MYH4_PIG
ID MYH4_PIG Reviewed; 1937 AA.
AC Q9TV62;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Myosin-4;
DE AltName: Full=Myosin heavy chain 2b;
DE Short=MyHC-2b;
DE AltName: Full=Myosin heavy chain 4;
DE AltName: Full=Myosin heavy chain, skeletal muscle, fetal;
GN Name=MYH4;
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. {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-4 (MYO4). {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; AB025261; BAA82145.1; -; mRNA.
DR RefSeq; NP_001116613.1; NM_001123141.1.
DR AlphaFoldDB; Q9TV62; -.
DR SMR; Q9TV62; -.
DR PeptideAtlas; Q9TV62; -.
DR PRIDE; Q9TV62; -.
DR ABCD; Q9TV62; 1 sequenced antibody.
DR Ensembl; ENSSSCT00000061472; ENSSSCP00000047526; ENSSSCG00000029441.
DR Ensembl; ENSSSCT00070003219; ENSSSCP00070002664; ENSSSCG00070001491.
DR GeneID; 100144306; -.
DR KEGG; ssc:100144306; -.
DR CTD; 4622; -.
DR GeneTree; ENSGT00940000154760; -.
DR InParanoid; Q9TV62; -.
DR OMA; DEQANTH; -.
DR OrthoDB; 47111at2759; -.
DR Proteomes; UP000008227; Chromosome 12.
DR Proteomes; UP000314985; Chromosome 12.
DR Bgee; ENSSSCG00000029441; Expressed in skeletal muscle tissue and 32 other tissues.
DR ExpressionAtlas; Q9TV62; 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; 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-4"
FT /id="PRO_0000274174"
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 1116..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 841..1937
FT /evidence="ECO:0000255"
FT COMPBIAS 1116..1153
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 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 755
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 774
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
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 1263
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1276
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 1286
FT /note="Phosphoserine"
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 1598
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 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; 223236 MW; BBC114C6824E0426 CRC64;
MSSDQEMAIF GEAAPYLRKS EKERIEAQNK PFDAKTSVFV AEPKESFVKG TVQSREGGKV
TVKTEAGATL TVKEDQVFPM NPPKFDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNAEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEP TPGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPEL
IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELMATDSAIE ILGFTSDERV SIYKLTGAVM
HYGNLKFKQK QREEQAEPDG TEVADKAAYL QGLNSADLLK ALCYPRVKVG NEFVTKGQTV
QQVYNAVGAL AKAVYDKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKAEAHF SLIHYAGTVD YNITGWLDKN
KDPLNETVVG LYQKSSVKTL AFLFAERQSS EEGGTKKGGK KKGSSFQTVS ALFRENLNKL
MTNLRSTHPH FVRCIIPNET KTPGAMEHEL VLHQLRCNGV LEGIRICRKG FPSRILYADF
KQRYKVLNAS AIPEGQFIDS KKASEKLLGS IDIDHTQYKF GHTKVFFKAG LLGTLEEMRD
EKLAQLITRT QAMCRGFLMR VEFRKMMERR ESIFCIQYNI RAFMNVKHWP WMKLYFKIKP
LLKSAETEKE MANMKEEFEK TKEDLAKSEA KRKELEEKMV ALMQEKNDLQ LQVQAEADGL
ADAEERCDQL IKTKIQLEAK IKEVTERAED EEEINAELTA KKRKLEDECS ELKKDIDDLE
LTLAKVEKEK HATENKVKNL TEEMAGLDEN IAKLTKEKKA LQEAHQQTLD DLQAEEDKVN
TLTKAKTKLE QQVDDLEGSL EQEKKLRMDL ERAKRKLEGD LKLAQESTMD IENDKQQLDE
KLKKKEFEMS NLQSKIEDEQ ALAMQLQKKI KELQARTEEL EEEIEAERAS RAKAEKQRSD
LSRELEEISE RLEEAGGATS AQIEMNKKRE AEFQKMRRDL EEATLQHEAT AAALRKKHAD
SVAELGEQID NLQRVKQKLE KEKSELKMEI DDLASNMETV SKAKGNLEKM CRTLEDQLSE
VKTKEEEHQR LINELSAQKA RLQTESGEFS RQLDEKEALV SQLSRGKQAF TQQIEELKRQ
LEEETKAKSA LAHAVQSSRH DCDLLREQYE EEQEAKAELQ RAMSKANSEV AQWRTKYETD
AIQRTEELEE AKKKLAQRLQ DAEEHVEAVN AKCASLEKTK QRLQNEVEDL MLDVERSNAA
CAALDKKQRN FDKILAEWKH KYEETQAELE ASQKESRSLS TELFKVKNAY EESLDQLETL
KRENKNLQQE ISDLTEQIAE GGKHIHELEK VKKQIEQEKS ELQAALEEAE ASLEHEEGKI
LRIQLELNQV KSEIDRKIAE KDEEIDQMKR NHIRVVESMQ STLDAEIRSR NDALRIKKKM
EGDLNEMEIQ LNHANRQATE AIRNLRNTQG VLKDTQLHLD DAIRGQDDLK EQLAMVERRA
NLMQAEIEEL RASLEQTERS RRVAEQELLD ASERVQLLHT QNTSLINTKK KLETDISQIQ
GEMEDIVQEA RNAEEKAKKA ITDAAMMAEE LKKEQDTSAH LERMKKNMEQ TVKDLQHRLD
EAEQLALKGG KKQIQKLEAR VRELENEVEN EQKRNVEAVK GLRKHERRVK ELTYQTEEDR
KNVLRLQDLV DKLQSKVKAY KRQAEEAEEQ SNVNLSKFRK LQHELEEAEE RADIAESQVN
KLRVKSREVH TKVISEE
