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MYH4_MOUSE
ID   MYH4_MOUSE              Reviewed;        1939 AA.
AC   Q5SX39; B9EJ73;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Myosin-4;
DE   AltName: Full=Myosin heavy chain 2b;
DE            Short=MyHC-2b;
DE   AltName: Full=Myosin heavy chain 4;
GN   Name=Myh4;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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: Cytoplasm, myofibril. Note=Thick filaments of the
CC       myofibrils.
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}.
CC   -!- CAUTION: Represents a conventional myosin. This protein should not be
CC       confused with the unconventional myosin-4 (MYO4). {ECO:0000305}.
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DR   EMBL; AL596129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC141362; AAI41363.1; -; mRNA.
DR   CCDS; CCDS24856.1; -.
DR   RefSeq; NP_034985.2; NM_010855.3.
DR   PDB; 7NEP; EM; 10.20 A; L/M=32-844.
DR   PDB; 7QIN; EM; 6.60 A; L/M=1-848.
DR   PDB; 7QIO; EM; 9.00 A; L/M=1-848.
DR   PDBsum; 7NEP; -.
DR   PDBsum; 7QIN; -.
DR   PDBsum; 7QIO; -.
DR   AlphaFoldDB; Q5SX39; -.
DR   SMR; Q5SX39; -.
DR   BioGRID; 201648; 7.
DR   STRING; 10090.ENSMUSP00000018632; -.
DR   iPTMnet; Q5SX39; -.
DR   PhosphoSitePlus; Q5SX39; -.
DR   UCD-2DPAGE; Q5SX39; -.
DR   EPD; Q5SX39; -.
DR   MaxQB; Q5SX39; -.
DR   PaxDb; Q5SX39; -.
DR   PeptideAtlas; Q5SX39; -.
DR   PRIDE; Q5SX39; -.
DR   ProteomicsDB; 293595; -.
DR   ABCD; Q5SX39; 1 sequenced antibody.
DR   DNASU; 17884; -.
DR   Ensembl; ENSMUST00000018632; ENSMUSP00000018632; ENSMUSG00000057003.
DR   Ensembl; ENSMUST00000170942; ENSMUSP00000127514; ENSMUSG00000057003.
DR   GeneID; 17884; -.
DR   KEGG; mmu:17884; -.
DR   UCSC; uc007jmj.2; mouse.
DR   CTD; 4622; -.
DR   MGI; MGI:1339713; Myh4.
DR   VEuPathDB; HostDB:ENSMUSG00000057003; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   GeneTree; ENSGT00940000163646; -.
DR   HOGENOM; CLU_000192_8_1_1; -.
DR   InParanoid; Q5SX39; -.
DR   OMA; AFLYAGH; -.
DR   OrthoDB; 47111at2759; -.
DR   PhylomeDB; Q5SX39; -.
DR   TreeFam; TF314375; -.
DR   BioGRID-ORCS; 17884; 3 hits in 73 CRISPR screens.
DR   PRO; PR:Q5SX39; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5SX39; protein.
DR   Bgee; ENSMUSG00000057003; Expressed in extensor digitorum longus and 92 other tissues.
DR   Genevisible; Q5SX39; MM.
DR   GO; GO:0030016; C:myofibril; ISO: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-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0006936; P:muscle contraction; ISO:MGI.
DR   GO; GO:0014823; P:response to activity; IDA:MGI.
DR   Gene3D; 1.20.5.370; -; 4.
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   InterPro; IPR014751; XRCC4-like_C.
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   3D-structure; Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
KW   Cytoplasm; Methylation; Motor protein; Muscle protein; Myosin;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Thick filament.
FT   CHAIN           1..1939
FT                   /note="Myosin-4"
FT                   /id="PRO_0000123399"
FT   DOMAIN          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          86..782
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          785..814
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          659..681
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          761..775
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1128..1147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1276..1299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          843..1939
FT                   /evidence="ECO:0000255"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
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         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         130
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         389
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         391
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         392
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         419
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         424
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         757
FT                   /note="Pros-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28641"
FT   MOD_RES         776
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1092
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1096
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1241
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1255
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1265
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1286
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1288
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1303
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         1413
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1464
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1467
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1492
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1501
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1517
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1542
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1547
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1554
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1574
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1600
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         1714
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1726
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1730
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1736
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1739
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
SQ   SEQUENCE   1939 AA;  222859 MW;  F4334DF4D674A244 CRC64;
     MSSDAEMAVF GEAAPYLRKS EKERIEAQNK PFDAKSSVFV VDAKESYVKA TVQSREGGKV
     TAKTEGGATV TVKDDQVFSM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYNPEVV AAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA VTGDKKKEEA TSGKMQGTLE DQIISANPLL EAFGNAKTVR
     NDNSSRFGKF IRIHFGATGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPEL
     IEMLLITTNP YDFAYVSQGE ITVPSIDDQE ELMATDTAVD ILGFSADEKV AIYKLTGAVM
     HYGNMKFKQK QREEQAEPDG TEVADKAAYL TSLNSADLLK ALCYPRVKVG NEYVTKGQTV
     QQVYNSVGAL AKSMYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNTLEQLC
     INFTNEKLQQ FFNHHMFVLE QEEYKKEGID WEFIDFGMDL AACIELIEKP MGIFSILEEE
     CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKAEAHF SLVHYAGTVD YNIIGWLDKN
     KDPLNETVVG LYQKSGLKTL AFLFSGGQAA EAEGGGGKKG GKKKGSSFQT VSALFRENLN
     KLMTNLKSTH PHFVRCLIPN ETKTPGAMEH ELVLHQLRCN GVLEGIRICR KGFPSRILYA
     DFKQRYKVLN ASAIPEGQFI DSKKASEKLL GSIDIDHTQY KFGHTKVFFK AGLLGTLEEM
     RDEKLAQLIT RTQAVCRGYL MRVEFKKMME RRESIFCIQY NVRAFMNVKH WPWMKLYFKI
     KPLLKSAETE KEMANMKEDF EKAKEDLAKS EAKRKELEEK MVALMQEKND LQLQVQAEAD
     GLADAEERCD QLIKTKIQLE AKIKELTERA EDEEEINAEL TAKKRKLEDE CSELKKDIDD
     LELTLAKVEK EKHATENKVK NLTEEMAGLD ENIAKLTKEK KALQEAHQQT LDDLQAEEDK
     VNTLTKAKTK LEQQVDDLEG SLEQEKKLRM DLERAKRKLE GDLKLAQEST MDIENDKQQL
     DEKLKKKEFE MSNLQSKIED EQALGMQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR
     SDLSRELEEI SERLEEAGGA TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAAALRKKH
     ADSVAELGEQ IDNLQRVKQK LEKEKSELKM EIDDLASNME TVSKAKGNLE KMCRTLEDQL
     SEVKTKEEEQ QRLINELSTQ KARLHTESGE FSRQLDEKDA MVSQLSRGKQ AFTQQIEELK
     RQLEEESKAK NALAHALQSA RHDCDLLREQ YEEEQEAKAE LQRAMSKANS EVAQWRTKYE
     TDAIQRTEEL EEAKKKLAQR LQDAEEHVEA VNSKCASLEK TKQRLQNEVE DLMIDVERSN
     AACAALDKKQ RNFDKVLAEW KQKYEETQAE LEASQKESRS LSTELFKVKN AYEESLDQLE
     TLKRENKNLQ QEISDLTEQI AEGGKHIHEL EKIKKQIDQE KSELQASLEE AEASLEHEEG
     KILRIQLELN QVKSEIDRKI AEKDEEIDQL KRNHLRVVES MQSTLDAEIR SRNDALRIKK
     KMEGDLNEME IQLNHANRQA AEAIRNLRNT QGMLKDTQLH LDDALRGQDD LKEQLAMVER
     RANLMQAEIE ELRASLEQTE RSRRVAEQEL LDASERVQLL HTQNTSLINT KKKLETDISQ
     IQGEMEDIVQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNM EQTVKDLQHR
     LDEAEQLALK GGKKQIQKLE ARVRELENEV ENEQKRNIEA VKGLRKHERR VKELTYQTEE
     DRKNVLRLQD LVDKLQTKVK AYKRQAEEAE EQSNVNLAKF RKIQHELEEA EERADIAESQ
     VNKLRVKSRE VHTKVISEE
 
 
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