ID   MYH3_MOUSE              Reviewed;        1940 AA.
AC   P13541; Q3V183; Q5SUD4;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Myosin-3;
DE   AltName: Full=Myosin heavy chain 3;
GN   Name=Myh3; Synonyms=Myhse;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 523-1292.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1747-1905.
RX   PubMed=3864153; DOI=10.1073/pnas.82.21.7183;
RA   Weydert A., Daubas P., Lazaridis I., Barton P., Garner I., Leader D.P.,
RA   Bonhomme F., Catalan J., Simon D., Guenet J.-L., Gros F., Buckingham M.E.;
RT   "Genes for skeletal muscle myosin heavy chains are clustered and are not
RT   located on the same mouse chromosome as a cardiac myosin heavy chain
RT   gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:7183-7187(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; AL596129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL645988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK132623; BAE21268.1; -; mRNA.
DR   EMBL; M11154; AAA39791.1; -; mRNA.
DR   CCDS; CCDS36184.1; -.
DR   PIR; A24733; A24733.
DR   RefSeq; NP_001093105.1; NM_001099635.1.
DR   RefSeq; XP_006532475.1; XM_006532412.1.
DR   AlphaFoldDB; P13541; -.
DR   SMR; P13541; -.
DR   BioGRID; 201647; 26.
DR   IntAct; P13541; 14.
DR   STRING; 10090.ENSMUSP00000104329; -.
DR   GlyGen; P13541; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P13541; -.
DR   PhosphoSitePlus; P13541; -.
DR   MaxQB; P13541; -.
DR   PaxDb; 10090-ENSMUSP00000104329; -.
DR   PeptideAtlas; P13541; -.
DR   ProteomicsDB; 287528; -.
DR   Antibodypedia; 12917; 131 antibodies from 29 providers.
DR   Ensembl; ENSMUST00000007301.14; ENSMUSP00000007301.8; ENSMUSG00000020908.15.
DR   Ensembl; ENSMUST00000108689.8; ENSMUSP00000104329.2; ENSMUSG00000020908.15.
DR   Ensembl; ENSMUST00000165221.2; ENSMUSP00000131883.2; ENSMUSG00000020908.15.
DR   GeneID; 17883; -.
DR   KEGG; mmu:17883; -.
DR   UCSC; uc007jlx.1; mouse.
DR   AGR; MGI:1339709; -.
DR   CTD; 4621; -.
DR   MGI; MGI:1339709; Myh3.
DR   VEuPathDB; HostDB:ENSMUSG00000020908; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   GeneTree; ENSGT00940000161575; -.
DR   HOGENOM; CLU_000192_8_0_1; -.
DR   InParanoid; P13541; -.
DR   OMA; HANKANE; -.
DR   OrthoDB; 2877572at2759; -.
DR   PhylomeDB; P13541; -.
DR   TreeFam; TF314375; -.
DR   Reactome; R-MMU-390522; Striated Muscle Contraction.
DR   BioGRID-ORCS; 17883; 6 hits in 77 CRISPR screens.
DR   PRO; PR:P13541; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P13541; Protein.
DR   Bgee; ENSMUSG00000020908; Expressed in extra-ocular muscle and 70 other cell types or tissues.
DR   GO; GO:0043292; C:contractile fiber; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IDA:MGI.
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:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; ISO:MGI.
DR   GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR   GO; GO:0003009; P:skeletal muscle contraction; ISO:MGI.
DR   CDD; cd14913; MYSc_Myh3; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 5.
DR   Gene3D; 1.20.5.370; -; 4.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.10.250.2420; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF6; MYOSIN-3; 1.
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; SSF90257; Myosin rod fragments; 4.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
DR   Genevisible; P13541; MM.
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   Reference proteome; Thick filament.
FT   CHAIN           1..1940
FT                   /note="Myosin-3"
FT                   /id="PRO_0000123395"
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                   /evidence="ECO:0000250"
FT   REGION          758..772
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1260..1289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          841..1928
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"
FT   CONFLICT        1747
FT                   /note="R -> Q (in Ref. 3; AAA39791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1858
FT                   /note="D -> A (in Ref. 3; AAA39791)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1940 AA;  223791 MW;  9CF748702D8353C9 CRC64;
     MSSDTEMEVF GIAAPFLRKS EKERIEAQNQ PFDAKTYCFV VDSKEEYVKG KIKSSQDGKV
     TVETEDSRTL VVKPEDVYAM NPPKFDKIED MAMLTHLNEP AVLYNLKDRY TSWMIYTYSG
     LFCVTVNPYK WLPVYNPEVV DGYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA ATGDLAKKKD SKMKGTLEDQ IISANPLLEA FGNAKTVRND
     NSSRFGKFIR IHFGTTGKLA SADIETYLLE KSRVTFQLKA ERSYHIFYQI LSNKKPELIE
     LLLITTNPYD YPFISQGEIL VASIDDAEEL 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 VHYAGTVDYS 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
     RGKNEEMQRS 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
     EVEDACRDAR NAEEKAKKAI TDAAMMAEEL KKEQDTSAHL ERMKKNLEQT VKDLQHRLDE
     AEQLALKGGK KQIQKLETRI RELEFELEGE QKRNTESVKG LRKYERRVKE LTYQSEEDRK
     NVLRLQDLVD KLQVKVKSYK RQAEEADEQA NAHLTKFRKA QHELEEAEER ADIAESQVNK
     LRAKTRDFTS SRMVVHESEE
//