ID MYH2_MOUSE Reviewed; 1942 AA. AC G3UW82; DT 24-JUL-2024, integrated into UniProtKB/Swiss-Prot. DT 16-NOV-2011, sequence version 1. DT 02-OCT-2024, entry version 99. DE RecName: Full=Myosin-2 {ECO:0000305}; DE AltName: Full=Myosin heavy chain 2 {ECO:0000250|UniProtKB:Q9UKX2}; DE AltName: Full=Myosin heavy chain 2a; DE Short=MyHC-2a {ECO:0000305}; DE AltName: Full=Myosin heavy chain IIa {ECO:0000305}; DE Short=MyHC-IIa {ECO:0000312|MGI:MGI:1339710}; DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 2; GN Name=Myh2 {ECO:0000312|MGI:MGI:1339710}; 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 {ECO:0000312|Proteomes:UP000000589}; RN [1] {ECO:0000312|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589}; 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] {ECO:0000305} RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=28752107; DOI=10.21769/bioprotoc.2279; RA Wang C., Yue F., Kuang S.; RT "Muscle Histology Characterization Using H&E Staining and Muscle Fiber Type RT Classification Using Immunofluorescence Staining."; RL Bio. Protoc. 7:0-0(2017). CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity CC essential for muscle contraction. {ECO:0000250|UniProtKB:P12883}. 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) (Probable). Interacts with CC GCSAM (By similarity). {ECO:0000250|UniProtKB:Q9UKX2, ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril CC {ECO:0000269|PubMed:28752107}. Note=Thick filaments of the myofibrils. CC -!- TISSUE SPECIFICITY: Expressed in type 2a myofibers in the tibialis CC anterior and soleus muscles (at protein level). CC {ECO:0000269|PubMed:28752107}. 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:0000255|PROSITE-ProRule:PRU00782}. CC -!- CAUTION: Represents a conventional myosin. This protein should not be CC confused with the unconventional myosin-2 (MYO2) found in fungi. CC {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 RefSeq; NP_001034634.2; NM_001039545.2. DR AlphaFoldDB; G3UW82; -. DR SMR; G3UW82; -. DR STRING; 10090.ENSMUSP00000129544; -. DR iPTMnet; G3UW82; -. DR PaxDb; 10090-ENSMUSP00000129544; -. DR PeptideAtlas; G3UW82; -. DR ProteomicsDB; 342711; -. DR DNASU; 17882; -. DR Ensembl; ENSMUST00000018641.8; ENSMUSP00000018641.8; ENSMUSG00000033196.18. DR Ensembl; ENSMUST00000170159.8; ENSMUSP00000129544.2; ENSMUSG00000033196.18. DR GeneID; 17882; -. DR KEGG; mmu:17882; -. DR UCSC; uc007jmd.2; mouse. DR AGR; MGI:1339710; -. DR CTD; 4620; -. DR MGI; MGI:1339710; Myh2. DR VEuPathDB; HostDB:ENSMUSG00000033196; -. DR eggNOG; KOG0161; Eukaryota. DR GeneTree; ENSGT00940000154760; -. DR HOGENOM; CLU_000192_8_1_1; -. DR OMA; IHIIEVM; -. DR OrthoDB; 2877572at2759; -. DR TreeFam; TF314375; -. DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation. DR BioGRID-ORCS; 17882; 2 hits in 77 CRISPR screens. DR ChiTaRS; Myh2; mouse. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; G3UW82; protein. DR Bgee; ENSMUSG00000033196; Expressed in soleus muscle and 56 other cell types or tissues. DR GO; GO:0031672; C:A band; IDA:MGI. DR GO; GO:0005826; C:actomyosin contractile ring; IDA:MGI. DR GO; GO:0005911; C:cell-cell junction; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IMP:MGI. DR GO; GO:0005859; C:muscle myosin complex; ISO:MGI. DR GO; GO:0030016; C:myofibril; 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; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central. DR GO; GO:0070252; P:actin-mediated cell contraction; IDA:MGI. DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central. DR GO; GO:0001778; P:plasma membrane repair; IMP:MGI. DR GO; GO:0014823; P:response to activity; IDA:MGI. 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:SF39; MYOSIN-2; 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; 5. 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. PE 1: Evidence at protein level; KW Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Methylation; KW Motor protein; Muscle protein; Myosin; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Thick filament. FT CHAIN 1..1942 FT /note="Myosin-2" FT /id="PRO_0000460618" 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:0000255|PROSITE-ProRule:PRU00782" FT REGION 1130..1175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 849..1930 FT /evidence="ECO:0000255" FT COMPBIAS 1130..1158 FT /note="Basic and acidic 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|PROSITE-ProRule:PRU00782" 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 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 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 1244 FT /note="Phosphothreonine" 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 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 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; 223219 MW; 9087D534CB3C4AD7 CRC64; MSSDAEMAVF GEAAPYLRKS EKERIEAQNR PFDAKTSVFV AEPKESFVKG TIQSKDAGKV TVKTEAGATL TVKEDQIFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG LFCVTVNPYK WLPVYNPEVV AAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE SGAGKTVNTK RVIQYFATIA VTGDKKKEEA TSGKMQGTLE DQIISANPLL EAFGNAKTVR NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QITSNKKPEL IEMLLITTNP YDYPFVSQGE ISVASIDDQE ELMATDSAID ILGFTNDEKV SIYKLTGAVM HYGNMKFKQK QREEQAEPDG TEVADKAAYL QGLNSADLLK ALCYPRVKVG NEYVTKGQTV EQVTNAVGAL AKAMYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP MGIFSILEEE CMFPKATDTS FKNKLYEQHL GKSANFQKPK VVKGKAEAHF SLIHYAGTVD YNITGWLDKN KDPLNETVVG LYQKSSVKTL AYLFSGAQTA EAEASSGGAA KKGAKKKGSS FQTVSALFRE NLNKLMTNLR STHPHFVRCI IPNETKTPGA MEHELVLHQL RCNGVLEGIR ICRKGFPSRI LYADFKQRYK VLNASAIPEG QYIDSKKASE KLLGSIDIDH TQYKFGHTKV FFKAGLLGLL EEMRDDKLAQ LITRTQAMCR GFLARVEYQK MVERRESIFC IQYNIRAFMN VKHWPWMKLF FKIKPLLKSA ETEKEMATMK EEFQKTKDDL AKSEAKRKEL EEKMVSLLKE KNDLQLQVQA EAEGLADAEE RCDQLIKTKI QLEAKIKEVT ERAEDEEEIN AELTAKKRKL EDECSELKKD IDDLELTLAK VEKEKHATEN KVKNLTEEMA GLDETIAKLT KEKKALQEAH QQTLDDLQAE EDKVNTLTKA KIKLEQQVDD LEGSLEQEKK LRMDLERAKR KLEGDLKLAQ ESIMDIENEK QQLDERLKKK EFEMSNLQSK IEDEQAIGIQ LQKKIKELQA RIEELEEEIE AERASRAKAE KQRSDLSREL EEISERLEEA GGATSAQIEM NKKREAEFQK MRRDLEEATL QHEATAATLR KKHADSVAEL GEQIDNLQRV KQKLEKEKSE MKMEIDDLAS NVETVSKAKG NLEKMCRTLE DQVSELKSKE EEQQRLINDL TTQRGRLQTE SGEFSRQLDE KEALVSQLSR GKQAFTQQIE ELKRQLEEEV KAKNALAHAL QSSRHDCDLL REQYEEEQES KAELQRALSK ANSEVAQWRT KYETDAIQRT EELEEAKKKL AQRLQAAEEH VEAVNAKCAS LEKTKQRLQN EVEDLMLDVE RTNAACAALD KKQRNFDKIL AEWKQKYEET HAELEASQKE ARSLGTELFK MKNAYEESLD QLETLKRENK NLQQEISDLT EQIAEGGKRI HELEKIKKQV EQEKCELQAA LEEAEASLEH EEGKILRIQL ELNQVKSEID RKIAEKDEEI DQLKRNHIRV VESMQSTLDA EIRSRNDAIR IKKKMEGDLN EMEIQLNHSN RMAAEALRNY RNTQGILKDT QLHLDDALRG QEDLKEQLAM VERRANLLQA EIEELRATLE QTERSRKIAE QELLDASERV QLLHTQNTSL INTKKKLETD ISQIQGEMED IVQEARNAEE KAKKAITDAA MMAEELKKEQ DTSAHLERMK KNMEQTVKDL QLRLDEAEQL ALKGGKKQIQ KLEARVRELE GEVESEQKRN AEAVKGLRKH ERRVKELTYQ TEEDRKNILR LQDLVDKLQA KVKSYKRQAE EAEEQSNTNL SKFRKIQHEL EEAEERADIA ESQVNKLRVK SREVHTKIIS EE //