MYH4_RAT
ID MYH4_RAT Reviewed; 1939 AA.
AC Q29RW1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Myosin-4;
DE AltName: Full=Myosin heavy chain 2b;
DE Short=MyHC-2b;
DE AltName: Full=Myosin heavy chain 4;
GN Name=Myh4 {ECO:0000312|RGD:3139};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-64; THR-69; SER-79;
RP TYR-389; THR-391; SER-392; THR-419; TYR-424; SER-625; THR-776; SER-1092;
RP SER-1096; SER-1162; SER-1237; THR-1241; SER-1243; THR-1255; SER-1261;
RP THR-1265; SER-1278; THR-1286; SER-1288; SER-1292; SER-1303; SER-1306;
RP SER-1413; TYR-1464; THR-1467; SER-1474; TYR-1492; SER-1495; THR-1501;
RP SER-1514; THR-1517; SER-1542; SER-1547; SER-1554; SER-1574; SER-1600;
RP SER-1603; SER-1714; SER-1726; THR-1730; THR-1736 AND SER-1739, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Muscle contraction. {ECO:0000305}.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
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. {ECO:0000305}.
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}.
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DR EMBL; BC113948; AAI13949.1; -; mRNA.
DR RefSeq; NP_062198.1; NM_019325.1.
DR AlphaFoldDB; Q29RW1; -.
DR SMR; Q29RW1; -.
DR BioGRID; 262010; 2.
DR IntAct; Q29RW1; 1.
DR STRING; 10116.ENSRNOP00000046362; -.
DR iPTMnet; Q29RW1; -.
DR PhosphoSitePlus; Q29RW1; -.
DR jPOST; Q29RW1; -.
DR PaxDb; Q29RW1; -.
DR PRIDE; Q29RW1; -.
DR ABCD; Q29RW1; 1 sequenced antibody.
DR GeneID; 360543; -.
DR KEGG; rno:360543; -.
DR UCSC; RGD:3139; rat.
DR CTD; 4622; -.
DR RGD; 3139; Myh4.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; Q29RW1; -.
DR OrthoDB; 47111at2759; -.
DR PRO; PR:Q29RW1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; ISO:RGD.
DR GO; GO:0061061; P:muscle structure development; IEP:RGD.
DR GO; GO:0014823; P:response to activity; ISO:RGD.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR GO; GO:0035994; P:response to muscle stretch; IEP:RGD.
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 1: Evidence at protein 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-4"
FT /id="PRO_0000240600"
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 1128..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 COILED 843..1939
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 130
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT MOD_RES 389
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 424
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 757
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 776
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1241
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1255
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1265
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1286
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1464
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1467
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1492
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1501
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1517
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1730
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1736
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1939 AA; 222880 MW; D875C3B566DE8151 CRC64;
MSSDAEMAVF GEAAPYLRKS EKERIEAQNK PFDAKSSVFV VDAKESYVKA TVQSREGGKV
TAKTEGGATV TVKEDQVFSM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV AAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGDKKKEEA PSGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGATGK LASADIETYL LEKSRVTFQL KAERSYHIFY QVMSNKKPEL
IEMLLITTNP YDFAYVSQGE ITVPSIDDQE ELMATDTAVD ILGFTADEKV AIYKLTGAVM
HYGNMKFKQK QREEQAEPDG TEVADKAAYL TSLNSADLLK ALCYPRVKVG NEYVTKGQTV
QQVYNSVGAL AKAMYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNTLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKAEAHF SLVHYAGTVD YNIIGWLDKN
KDPLNETVVG LYQKSGLKTL AFLFSGGQAA EAEGGGGKKG GKKKGSSFQT VSALFRENLN
KLMTNLKSTH PHFVRCLIPN ETKTPGAMEH ELVLHQLRCN GVLEGIRICR KGFPSRILYA
DFKQRYKVLN ASAIPEGQFI DSKKASEKLL GSIDIDHTQY KFGHTKVFFK AGLLGTLEEM
RDEKLAQLIT RTQAVCRGYL MRVEFRKMME RRESIFCIQY NVRAFMNVKH WPWMKLYFKI
KPLLKSAETE KEMATMKEDF EKAKEDLAKS EAKRKELEEK MVALMQEKND LQLQVQAEAD
GLADAEERCD QLIKTKIQLE AKIKELTERA EDEEEINAEL TAKKRKLEDE CSELKKDIDD
LELTLAKVEK EKHATENKVK NLTEEMAGLD ENIVKLTKEK KALQEAHQQT LDDLQAEEDK
VNTLTKAKTK LEQQVDDLEG SLEQEKKLRM DLERAKRKLE GDLKLAQEST MDIENDKQQL
DEKLKKKEFE MSNLQSKIED EQALGMQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR
SDLSRELEEI SERLEEAGGA TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAAALRKKH
ADSVAELGEQ IDNLQRVKQK LEKEKSELKM EIDDLASNME TVSKAKGNLE KMCRTLEDQL
SEVKTKEEEQ QRLINELSAQ KARLHTESGE FSRQLDEKDA MVSQLSRGKQ AFTQQIEELK
RQLEEESKAK NALAHALQSA RHDCDLLREQ YEEEQEAKAE LQRAMSKANS EVAQWRTKYE
TDAIQRTEEL EEAKKKLAQR LQDAEEHVEA VNSKCASLEK TKQRLQNEVE DLMIDVERSN
AACAALDKKQ RNFDKVLAEW KQKYEETQAE LEASQKESRS LSTELFKVKN AYEESLDQLE
TLKRENKNLQ QEISDLTEQI AEGGKHIHEL EKIKKQIDQE KSELQASLEE AEASLEHEEG
KILRIQLELN QVKSEIDRKI AEKDEEIDQL KRNHLRVVES MQSTLDAEIR SRNDALRIKK
KMEGDLNEME IQLNHANRQA AEAIRNLRNT QGMLKDTQLH LDDALRGQDD LKEQLAMVER
RANLMQAEIE ELRASLEQTE RSRRVAEQEL LDASERVQLL HTQNTSLINT KKKLETDISQ
IQGEMEDIVQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNM EQTVKDLQHR
LDEAEQLALK GGKKQIQKLE ARVRELENEV ENEQKRNIEA VKGLRKHERR VKELTYQTEE
DRKNVLRLQD LVDKLQTKVK AYKRQAEEAE EQSNVNLAKF RKIQHELEEA EERADIAESQ
VNKLRVKSRE VHTKVISEE
