MYO1_CAEEL
ID MYO1_CAEEL Reviewed; 1938 AA.
AC P02567; Q19674;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Myosin-1 {ECO:0000312|WormBase:R06C7.10};
DE AltName: Full=Myosin heavy chain D {ECO:0000303|PubMed:2926820};
DE Short=MHC D {ECO:0000303|PubMed:2926820};
GN Name=myo-1 {ECO:0000312|WormBase:R06C7.10};
GN ORFNames=R06C7.10 {ECO:0000312|WormBase:R06C7.10};
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 34-1795.
RX PubMed=6576334; DOI=10.1073/pnas.80.14.4253;
RA Karn J., Brenner S., Barnett L.;
RT "Protein structural domains in the Caenorhabditis elegans unc-54 myosin
RT heavy chain gene are not separated by introns.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4253-4257(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-365 AND 1492-1763.
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 [5]
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 (via c-
CC terminal coiled coil domain). {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; X08065; CAA30854.1; -; Genomic_DNA.
DR EMBL; Z71266; CAA95848.1; -; Genomic_DNA.
DR EMBL; Z71261; CAA95848.1; JOINED; Genomic_DNA.
DR EMBL; M37232; AAA28119.1; -; Genomic_DNA.
DR EMBL; M37234; AAA28120.1; -; Genomic_DNA.
DR PIR; T21193; MWKW1.
DR RefSeq; NP_492053.1; NM_059652.4.
DR AlphaFoldDB; P02567; -.
DR SMR; P02567; -.
DR BioGRID; 37913; 13.
DR DIP; DIP-24827N; -.
DR STRING; 6239.R06C7.10.1; -.
DR iPTMnet; P02567; -.
DR EPD; P02567; -.
DR PaxDb; P02567; -.
DR PeptideAtlas; P02567; -.
DR EnsemblMetazoa; R06C7.10.1; R06C7.10.1; WBGene00002348.
DR GeneID; 172471; -.
DR KEGG; cel:CELE_R06C7.10; -.
DR UCSC; R06C7.10.1; c. elegans.
DR CTD; 172471; -.
DR WormBase; R06C7.10; CE06253; WBGene00002348; myo-1.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_8_0_1; -.
DR InParanoid; P02567; -.
DR OMA; TWDWFLL; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P02567; -.
DR PRO; PR:P02567; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002348; Expressed in larva and 3 other tissues.
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:WormBase.
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; IBA:GO_Central.
DR GO; GO:0008307; F:structural constituent of muscle; IDA:WormBase.
DR GO; GO:0006936; P:muscle contraction; IMP:WormBase.
DR GO; GO:0043050; P:pharyngeal pumping; IMP:WormBase.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR Gene3D; 1.20.5.370; -; 3.
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..1938
FT /note="Myosin-1"
FT /id="PRO_0000123380"
FT DOMAIN 30..80
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 84..785
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..682
FT /note="Actin-binding"
FT REGION 764..778
FT /note="Actin-binding"
FT REGION 846..1938
FT /note="Rodlike tail (S2 and LMM domains)"
FT REGION 846..1170
FT /note="Alpha-helical tailpiece (short S2)"
FT REGION 919..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1938
FT /note="Light meromyosin (LMM)"
FT COILED 846..1938
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 128
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT CONFLICT 94
FT /note="F -> E (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="A -> R (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="D -> V (in Ref. 1; CAA30854)"
FT /evidence="ECO:0000305"
FT CONFLICT 389..390
FT /note="DV -> GD (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="D -> V (in Ref. 1; CAA30854)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="W -> N (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="Q -> G (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="F -> L (in Ref. 1; CAA30854)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="N -> I (in Ref. 1; CAA30854)"
FT /evidence="ECO:0000305"
FT CONFLICT 1373
FT /note="S -> D (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1659
FT /note="E -> Q (in Ref. 4; AAA28120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1938 AA; 223323 MW; 2569618A19034E4C CRC64;
MSLEHEKDPG WQYLKRSREQ QLADQSRPYD SKKNVWIPDA EEGYIEGVIK GPGPKADTVI
VTAGGKDVTL KKDIVQEVNP PKFEKTEDMS NLTFLNDASV LWNLRSRYAA MLIYTYSGLF
CVVINPYKRL PIYTDSVARM FMGKRRTEMP PHLFAVSDQA YRYMLQDHEN QSMLITGESG
AGKTENTKKV ICYFATVGAS QKAALKEGEK EVTLEDQIVQ TNPVLEAFGN AKTVRNNNSS
RFGKFIRIHF NKHGTLASCD IEHYLLEKSR VIRQAPGERC YHIFYQIYSD FKPQLRDELL
LNHPISNYWF VAQAELLIDG IDDTEEFQLT DEAFDVLKFS PTEKMDCYRL MSAHMHMGNM
KFKQRPREEQ AEPDGQDEAE RACNMYGIDV DQFLKALVSP RVKVGTEWVS KGQNVDQVHW
AIGAMAKGLY ARVFHWLVKK CNLTLDQKGI DRDYFIGVLD IAGFEIFDFN SFEQLWINFV
NEKLQQFFNH HMFVLEQEEY AREGIQWTFI DFGLDLQACI ELIEKPLGII SMLDEECIVP
KATDMTLAQK LTDQHLGKHP NFEKPKPPKG KQGEAHFAMR HYAGTVRYNV LNWLEKNKDP
LNDTVVSVMK ASKKNDLLVE IWQDYTTQEE AAAAAKAGGG RKGGKSGSFM TVSMMYRESL
NKLMTMLHKT HPHFIRCIIP NEKKQSGMID AALVLNQLTC NGVLEGIRIC RKGFPNRTQH
PDFVQRYAIL AAKEAKSSDD MKTCAGAILQ ALINQKQLND EQFRIGHTKV FFKAGVVAHI
EDLRDDKLNQ IITGFQSAIR WYTATADAGA RRKQLNSYII LQRNIRSWCV LRTWDWFLLF
GKLRPQLKCG KMAEEMIKMA EEQKVLEAEA KKAESARKSQ EEAYAKLSAE RSKLLEALEL
TQGGSAAIEE KLTRLNSARQ EVEKSLNDAN DRLSEHEEKN ADLEKQRRKA QQEVENLKKS
IEAVDGNLAK SLEEKAAKEN QIHSLQDEMN SQDETIGKIN KEKKLLEENN RQLVDDLQAE
EAKQAQANRL RGKLEQTLDE MEEAVEREKR IRAETEKSKR KVEGELKGAQ ETIDELSAIK
LETDASLKKK EADIHALGVR IEDEQALANR LTRQSKENAQ RIIEIEDELE HERQSRSKAD
RARAELQREL DELNERLDEQ NKQLEIQQDN NKKKDSEIIK FRRDLDEKNM ANEDQMAMIR
RKNNDQISAL TNTLDALQKS KAKIEKEKGV LQKELDDINA QVDQETKSRV EQERLAKQYE
IQVAELQQKV DEQSRQIGEY TSTKGRLSND NSDLARQVEE LEIHLATINR AKTAFSSQLV
EAKKAAEDEL HERQEFHAAC KNLEHELDQC HELLEEQING KDDIQRQLSR INSEISQWKA
RYEGEGLVGS EELEELKRKQ MNRVMDLQEA LSAAQNKVIS LEKAKGKLLA ETEDARSDVD
RHLTVIASLE KKQRAFDKIV DDWKRKVDDI QKEIDATTRD SRNTSTEVFK LRSSMDNLSE
QIETLRRENK IFSQEIRDIN EQITQGGRTY QEVHKSVRRL EQEKDELQHA LDEAEAALEA
EESKVLRLQI EVQQIRSEIE KRIQEKEEEF ENTRKNHQRA LESIQASLET EAKSKAELAR
AKKKLETDIN QLEIALDHAN KANVDAQKNL KKLFDQVKEL QGQVDDEQRR REEIRENYLA
AEKRLAIALS ESEDLAHRIE ASDKHKKQLE IEQAELKSSN TELIGNNAAL SAMKRKVENE
VQIARNELDE YLNELKASEE RARKAAADAD RLAEEVRQEQ EHAVHVDRQR KSLELNAKEL
QAKIDDAERA MIQFGAKALA KVEDRVRSLE AELHSEQRRH QESIKGYTKQ ERRARELQFQ
VEEDKKAFDR LQENVEKLQQ KIRVQKRQIE EAEEVATQNL SKFRQIQLAL ENAEERAEVA
ENSLVRMRGQ VVRSATNK
