ID E9QPE7_MOUSE Unreviewed; 1972 AA.
AC E9QPE7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Myosin-11 {ECO:0000256|ARBA:ARBA00040393};
DE AltName: Full=Myosin heavy chain 11 {ECO:0000256|ARBA:ARBA00042406};
GN Name=Myh11 {ECO:0000313|Ensembl:ENSMUSP00000087756.5,
GN ECO:0000313|MGI:MGI:102643};
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:ENSMUSP00000087756.5, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000087756.5, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000087756.5,
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 [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000087756.5}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000087756.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Muscle contraction. {ECO:0000256|ARBA:ARBA00037488}.
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 {ECO:0000256|ARBA:ARBA00038612}.
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_001155247.1; NM_001161775.1.
DR SMR; E9QPE7; -.
DR EPD; E9QPE7; -.
DR jPOST; E9QPE7; -.
DR PeptideAtlas; E9QPE7; -.
DR ProteomicsDB; 311929; -.
DR Antibodypedia; 1966; 846 antibodies from 33 providers.
DR DNASU; 17880; -.
DR Ensembl; ENSMUST00000090287.5; ENSMUSP00000087756.5; ENSMUSG00000018830.11.
DR GeneID; 17880; -.
DR KEGG; mmu:17880; -.
DR UCSC; uc007yhd.2; mouse.
DR AGR; MGI:102643; -.
DR CTD; 4629; -.
DR MGI; MGI:102643; Myh11.
DR VEuPathDB; HostDB:ENSMUSG00000018830; -.
DR GeneTree; ENSGT00940000155421; -.
DR HOGENOM; CLU_000192_4_3_1; -.
DR OrthoDB; 2877572at2759; -.
DR PhylomeDB; E9QPE7; -.
DR TreeFam; TF333601; -.
DR BioGRID-ORCS; 17880; 7 hits in 77 CRISPR screens.
DR ChiTaRS; Myh11; mouse.
DR Proteomes; UP000000589; Chromosome 16.
DR Bgee; ENSMUSG00000018830; Expressed in aorta tunica media and 199 other cell types or tissues.
DR ExpressionAtlas; E9QPE7; baseline and differential.
DR Genevisible; E9QPE7; MM.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd14921; MYSc_Myh11; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.340; -; 4.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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 Gene3D; 4.10.270.10; Myosin, subunit A; 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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF23; MYOSIN-11; 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; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 6.
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 {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};
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:E9QPE7,
KW ECO:0007829|MaxQB:E9QPE7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 661..683
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1771..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1829..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1866..1915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1945..1972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1972 AA; 227119 MW; 012A791D43E94111 CRC64;
MAQKGQLSDD EKFLFVDKNF MNSPMAQADW VAKKLVWVPS EKQGFEAASI KEEKGDEVVV
ELVENGKKVT VGKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL
FCVVVNPYKY LPIYSEKIVD MYKGKKRHEM PPHIYAIADT AYRSMLQDRE DQSILCTGES
GAGKTENTKK VIQYLAVVAS SHKGKKDSSI TGELEKQLLQ ANPILEAFGN AKTVKNDNSS
RFGKFIRINF DVTGYIVGAN IETYLLEKSR AIRQARDERT FHIFYYLLAG AKEKMKSDLL
LESFNSYTFL SNGFVPIPAA QDDEMFQETL EAMSIMGFNE EEQLAILKVV SSVLQLGNIV
FKKERNTDQA SMPDNTAAQK VCHLVGINVT DFTRAILTPR IKVGRDVVQK AQTKEQADFA
IEALAKATYE RLFRWILSRV NKALDKTHRQ GASFLGILDI AGFEIFEVNS FEQLCINYTN
EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCIE LIERPNNPPG VLALLDEECW
FPKATDKSFV EKLCSEQGNH PKFQKPKQLK DKTEFSIIHY AGKVDYNASA WLTKNMDPLN
DNVTSLLNAS SDKFVADLWK DVDRIVGLDQ MAKMTESSLP SASKTKKGMF RTVGQLYKEQ
LGKLMTTLRN TTPNFVRCII PNHEKRSGKL DAFLVLEQLR CNGVLEGIRI CRQGFPNRIV
FQEFRQRYEI LAANAIPKGF MDGKQACILM IKALELDPNL YRIGQSKIFF RTGVLAHLEE
ERDLKITDVI MAFQAMCRGY LARKAFTKRQ QQLTAMKVIQ RNCAAYLKLR NWQWWRLFTK
VKPLLQVTRQ EEEMQAKEEE MQKIKERQQK AETELKELEQ KHTQLAEEKT LLQEQLQAET
ELYAEAEEMR VRLAAKKQEL EEILHEMEAR LEEEEDRGQQ LQAERKKMAQ QMLDLEEQLE
EEEAARQKLQ LEKVTAEAKI KKLEDDILVM DDQNSKLSKE RKLLEERVSD LTTNLAEEEE
KAKNLTKLKS KHESMISELE VRLKKEEKSR QELEKLKRKL EGDASDFHEQ IADLQAQIAE
LKMQLAKKEE ELQAALARLD EEIAQKNNAL KKIRELEGHI SDLQEDLDSE RAARNKAEKQ
KRDLGEELEA LKTELEDTLD STATQQELRA KREQEVTVLK KALDEETRSH EAQVQEMRQK
HTQAVEELTE QLEQFKRAKA NLDKSKQTLE KENADLAGEL RVLGQAKQEV EHKKKKLEVQ
LQDLQSKCSD GERARAELSD KVHKLQNEVE SVTGMLNEAE GKAIKLAKDV ASLGSQLQDT
QELLQEETRQ KLNVSTKLRQ LEDERNSLQD QLDEEMEAKQ NLERHVSTLN IQLSDSKKKL
QDFASTIEVM EEGKKRLQKE MEGLSQQYEE KAAAYDKLEK TKNRLQQELD DLVVDLDNQR
QLVSNLEKKQ KKFDQLLAEE KNISSKYADE RDRAEAEARE KETKALSLAR ALEEALEAKE
ELERTNKMLK AEMEDLVSSK DDVGKNVHEL EKSKRALETQ MEEMKTQLEE LEDELQATED
AKLRLEVNMQ ALKGQFERDL QARDEQNEEK RRQLQRQLHE YETELEDERK QRALAAAAKK
KLEGDLKDLE LQADSAIKGR EEAIKQLRKL QAQMKDFQRE LDDARASRDE IFATSKENEK
KAKSLEADLM QLQEDLAAAE RARKQADLEK EELAEELASS LSGRNTLQDE KRRLEARIAQ
LEEELEEEQG NMEAMSDRVR KATLQAEQLS NELATERSTA QKNESARQQL ERQNKELRSK
LQEVEGAVKA KLKSTVAALE AKIAQLEEQV EQEAREKQAA TKSLKQKDKK LKEVLLQVED
ERKMAEQYKE QAEKGNTKVK QLKRQLEEAE EESQRINANR RKLQRELDEA TESNEAMGRE
VNALKSKLRR GNEASFVPSR RAGGRRVIEN TDGSEEEMDA RDSDFNGTKA SE
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