MYH2_PIG
ID MYH2_PIG Reviewed; 1939 AA.
AC Q9TV63;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Landrace; TISSUE=Skeletal muscle;
RX AGRICOLA=IND22089526; DOI=10.1016/S0309-1740(00)00107-8;
RA Chikuni K., Tanabe R., Muroya S., Nakajima I.;
RT "Differences in molecular structure among the porcine myosin heavy chain-
RT 2a, -2x, and -2b isoforms.";
RL Meat Sci. 57:311-317(2001).
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; AB025260; BAA82144.1; -; mRNA.
DR RefSeq; NP_999301.1; NM_214136.1.
DR AlphaFoldDB; Q9TV63; -.
DR SMR; Q9TV63; -.
DR BioGRID; 1149388; 1.
DR STRING; 9823.ENSSSCP00000019078; -.
DR BindingDB; Q9TV63; -.
DR ChEMBL; CHEMBL4680041; -.
DR PaxDb; Q9TV63; -.
DR PeptideAtlas; Q9TV63; -.
DR PRIDE; Q9TV63; -.
DR ABCD; Q9TV63; 1 sequenced antibody.
DR GeneID; 397256; -.
DR KEGG; ssc:397256; -.
DR CTD; 4620; -.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; Q9TV63; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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..1939
FT /note="Myosin-2"
FT /id="PRO_0000274168"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..782
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 785..814
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 659..681
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 761..775
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1126..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 843..1939
FT /evidence="ECO:0000255"
FT COMPBIAS 1901..1915
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 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 757
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1255
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1286
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1464
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1467
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1492
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1501
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1517
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1730
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1736
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
SQ SEQUENCE 1939 AA; 223150 MW; B520182094179343 CRC64;
MSSDQEMAIF GEAAPYLRKS EKERIEAQNR PFDAKTSVFV AEPKESFVKG TIQSREGGKV
TVKTEAGATL TVKEDQVFPM NPPKFDKIED MAMMTHLHEP GVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEP TSGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QITSNRKPEL
IEMLLITTNP YDYPFISQGE ISVASIDDQE ELIATDSAID ILGFTNEEKV SIYKLTGAVM
HYGNLKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
EQVTNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKREGIE WTFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSANFQKPK PAKGKVEAHF SLIHYAGTVD YNITGWLDKN
KDPLNDTVVG LYQKSALKTL AFLFSGAQTG EAEAGGTKKG GKKKGSSFQT VSALFRENLN
KLMTNLRSTH PHFVRCIIPN ETKTPGAMEH ELVLHQLRCN GVLEGIRICR KGFPSRILYA
DFKQRYKVLN ASAIPEGQYI DSKKASEKLL ASIDIDHTQY KFGHTKVFFK AGLLGLLEEM
RDDKLAQLIT RTQARCRGFL ARVEYQKMVE RRESIFCIQY NIRAFMNVKH WPWMKLFFKI
KPLLKSAESE KEMATMKEEF QKTKDELAKS EAKRKELEEK MVTLLKEKND LQLQVQAEAE
GLADAEERCD QLIKTKIQLE AKIKEVTERA EDEEEINAEL TAKKRKLEDE CSELKKDIDD
LELTLAKVEK EKHATENKVK NLTEEMAGLD ETIAKLTKEK KALQEAHQQT LDDLQAEEDK
VNTLTKAKTK LEQQVDDLEG SLEQEKKLRM DLERAKRKLE GDLKLAQESI MDIENEKQQL
DEKLKKKEFE ISNLQSKIED EQALAIQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR
SDLSRELEEI SERLEEAGGA TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAAALRKKH
ADSVAELGEQ IDNLQRVKQK LEKEKSEMKM EIDDLASNME TVSKAKGNLE KMCRTLEDQL
SELKSKEEEQ QRLINDLTAQ RGRLQTESGE FSRQLDEKEA LVSQLSRGKQ AYTQQIEELK
RQLEEEIKAK NALAHALQSS RHDCDLLREQ YEEEQESKAE LQRALSKANT EVAQWRTKYE
TDAIQRTEEL EEAKKKLAQR LQAAEEHVEA VNAKCASLEK TKQRLQNEVE DLMLDVERTN
AACAALDKKQ RNFDKILAEW KQKYEETHAE LEASQKEARS LGTELFKMKN AYEESLDQLE
TLKRENKNLQ QEISDLTEQI AEGGKRIHEL EKIKKQVEQE KSEIQAALEE AEASLEHEEG
KILRIQLELN QVKSEVDRKI AEKDEEIDQL KRNHVRVVES MQSMLDAEIR SRNDAIRLKK
KMEGDLNEME IQLNHANRMA AEALRNYRNT QGILKDTQIH LDDALRGQED LKEQLAMVER
RANLLQAEIE ELRATLEQTE RSRKVAEQEL LDASERVQLL HTQNTSLINT KKKLETDISQ
MQGEMEDILQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNM EQTVKDLQHR
LDEAEQLALK GGKKQIQKLE ARVRELEGEV ESEQKRNAEA VKGLRKHERR VKELTYQTEE
DRKNILRLQD LVDKLQAKVK SYKRQAEEAE EQSNTNLSKF RKLQHELEEA EERADIAESQ
VNKLRVKSRE VHTKVISEE
