRM AAEALKNYRN TQAILKDTQI HLDDALRGQE DLKEQLAMVE
RRANLLQAEI EELRATLEQT ERSRKIAEQE LLDASERVQL LHTQNTSLIN TKKKLETDIT
QIQGEMEDIL QEARNAEEKA KKAITDAAMM AEELKKEQDT SAHLERMKKN MEQTVKDLQN
RLDEAEQLAL KGGKKQIQKL EARVRELEGE VESEQKRNVE AVKGLRKHER RVKELTYQTE
EDRKNILRLQ DLVDKLQAKV KSYKRQAEEA EEQSNTNLSK FRKLQHELEE AEERADIAES
QVNKLRVKSR EVHTKIISEE
