MYH11_MOUSE
ID MYH11_MOUSE Reviewed; 1972 AA.
AC O08638; O08639; Q62462; Q64195;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Myosin-11;
DE AltName: Full=Myosin heavy chain 11;
DE AltName: Full=Myosin heavy chain, smooth muscle isoform;
DE AltName: Full=SMMHC;
GN Name=Myh11;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Uterus;
RX PubMed=9125171; DOI=10.1006/bbrc.1997.6281;
RA Hasegawa K., Arakawa E., Oda S., Matsuda Y.;
RT "Molecular cloning and expression of murine smooth muscle myosin heavy
RT chains.";
RL Biochem. Biophys. Res. Commun. 232:313-316(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-368.
RC TISSUE=Uterus;
RX PubMed=7923625; DOI=10.1161/01.res.75.5.803;
RA Miano J.M., Cserjesi P., Ligon K.L., Periasamy M., Olson E.N.;
RT "Smooth muscle myosin heavy chain exclusively marks the smooth muscle
RT lineage during mouse embryogenesis.";
RL Circ. Res. 75:803-812(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-126.
RC TISSUE=Uterus;
RX PubMed=8593698; DOI=10.1161/01.res.78.3.395;
RA Suzuki T., Kim H.S., Kurabayashi M., Hamada H., Fujii H., Aikawa M.,
RA Watanabe M., Watanabe N., Sakomura Y., Yazaki Y., Nagai R.;
RT "Preferential differentiation of P19 mouse embryonal carcinoma cells into
RT smooth muscle cells. Use of retinoic acid and antisense against the central
RT nervous system-specific POU transcription factor Brn-2.";
RL Circ. Res. 78:395-404(1996).
RN [4]
RP PROTEIN SEQUENCE OF 1218-1224, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-1951 AND SER-1954, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-1951; SER-1954 AND
RP SER-1971, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Melanosome {ECO:0000250}. Cytoplasm, myofibril.
CC Note=Thick filaments of the myofibrils.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O08638-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O08638-2; Sequence=VSP_003346;
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}.
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DR EMBL; D85923; BAA19690.1; -; mRNA.
DR EMBL; D85924; BAA19691.1; -; mRNA.
DR EMBL; L25860; AAA67552.1; -; mRNA.
DR EMBL; S81516; AAB36168.1; -; mRNA.
DR CCDS; CCDS27972.1; -. [O08638-2]
DR CCDS; CCDS88881.1; -. [O08638-1]
DR PIR; I52863; I52863.
DR PIR; JC5420; JC5420.
DR PIR; JC5421; JC5421.
DR AlphaFoldDB; O08638; -.
DR SMR; O08638; -.
DR IntAct; O08638; 8.
DR STRING; 10090.ENSMUSP00000087756; -.
DR iPTMnet; O08638; -.
DR PhosphoSitePlus; O08638; -.
DR SwissPalm; O08638; -.
DR EPD; O08638; -.
DR jPOST; O08638; -.
DR MaxQB; O08638; -.
DR PaxDb; O08638; -.
DR PeptideAtlas; O08638; -.
DR PRIDE; O08638; -.
DR ProteomicsDB; 287654; -. [O08638-1]
DR ProteomicsDB; 287655; -. [O08638-2]
DR MGI; MGI:102643; Myh11.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; O08638; -.
DR PhylomeDB; O08638; -.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR ChiTaRS; Myh11; mouse.
DR PRO; PR:O08638; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O08638; protein.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005859; C:muscle myosin complex; IDA:MGI.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; 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:0030485; C:smooth muscle contractile fiber; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
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:0003774; F:cytoskeletal motor activity; IMP:MGI.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0055013; P:cardiac muscle cell development; ISS:UniProtKB.
DR GO; GO:0048251; P:elastic fiber assembly; ISS:UniProtKB.
DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; ISS:UniProtKB.
DR GO; GO:0006939; P:smooth muscle contraction; IDA:MGI.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 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 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; SSF52540; SSF52540; 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; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Coiled coil; Cytoplasm; Direct protein sequencing; Methylation;
KW Motor protein; Muscle protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Thick filament.
FT CHAIN 1..1972
FT /note="Myosin-11"
FT /id="PRO_0000123425"
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 85..783
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 786..815
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 661..683
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 762..776
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1771..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1867..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1935..1972
FT /note="C-terminal"
FT COILED 844..1934
FT /evidence="ECO:0000255"
FT COMPBIAS 1771..1787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1867..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:0000255"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35749"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z406"
FT MOD_RES 129
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT MOD_RES 1177
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z406"
FT MOD_RES 1684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63862"
FT MOD_RES 1722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63862"
FT MOD_RES 1951
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1954
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1930..1972
FT /note="RGNEASFVPSRRAGGRRVIENTDGSEEEMDARDSDFNGTKASE -> GPPPQ
FT ETSQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003346"
FT CONFLICT 126
FT /note="N -> D (in Ref. 3; AAB36168)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="A -> V (in Ref. 2; AAA67552)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="Q -> K (in Ref. 2; AAA67552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1972 AA; 227028 MW; A1398E3F5B11F15A CRC64;
MAQKGQLSDD EKFLFVDKNF MNSPMAQADW VAKKLVWVPS EKQGFEAASI KEEKGDEVVV
ELVENGKKVT VGKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL
FCVVVNPYKY LPIYSEKIVD MYKGKKRHEM PPHIYAIADT AYRSMLQDRE DQSILCTGES
GAGKTENTQK 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 FGLDLQPSIE LIERPNNPPG VLALLDEECW
FPKATDKSFV EKLCSEQGNH PKFQKPKQLK DKTEFSIIHY AGKVDYNASA WLTKNMDPLN
DNVTSLLNAS SDKFVADLWK DVDRIVGLDQ MAKMTESSLP SASKTKKGMF RTVGQLYKEQ
LGKLMATLRN TTANFVRCII PNHEKRSGKL DAFLVLEQLR CNGVLEGIRI CRQGFPNRIV
FQEFRQRYEI LAANAIPKGF MDGKQACILM IKALELDPNL YRIGQSKIFF RTGVLAHLEE
ERDLKITDVI MAFQAMCRGY LARKAFTKRQ QQLTAMKVIQ RNCAAYLKLR NWQWWRLFTK
VKPLLQVTRQ EEEMQAKEEE MQKITERQQK AETELKELEQ KHTQLAEEKT LLQEQLQAET
ELYAESEEMR VRLAAKKQEL EEILHEMEAR LEEEEDRRQQ 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 SEDDVQATED
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 EESQCINANR RKLQRELDEA TESNEAMGRE
VNALKSKLRR GNEASFVPSR RAGGRRVIEN TDGSEEEMDA RDSDFNGTKA SE
