MYO3_CAEEL
ID MYO3_CAEEL Reviewed; 1969 AA.
AC P12844; Q21440;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Myosin-3;
DE AltName: Full=Myosin heavy chain A;
DE Short=MHC A;
GN Name=myo-3; Synonyms=mhcA; ORFNames=K12F2.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=2926820; DOI=10.1016/0022-2836(89)90229-5;
RA Dibb N.J., Maruyama I.N., Krause M., Karn J.;
RT "Sequence analysis of the complete Caenorhabditis elegans myosin heavy
RT chain gene family.";
RL J. Mol. Biol. 205:603-613(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=6352051; DOI=10.1016/0092-8674(83)90381-1;
RA Miller D.M. III, Ortiz I., Berliner G.C., Epstein H.F.;
RT "Differential localization of two myosins within nematode thick
RT filaments.";
RL Cell 34:477-490(1983).
RN [4]
RP IDENTIFICATION.
RX PubMed=2422655; DOI=10.1073/pnas.83.8.2305;
RA Miller D.M., Stockdale F.E., Karn J.;
RT "Immunological identification of the genes encoding the four myosin heavy
RT chain isoforms of Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2305-2309(1986).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=3320053; DOI=10.1083/jcb.105.6.2763;
RA Ardizzi J.P., Epstein H.F.;
RT "Immunochemical localization of myosin heavy chain isoforms and paramyosin
RT in developmentally and structurally diverse muscle cell types of the
RT nematode Caenorhabditis elegans.";
RL J. Cell Biol. 105:2763-2770(1987).
RN [6]
RP IDENTIFICATION.
RX PubMed=2583105; DOI=10.1002/j.1460-2075.1989.tb08506.x;
RA Fire A., Waterston R.H.;
RT "Proper expression of myosin genes in transgenic nematodes.";
RL EMBO J. 8:3419-3428(1989).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=2583106; DOI=10.1002/j.1460-2075.1989.tb08507.x;
RA Waterston R.H.;
RT "The minor myosin heavy chain, mhcA, of Caenorhabditis elegans is necessary
RT for the initiation of thick filament assembly.";
RL EMBO J. 8:3429-3436(1989).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=2300580; DOI=10.1073/pnas.87.3.876;
RA Honda S., Epstein H.F.;
RT "Modulation of muscle gene expression in Caenorhabditis elegans:
RT differential levels of transcripts, mRNAs, and polypeptides for thick
RT filament proteins during nematode development.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:876-880(1990).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17326220; DOI=10.1002/dvdy.21091;
RA Ono K., Yu R., Ono S.;
RT "Structural components of the nonstriated contractile apparatuses in the
RT Caenorhabditis elegans gonadal myoepithelial sheath and their essential
RT roles for ovulation.";
RL Dev. Dyn. 236:1093-1105(2007).
CC -!- FUNCTION: Essential for muscle contraction (PubMed:2583106). Involved
CC in ovulation likely by regulating the contraction of gonadal
CC myoepithelial sheath cells (PubMed:17326220).
CC {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:2583106}.
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
CC {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:6352051}. Cytoplasm,
CC myofibril, sarcomere, A band {ECO:0000269|PubMed:17326220,
CC ECO:0000269|PubMed:6352051}. Note=In myoepithelial sheath cells, forms
CC filaments assembled in a nonstriated meshwork. Colocalizes with unc-
CC 15/paramyosin and with unc-89 to M line-like structures. Does not
CC colocalize with beta integrin pat-3. {ECO:0000269|PubMed:17326220}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles, neighboring vulval
CC muscle cells and the contractile sheath covering the hermaphrodite
CC gonad (myoepithelial sheath cells). {ECO:0000269|PubMed:17326220,
CC ECO:0000269|PubMed:3320053, ECO:0000269|PubMed:6352051}.
CC -!- DEVELOPMENTAL STAGE: Expression at early and late larval stages is 1:20
CC of unc-54 (mhc b), however later at L1 and L4 expression is more equal
CC at 1:1.7 and 1:3.1 respectively. {ECO:0000269|PubMed:2300580}.
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 -!- DISRUPTION PHENOTYPE: Worms exhibit retarded embryonic development and
CC paralysis (PubMed:2583106). Muscle organization shows disruption with
CC abnormalities of both the filament lattice that constitutes the A-band
CC and the hypodermal cell (PubMed:2583106). RNAi-mediated knockdown
CC causes an accumulation in the proximal gonad of endomitotic mature
CC oocytes in 51 percent of animals (PubMed:17326220).
CC {ECO:0000269|PubMed:2583106, ECO:0000269|PubMed:3320053}.
CC -!- MISCELLANEOUS: There are four different myosin heavy chains in
CC C.elegans.
CC -!- MISCELLANEOUS: MHC A and MHC B are found exclusively in the body wall
CC muscle. They co-assemble into body wall thick filament.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; X08067; CAA30856.1; -; Genomic_DNA.
DR EMBL; Z78199; CAB01576.2; -; Genomic_DNA.
DR PIR; T23622; S02771.
DR RefSeq; NP_506065.2; NM_073664.5.
DR AlphaFoldDB; P12844; -.
DR SMR; P12844; -.
DR BioGRID; 44699; 13.
DR IntAct; P12844; 6.
DR STRING; 6239.K12F2.1; -.
DR iPTMnet; P12844; -.
DR EPD; P12844; -.
DR PaxDb; P12844; -.
DR PeptideAtlas; P12844; -.
DR PRIDE; P12844; -.
DR EnsemblMetazoa; K12F2.1.1; K12F2.1.1; WBGene00003515.
DR GeneID; 179676; -.
DR KEGG; cel:CELE_K12F2.1; -.
DR UCSC; K12F2.1; c. elegans.
DR CTD; 179676; -.
DR WormBase; K12F2.1; CE34936; WBGene00003515; myo-3.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_4_2_1; -.
DR InParanoid; P12844; -.
DR OMA; TDTTQDK; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P12844; -.
DR SignaLink; P12844; -.
DR PRO; PR:P12844; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003515; Expressed in larva and 3 other tissues.
DR GO; GO:0031672; C:A band; IDA:UniProtKB.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0005863; C:striated muscle myosin thick filament; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IMP:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; IMP:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Methylation;
KW Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW Reference proteome; Thick filament.
FT CHAIN 1..1969
FT /note="Myosin-3"
FT /id="PRO_0000123382"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..791
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 794..823
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 667..689
FT /note="Actin-binding"
FT REGION 770..784
FT /note="Actin-binding"
FT REGION 942..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 857..1969
FT /evidence="ECO:0000255"
FT COMPBIAS 1131..1162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1213
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 MOD_RES 130
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1969 AA; 225510 MW; 64577BBAF7EAD80A CRC64;
MSGNPDAFEN DPGFPFLGIS REARAATAAR PFDSKKNCWI PDPEDGFVAA EIQSTTGEQV
TVVTVKGNQI TVKKDQCQEM NPPKFDKTED MANLTFLNEA SVLGNLKDRY KDLMIYTYSG
LFCVVINPYK RLPIYSESVI KHFMGKRRNE MPPHLFAVSD EAYRNMVQDK ENQSMLITGE
SGAGKTENTK KVISYFAIVG ATQAASGKEA KDGKKGGTLE EQIVQTNPVL EAFGNAKTVR
NNNSSRFGKF IRTHFSGSGK LAGGDIEHYL LEKSRVVRQA PGERCYHIFY QIMSGNDPSL
RGKLKLSNDI TYYHFCSQAE LTIEGMDDKE EMRLTQEAFD IMGFEDNETM DLYRSTAGIM
HMGEMKFKQR PREEQAEPDG EEDALNAAAM LGIQAEEFLK ALTKPRVRVG TEWVNKGQNL
EQVNWAVSGL AKAIYARMFK WIITRCNKTL DAKEIERKHF IGVLDIAGFE IFDLNSFEQL
WINFVNERLQ QFFNHHMFVL EQEEYKREGI AWTFIDFGLD LQACIELIEK PLGIISILDE
ECIVPKATDM TYAQKLLDQH LGKHPNFQKP KPPKGKQGDA HFAIVHYAGT VRYNATNFLE
KNKDPLNDTA VALLKHSTDN SLMLDIWQDY QTQEEAAEAA KAGQTAGGKR GKSSSFATVS
MIYRESLNNL MNMLYQTHPH FIRCIIPNEK KASGVIDSAL VLNQLTCNGV LEGIRICRKG
FPNRMLYPDF KHRYAILAAD AAKESDPKKA SVGILDKISV DGNLTDEEFK VGETKIFFKA
GVLAKLEDLR DEILSRIVTM FQSRIRSYLA KAEVRRRYEQ QTGLLVVQRN VRAWCTLRTW
EWFKLFGKVK PMLKAGKEQE AMGELAVKIQ KLEEAVQRGE IARSQLESQV ADLVEEKNAL
FLSLETEKAN LADAEERNEK LNQLKATLES KLSDITGQLE DMQERNEDLA RQKKKTDQEL
SDTKKHVQDL ELSLRKAEQE KQSRDHNIRS LQDEMANQDE AVAKLNKEKK HQEESNRKLN
EDLQSEEDKV NHLEKIRNKL EQQMDELEEN IDREKRSRGD IEKAKRKVEG DLKVAQENID
EITKQKHDVE TTLKRKEEDL HHTNAKLAEN NSIIAKLQRL IKELTARNAE LEEELEAERN
SRQKSDRSRS EAERELEELT ERLEQQGGAT AAQLEANKKR EAEIAKLRRE KEEDSLNHET
AISSLRKRHG DSVAELTEQL ETLQKLKAKS EAEKSKLQRD LEESQHATDS EVRSRQDLEK
ALKTIEVQYS ELQTKADEQS RQLQDFAALK NRLNNENSDL NRSLEEMDNQ LNSLHRLKST
LQSQLDETRR NYDEESRERQ ALAATAKNLE HENTILREHL DEEAESKADL TRQISKLNAE
IQQWKARFDS EGLNKLEEIE AAKKALQLKV QELTDTNEGL FAKIASQEKV RFKLMQDLDD
AQSDVEKAAA QVAFYEKHRR QFESIIAEWK KKTDDLSSEL DAAQRDNRQL STDLFKAKTA
NDELAEYLDS TRRENKSLAQ EVKDLTDQLG EGGRSVAELQ KIVRKLEVEK EELQKALDEA
EAALEAEEAK VLRAQIEVSQ IRSEIEKRIQ EKEEEFENTR RNHQRALESM QATLEAETKQ
KEEALRIKKK LESDINDLEI ALDHANRAYA DAQKTIKKYM ETVQELQFQI EEEQRQKDEI
REQFLASEKR NAILQSEKDE LAQQAEAAER ARRNAEAECI ELREQNNDLN AHVSALTGQR
RKLEGELLAA HAELEEIANE LKNAVEQGQK ASADAARLAE ELRQEQEHSM HIERIRKGLE
LQIKEMQIRL DDAENAALKG GKKIIAQLEA RIRAIEQELD GEQRRHQDTE KNWRKAERRV
KEVEFQVVEE KKNEERLTEL VDKLQCKLKI FKRQVEEAEE VAASNLNKYK VLTAQFEQAE
ERADIAENAL SKMRNKIRAS ASMAPPDGFP MVPSASSALI RSSSNARFL
