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}.
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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 Genevisible; Q5SX40; MM.
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.
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
//
