MYH3_RAT
ID MYH3_RAT Reviewed; 1940 AA.
AC P12847;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Myosin-3;
DE AltName: Full=Myosin heavy chain 3;
DE AltName: Full=Myosin heavy chain, fast skeletal muscle, embryonic;
GN Name=Myh3;
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 [GENOMIC DNA].
RX PubMed=3783701; DOI=10.1016/0022-2836(86)90003-3;
RA Strehler E.E., Strehler-Page M.-A., Perriard J.-C., Periasamy M.,
RA Nadal-Ginard B.;
RT "Complete nucleotide and encoded amino acid sequence of a mammalian myosin
RT heavy chain gene. Evidence against intron-dependent evolution of the rod.";
RL J. Mol. Biol. 190:291-317(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168.
RX PubMed=2981212; DOI=10.1016/s0021-9258(18)89755-1;
RA Strehler E.E., Mahdavi V., Periasamy M., Nadal-Ginard B.;
RT "Intron positions are conserved in the 5' end region of myosin heavy-chain
RT genes.";
RL J. Biol. Chem. 260:468-471(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1453-1940.
RX PubMed=2999140; DOI=10.1016/s0021-9258(17)36337-8;
RA Periasamy M., Wydro R.M., Strehler-Page M.-A., Strehler E.E.,
RA Nadal-Ginard B.;
RT "Characterization of cDNA and genomic sequences corresponding to an
RT embryonic myosin heavy chain.";
RL J. Biol. Chem. 260:15856-15862(1985).
CC -!- FUNCTION: Muscle contraction.
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).
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.
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-3 (MYO3). {ECO:0000305}.
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DR EMBL; X04267; CAA27817.1; -; Genomic_DNA.
DR PIR; A24922; A24922.
DR RefSeq; NP_036736.1; NM_012604.1.
DR AlphaFoldDB; P12847; -.
DR SMR; P12847; -.
DR STRING; 10116.ENSRNOP00000004147; -.
DR iPTMnet; P12847; -.
DR PhosphoSitePlus; P12847; -.
DR jPOST; P12847; -.
DR PaxDb; P12847; -.
DR PRIDE; P12847; -.
DR GeneID; 24583; -.
DR KEGG; rno:24583; -.
DR UCSC; RGD:3138; rat.
DR CTD; 4621; -.
DR RGD; 3138; Myh3.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; P12847; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P12847; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR PRO; PR:P12847; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043292; C:contractile fiber; ISO:RGD.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; 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; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; ISO:RGD.
DR GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
DR GO; GO:0032502; P:developmental process; IEA:UniProt.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; ISO:RGD.
DR CDD; cd14913; MYSc_Myh3; 1.
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; IPR036000; MYSc_Myh3.
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 3: Inferred from homology;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Methylation; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW Reference proteome; Thick filament.
FT CHAIN 1..1940
FT /note="Myosin-3"
FT /id="PRO_0000123396"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..779
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 782..811
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 656..678
FT /note="Actin-binding"
FT REGION 758..772
FT /note="Actin-binding"
FT REGION 1260..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 840..1933
FT /evidence="ECO:0000255"
FT COMPBIAS 1269..1286
FT /note="Polar 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 130
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1940 AA; 223858 MW; B5D546A596E5A696 CRC64;
MSSDTEMEVF GIAAPFLRKS EKERIEAQNQ PFDAKTYCFV VDSKEEYAKG KIKSSQDGKV
TVETEDNRTL VVKPEDVYAM NPPKFDKIED MAMLTHLNEP AVLYNLKDRY TSWMIYTYSG
LFCVTVNPYK WLPVYTPEVV DGYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA ATGDLAKKKD SKMKGTLEDQ IISANPLLEA FGNAKTVRND
NSSRFGKFIR IHFGTTGKLA SADIETYLLE KSRVTFQLKA ERSYHIFYQI LSNKKPELIE
LLLITTNPYD YPFISQGEIL VASIDDREEL LATDSAIDIL GFTPEEKSGL YKLTGAVMHY
GNMKFKQKQR EEQAEPDGTE VADKTAYLMG LNSSDLLKAL CFPRVKVGNE YVTKGQTVDQ
VHHAVNALSK SVYEKLFLWM VTRINQQLDT KLPRQHFIGV LDIAGFEIFE YNSLEQLCIN
FTNEKLQQFF NHHMFVLEQE EYKKEGIEWT FIDFGMDLAA CIELIEKPMG IFSILEEECM
FPKATDTSFK NKLYDQHLGK SNNFQKPKVV KGKAEAHFSL IHYAGTVDYS VSGWLEKNKD
PLNETVVGLY QKSSNRLLAH LYATFATTDA DGGKKKVAKK KGSSFQTVSA LFRENLNKLM
SNLRTTHPHF VRCIIPNETK TPGAMEHSLV LHQLRCNGVL EGIRICRKGF PNRILYGDFK
QRYRVLNASA IPEGQFIDSK KACEKLLASI DIDHTQYKFG HTKVFFKAGL LGTLEEMRDE
RLAKLITRTQ AVCRGFLMRV EFQKMMQRRE SIFCIQYNIR AFMNVKHWPW MKLFFKIKPL
LKSAETEKEM ATMKEEFQKT KDELAKSEAK RKELEEKLVT LVQEKNDLQL QVQAESENLL
DAEERCDQLI KAKFQLEAKI KEVTERAEDE EEINAELTAK KRKLEDECSE LKKDIDDLEL
TLAKVEKEKH ATENKVKNLT EELAGLDETI AKLTREKKAL QEAHQQTLDD LQAEEDKVNS
LSKLKSKLEQ QVDDLESSLE QEKKLRVDLE RNKRKLEGDL KLAQESILDL ENDKQQLDER
LKKKDFEYSQ LQSKVEDEQT LSLQLQKKIK ELQARIEELE EEIEAERATR AKTEKQRSDY
ARELEELSER LEEAGGVTST QIELNKKREA EFLKLRRDLE EATLQHEATV ATLRKKHADS
AAELAEQIDN LQRVKQKLEK EKSEFKLEID DLSSSVESVS KSKANLEKIC RTLEDQLSEA
RGKNEETQRS LSELTTQKSR LQTEAGELSR QLEEKESIVS QLSRSKQAFT QQIEELKRQL
EEENKAKNAL AHALQSSRHD CDLLREQYEE EQEGKAELQR ALSKANSEVA QWRTKYETDA
IQRTEELEEA KKKLAQRLQD SEEQVEAVNA KCASLEKTKQ RLQGEVEDLM VDVERANSLA
AALDKKQRNF DKVLAEWKTK CEESQAELEA ALKESRSLST ELFKLKNAYE EALDQLETVK
RENKNLEQEI ADLTEQIAEN GKSIHELEKS RKQMELEKAD IQMALEEAEA ALEHEEAKIL
RIQLELTQVK SEIDRKIAEK DEEIEQLKRN YQRTVETMQG ALDAEVRSRN EAIRLKKKME
GDLNEIEIQL SHANRQAAET IKHLRSVQGQ LKDTQLHLDD ALRGQEDLKE QLAIVERRAN
LLQAEVEELR ATLEQTERAR KLAEQELLDS NERVQLLHTQ NTSLIHTKKK LETDLTQLQS
EVEDASRDAR NAEEKAKKAI TDAAMMAEEL KKEQDTSAHL ERMKKNLEQT VKDLQHRLDE
AEQLALKGGK KQIQKLETRI RELEFELEGE QKRNTESVKG LRKYERRVKE LTYQSEEDRK
NVLRLQDLVD KLQVKVKSYK RQAEEADEQA NVHLTKFRKA QHELEEAEER ADIAESQVNK
LRAKTRDFTS SRMVVHESEE
