ID G3UW82_MOUSE Unreviewed; 1942 AA. AC G3UW82; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 03-MAY-2023, entry version 91. DE SubName: Full=Myosin, heavy polypeptide 2, skeletal muscle, adult {ECO:0000313|Ensembl:ENSMUSP00000129544.2}; GN Name=Myh2 {ECO:0000313|Ensembl:ENSMUSP00000129544.2, GN ECO:0000313|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:0000313|Ensembl:ENSMUSP00000129544.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000129544.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000129544.2, RC ECO:0000313|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:0000313|Ensembl:ENSMUSP00000129544.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000129544.2}; RG Ensembl; RL Submitted (JAN-2023) to UniProtKB. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314, CC ECO:0000256|PROSITE-ProRule:PRU00782}. 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 STRING; 10090.ENSMUSP00000129544; -. 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; RNFGWLV; -. 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 Bgee; ENSMUSG00000033196; Expressed in soleus muscle and 56 other 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:0032991; C:protein-containing complex; ISO:MGI. 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; ISO:MGI. 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 {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE- KW ProRule:PRU00782}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00782}; Coiled coil {ECO:0000256|ARBA:ARBA00023054}; KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE- KW ProRule:PRU00782}; Muscle protein {ECO:0000256|ARBA:ARBA00023179}; KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE- KW ProRule:PRU00782}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00782}; KW Proteomics identification {ECO:0007829|EPD:G3UW82, KW ECO:0007829|MaxQB:G3UW82}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Thick filament {ECO:0000256|ARBA:ARBA00022433}. FT DOMAIN 33..82 FT /note="Myosin N-terminal SH3-like" FT /evidence="ECO:0000259|PROSITE:PS51844" FT DOMAIN 86..785 FT /note="Myosin motor" FT /evidence="ECO:0000259|PROSITE:PS51456" FT REGION 662..684 FT /note="Actin-binding" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782" FT REGION 1130..1175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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:0000256|PROSITE-ProRule:PRU00782" 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 //