ID   MYH1_MOUSE              Reviewed;        1942 AA.
AC   Q5SX40; Q32P18;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Myosin-1;
DE   AltName: Full=Myosin heavy chain 1;
DE   AltName: Full=Myosin heavy chain 2x;
DE            Short=MyHC-2x;
DE   AltName: Full=Myosin heavy chain, skeletal muscle, adult 1;
GN   Name=Myh1;
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].
RC   TISSUE=Thyroid;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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-1 (MYO1). {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; AL596129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC108329; AAI08330.1; -; mRNA.
DR   CCDS; CCDS24855.1; -.
DR   RefSeq; NP_109604.1; NM_030679.1.
DR   RefSeq; XP_017169807.1; XM_017314318.1.
DR   AlphaFoldDB; Q5SX40; -.
DR   SMR; Q5SX40; -.
DR   BioGRID; 201643; 14.
DR   IntAct; Q5SX40; 2.
DR   STRING; 10090.ENSMUSP00000117569; -.
DR   GlyGen; Q5SX40; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5SX40; -.
DR   PhosphoSitePlus; Q5SX40; -.
DR   EPD; Q5SX40; -.
DR   MaxQB; Q5SX40; -.
DR   PaxDb; 10090-ENSMUSP00000117569; -.
DR   ProteomicsDB; 287527; -.
DR   Pumba; Q5SX40; -.
DR   Antibodypedia; 4383; 232 antibodies from 28 providers.
DR   DNASU; 17879; -.
DR   Ensembl; ENSMUST00000018637.15; ENSMUSP00000018637.9; ENSMUSG00000056328.15.
DR   Ensembl; ENSMUST00000075734.6; ENSMUSP00000075147.6; ENSMUSG00000056328.15.
DR   Ensembl; ENSMUST00000124516.8; ENSMUSP00000117569.2; ENSMUSG00000056328.15.
DR   GeneID; 17879; -.
DR   KEGG; mmu:17879; -.
DR   UCSC; uc007jmg.1; mouse.
DR   AGR; MGI:1339711; -.
DR   CTD; 4619; -.
DR   MGI; MGI:1339711; Myh1.
DR   VEuPathDB; HostDB:ENSMUSG00000056328; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   GeneTree; ENSGT00940000154760; -.
DR   HOGENOM; CLU_000192_8_1_1; -.
DR   InParanoid; Q5SX40; -.
DR   OMA; CERMAKQ; -.
DR   OrthoDB; 2877572at2759; -.
DR   PhylomeDB; Q5SX40; -.
DR   TreeFam; TF314375; -.
DR   BioGRID-ORCS; 17879; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Myh1; mouse.
DR   PRO; PR:Q5SX40; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5SX40; Protein.
DR   Bgee; ENSMUSG00000056328; Expressed in masseter muscle and 97 other cell types or tissues.
DR   ExpressionAtlas; Q5SX40; baseline and differential.
DR   GO; GO:0031672; C:A band; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR   GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR   GO; GO:0005859; C:muscle myosin complex; ISO: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; 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   CDD; cd14910; MYSc_Myh1_mammals; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF2; MYOSIN-1; 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; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 5.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
DR   Genevisible; Q5SX40; MM.
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..1942
FT                   /note="Myosin-1"
FT                   /id="PRO_0000123392"
FT   DOMAIN          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          86..785
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          788..817
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          662..684
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          764..778
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1156..1175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          846..1942
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:0000250|UniProtKB:Q29RW1"
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         625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         760
FT                   /note="Pros-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28641"
FT   MOD_RES         1095
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1099
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1258
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1268
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1289
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1291
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1295
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         1309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1467
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1470
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1477
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1495
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1498
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1504
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1520
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1545
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1557
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1577
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         1606
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1717
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1729
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1733
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1739
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1742
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
SQ   SEQUENCE   1942 AA;  223342 MW;  946BBA18567A2FB0 CRC64;
     MSSDAEMAVF GEAAPYLRKS EKERIEAQNK PFDAKSSVFV VDAKESFVKA TVQSREGGKV
     TAKTEGGTTV TVKDDQVYPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYNAEVV AAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA VTGEKKKEEA TSGKMQGTLE DQIISANPLL EAFGNAKTVR
     NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPDL
     IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELMATDSAID ILGFTSDERV SIYKLTGAVM
     HYGNMKFKQK QREEQAEPDG TEVADKAAYL QNLNSADLLK ALCYPRVKVG NEYVTKGQTV
     QQVYNSVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
     INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
     CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKVEAHF SLVHYAGTVD YNIAGWLDKN
     KDPLNETVVG LYQKSSMKTL AYLFSGAAAA AEAESGGGGG KKGAKKKGSS FQTVSALFRE
     NLNKLMTNLR STHPHFVRCI IPNETKTPGA MEHELVLHQL RCNGVLEGIR ICRKGFPSRI
     LYADFKQRYK VLNASAIPEG QFIDSKKASE KLLGSIDIDH TQYKFGHTKV FFKAGLLGLL
     EEMRDDKLAQ LITRTQAMCR GYLARVEYQK MVERRESIFC IQYNVRAFMN VKHWPWMKLY
     FKIKPLLKSA ETEKEMANMK EEFEKAKENL AKAEAKRKEL EEKMVALMQE KNDLQLQVQS
     EADSLADAEE RCDQLIKTKI QLEAKIKEVT ERAEDEEEIN AELTAKKRKL EDECSELKKD
     IDDLELTLAK VEKEKHATEN KVKNLTEEMA GLDETIAKLT KEKKALQEAH QQTLDDLQAE
     EDKVNTLTKA KIKLEQQVDD LEGSLEQEKK IRMDLERAKR KLEGDLKLAQ ESTMDVENDK
     QQLDEKLKKK EFEMSNLQSK IEDEQALGMQ LQKKIKELQA RIEELEEEIE AERASRAKAE
     KQRSDLSREL EEISERLEEA GGATSAQIEM NKKREAEFQK MRRDLEEATL QHEATAATLR
     KKHADSVAEL GEQIDNLQRV KQKLEKEKSE MKMEIDDLAS NMEVISKSKG NLEKMCRTLE
     DQVSELKTKE EEQQRLINEL TAQRGRLQTE SGEYSRQLDE KDSLVSQLSR GKQAFTQQIE
     ELKRQLEEEI KAKSALAHAL QSSRHDCDLL REQYEEEQEA KAELQRAMSK ANSEVAQWRT
     KYETDAIQRT EELEEAKKKL AQRLQDAEEH VEAVNAKCAS LEKTKQRLQN EVEDLMIDVE
     RTNAACAALD KKQRNFDKIL AEWKQKYEET HAELEASQKE SRSLSTELFK IKNAYEESLD
     HLETLKRENK NLQQEISDLT EQIAEGGKRI HELEKIKKQI EQEKSELQAA LEEAEASLEH
     EEGKILRIQL ELNQVKSEID RKIAEKDEEI DQLKRNHIRV VESMQSTLDA EIRSRNDAIR
     LKKKMEGDLN EMEIQLNHSN RMAAEALRNY RNTQGILKDT QLHLDDALRG QEDLKEQLAM
     VERRANLLQA EIEELRATLE QTERSRKIAE QELLDASERV QLLHTQNTSL INTKKKLETD
     ISQIQGEMED IVQEARNAEE KAKKAITDAA MMAEELKKEQ DTSAHLERMK KNLEQTVKDL
     QHRLDEAEQL ALKGGKKQIQ KLEARVRELE GEVENEQKRN VEAIKGLRKH ERRVKELTYQ
     TEEDRKNVLR LQDLVDKLQS KVKAYKRQAE EAEEQSNVNL AKFRKIQHEL EEAEERADIA
     ESQVNKLRVK SREVHTKIIS EE
//