MYO2_CAEEL
ID MYO2_CAEEL Reviewed; 1947 AA.
AC P12845; Q20439; Q22545;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Myosin-2;
DE AltName: Full=Myosin heavy chain C;
DE Short=MHC C;
GN Name=myo-2; ORFNames=T18D3.4;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21; 112-371 AND 1501-1772.
RC STRAIN=Bristol N2;
RX PubMed=3888374; DOI=10.1007/978-1-4757-4723-2_7;
RA Karn J., Dibb N.J., Miller D.M.;
RT "Cloning nematode myosin genes.";
RL Cell Muscle Motil. 6:185-237(1985).
RN [4]
RP INTERACTION WITH ITR-1.
RX PubMed=12062062; DOI=10.1016/s0960-9822(02)00868-0;
RA Walker D.S., Ly S., Lockwood K.C., Baylis H.A.;
RT "A direct interaction between IP(3) receptors and myosin II regulates IP(3)
RT signaling in C. elegans.";
RL Curr. Biol. 12:951-956(2002).
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). Interacts with itr-1.
CC {ECO:0000269|PubMed:12062062}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
CC -!- TISSUE SPECIFICITY: Found exclusively in the pharyngeal muscle.
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 -!- MISCELLANEOUS: There are four different myosin heavy chains in
CC C.elegans.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; X08066; CAA30855.1; -; Genomic_DNA.
DR EMBL; Z68119; CAA92197.2; -; Genomic_DNA.
DR EMBL; Z68117; CAA92197.2; JOINED; Genomic_DNA.
DR EMBL; M37233; AAA28121.1; -; Genomic_DNA.
DR EMBL; M37235; AAA28122.1; -; Genomic_DNA.
DR EMBL; M37236; AAA28123.1; -; Genomic_DNA.
DR PIR; T22232; S05697.
DR RefSeq; NP_510092.2; NM_077691.4.
DR AlphaFoldDB; P12845; -.
DR SMR; P12845; -.
DR BioGRID; 46308; 9.
DR STRING; 6239.T18D3.4; -.
DR iPTMnet; P12845; -.
DR EPD; P12845; -.
DR PaxDb; P12845; -.
DR PeptideAtlas; P12845; -.
DR PRIDE; P12845; -.
DR EnsemblMetazoa; T18D3.4.1; T18D3.4.1; WBGene00003514.
DR GeneID; 181404; -.
DR KEGG; cel:CELE_T18D3.4; -.
DR UCSC; T18D3.4; c. elegans.
DR CTD; 181404; -.
DR WormBase; T18D3.4; CE31619; WBGene00003514; myo-2.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_8_0_1; -.
DR InParanoid; P12845; -.
DR OMA; QFKFGHT; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P12845; -.
DR PRO; PR:P12845; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003514; Expressed in larva and 3 other tissues.
DR GO; GO:0005859; C:muscle myosin complex; ISS:WormBase.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0030017; C:sarcomere; IEA:UniProt.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; ISS:WormBase.
DR GO; GO:0006936; P:muscle contraction; ISS:WormBase.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR Gene3D; 1.20.5.370; -; 1.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
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; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein 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..1947
FT /note="Myosin-2"
FT /id="PRO_0000123381"
FT DOMAIN 28..77
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 81..794
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 668..690
FT /note="Actin-binding"
FT REGION 773..787
FT /note="Actin-binding"
FT REGION 856..1947
FT /note="Rodlike tail (S2 and LMM domains)"
FT REGION 1047..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1516..1537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 856..1947
FT /evidence="ECO:0000255"
FT COMPBIAS 1049..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 125
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT CONFLICT 132
FT /note="D -> E (in Ref. 1; CAA30855)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="M -> I (in Ref. 3; AAA28121)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="C -> S (in Ref. 1; CAA30855 and 3; AAA28121)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="N -> K (in Ref. 1; CAA30855)"
FT /evidence="ECO:0000305"
FT CONFLICT 1248
FT /note="S -> C (in Ref. 1; CAA30855)"
FT /evidence="ECO:0000305"
FT CONFLICT 1271..1273
FT /note="RLL -> QTS (in Ref. 1; CAA30855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1947 AA; 223048 MW; 09024B39E16DEA78 CRC64;
MDYENDPGWK YLRRSREEML QDQSRAYDSK KNVWIPDSED GYIEGVITKT AGDNVTVSIG
QGAEKTVKKD VVQEMNPPKF EKTEDMSNLT FLNDASVLYN LKARYAAMLI YTYSGLFCVV
INPYKRLPIY TDSVARMFMG KRRTEMPPHL FAVSDEAYRN MLQNHENQSM LITGESGAGK
TENTKKVISY FAAVGAAQQE TFGAKKAATE EDKNKKKVTL EDQIVQTNPV LEAFGNAKTV
RNNNSSRFGK FIRIHFSKQG RVASCDIEHY LLEKSRVIRQ APGERCYHIF YQVFSDYLPN
LKKDLLLNKP VKDYWFIAQA ELIIDGINDK EEHQLTDEAF DILKFTPTEK MECYRLVAAM
MHMGNMKFKQ RPREEQAEPD GTDDAERAAK CFGIDSEEFL KALTRPRVKV GNEWVNKGQN
IEQVNWAVGA MAKGLYSRIF NWLVKKCNQT LDQKGISRDH FIGVLDIAGF EIFDFNSFEQ
LWINFVNEKL QQFFNHHMFV LEQEEYAREG IQWTFIDFGL DLQACIELIE KPLGIIAMLD
EECIVPKATD LTLAQKLIDQ HLGKHPNFEK PKPPKGKQAE AHFAMRHYAG TVRYNCLNWL
EKNKDPLNDT VVTVMKASKE HALIVEVWQD YTTQEEAAAA AAKGTAGAKK KGKSGSFMTV
SMLYRESLNK LMTMLHSTHP HFIRCIIPNE KKASGVIDAG LVLNQLTCNG VLEGIRICRK
GFPNRTLHPD FVQRYALLAA DESIIGKTDA KKGSALMLAR LVKEKKLEEE NFRVGLTKVF
FKAGIVAHLE DLRDQSLAQL ITGLQAQIRW YYQTIERKRR VEKITALKII QRNIRSWAEL
RTWVWFKLYG KVKPLVNSGK IEAQYEKLQE TVATLKDTVV QEEEKKRQLQ EGAERLNKET
ADLLAQLEAS KGSTREVEER MTAMNEQKVA LEGKLADASK KLEVEEARAV EINKQKKLVE
AECADLKKNC QDVDLSLRKV EAEKNAKEHQ IRALQDEMRQ QDENISKLNK ERKNQEEQNK
KLTEDLQAAE EQNLAANKLK AKLMQSLEDS EQTMEREKRN RADMDKNKRK AEGELKIAQE
TLEELNKSKS DAENALRRKE TELHTLGMKL EDEQAAVAKL QKGIQQDEAR VKDLHDQLAD
EKDARQRADR SRADQQAEYD ELTEQLEDQA RATAAQIELG KKKDAELTKL RRDLEESGLK
FGEQLTVLKK KGSDAIQELS DQIEQLQKQK GRIEKEKGHM QREFDESSAA LDQEAKLRAD
QERIAKGYEV RLLELRLKAD EQSRQLQDFV SSKGRLNSEN SDLARQVEEL EAKIQAANRL
KLQFSNELDH AKRQAEEESR ERQNLSNLSK NLARELEQLK ESIEDEVAGK NEASRQLSKA
SVELDQWRTK FETEGLIGAD EFDEVKKRQN QKTSEIQDAL DACNAKIVAL ENARSRLTAE
ADANRLEAEH HAQAVSSLEK KQKAFDKVID EWKKKVDDLY LELDGAQRDA RQLSGEAHKL
RGQHDTLADQ VEGLRRENKS LSDETRDLTE SLSEGGRATH ALSKNLRRLE MEKEELQRGL
DEAEAALESE ESKALRCQIE VSQIRAEIEK RIAEKEEEFE NHRKVHQQTI DSIQATLDSE
TKAKSELFRV KKKLEADINE LEIALDHANK ANEDAQKNIR RYLDQIRELQ QTVDEEQKRR
EEFREHLLAA ERKLAVAKQE QEELIVKLEA LERARRVVES SVKEHQEHNN ELNSQNVALA
AAKSQLDNEI ALLNSDIAEA HTELSASEDR GRRAASDAAK LAEDLRHEQE QSQQLERFKK
QLESAVKDLQ ERADAAEAAV MKGGAKAIQK AEQRLKAFQS DLETESRRAG EASKTLARAD
RKVREFEFQV AEDKKNYDKL QELVEKLTAK LKLQKKQLEE AEEQANSHLS KYRTVQLSLE
TAEERADSAE QCLVRIRSRT RANAEQK
