ID G3UW82_MOUSE Unreviewed; 1942 AA.
AC G3UW82;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Myosin-2 {ECO:0000256|ARBA:ARBA00039812};
DE AltName: Full=Myosin heavy chain 2 {ECO:0000256|ARBA:ARBA00041436};
DE AltName: Full=Myosin heavy chain 2a {ECO:0000256|ARBA:ARBA00042414};
DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 2 {ECO:0000256|ARBA:ARBA00041387};
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 (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Muscle contraction. Required for cytoskeleton organization.
CC {ECO:0000256|ARBA:ARBA00037212}.
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). Interacts with GCSAM.
CC {ECO:0000256|ARBA:ARBA00038665}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR RefSeq; NP_001034634.2; NM_001039545.2.
DR STRING; 10090.ENSMUSP00000129544; -.
DR PaxDb; 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; 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 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: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
//
