MYO4_CAEEL
ID MYO4_CAEEL Reviewed; 1963 AA.
AC P02566; O02244;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Myosin-4;
DE AltName: Full=Myosin heavy chain B;
DE Short=MHC B;
DE AltName: Full=Uncoordinated protein 54;
GN Name=unc-54; Synonyms=myo-4; ORFNames=F11C3.3;
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].
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 [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 847-1963.
RX PubMed=7202124; DOI=10.1038/299226a0;
RA McLachlan A.D., Karn J.;
RT "Periodic charge distributions in the myosin rod amino acid sequence match
RT cross-bridge spacings in muscle.";
RL Nature 299:226-231(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1873-1963.
RX PubMed=6571695; DOI=10.1016/0092-8674(83)90438-5;
RA Wills N., Gesteland R.F., Karn J., Barnett L., Bolten S., Waterston R.H.;
RT "The genes sup-7 X and sup-5 III of C. elegans suppress amber nonsense
RT mutations via altered transfer RNA.";
RL Cell 33:575-583(1983).
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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27123983; DOI=10.1371/journal.pgen.1006010;
RA D'Souza S.A., Rajendran L., Bagg R., Barbier L., van Pel D.M., Moshiri H.,
RA Roy P.J.;
RT "The MADD-3 LAMMER kinase interacts with a p38 MAP kinase pathway to
RT regulate the display of the EVA-1 guidance receptor in Caenorhabditis
RT elegans.";
RL PLoS Genet. 12:E1006010-E1006010(2016).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH UNC-45 AND UFD-2, INTERACTION WITH UNC-45
RP AND UFD-2, AND UBIQUITINATION.
RX PubMed=29396393; DOI=10.1038/s41467-018-02924-7;
RA Hellerschmied D., Roessler M., Lehner A., Gazda L., Stejskal K., Imre R.,
RA Mechtler K., Dammermann A., Clausen T.;
RT "UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins.";
RL Nat. Commun. 9:484-484(2018).
CC -!- FUNCTION: Required for muscle contraction.
CC {ECO:0000269|PubMed:27123983}.
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). Forms a complex composed of
CC chaperone unc-45, unc-54 and ubiquitin-protein ligase ufd-2; promotes
CC poly-ubiquitination of unfolded unc-54 (PubMed:29396393). Within the
CC complex interacts with unc-45 (via UCS domain) and ufd-2
CC (PubMed:29396393). Interacts with itr-1 (via c-terminal coiled coil
CC domain) (PubMed:12062062). {ECO:0000269|PubMed:12062062,
CC ECO:0000269|PubMed:29396393}.
CC -!- INTERACTION:
CC P02566; G5EG62: unc-45; NbExp=3; IntAct=EBI-329238, EBI-6675165;
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 -!- PTM: Unfolded unc-54 is poly-ubiquitinated by ufd-2.
CC {ECO:0000269|PubMed:29396393}.
CC -!- DISRUPTION PHENOTYPE: Viable, but paralyzed. Double knockout with madd-
CC 3 results in lethality. Triple knockout with madd-3, and either cebp-1,
CC dlk-1, mak-2, pmk-3 or sek-3 results in paralysis (as in the unc-54
CC single knockout), and suppresses the lethality phenotype in the double
CC madd-3 and unc-54 mutant. {ECO:0000269|PubMed:27123983}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28124.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; J01050; AAA28124.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z81499; CAB04089.1; -; Genomic_DNA.
DR EMBL; Z83107; CAB04089.1; JOINED; Genomic_DNA.
DR EMBL; V01494; CAA24738.1; -; Genomic_DNA.
DR PIR; T20770; MWKW.
DR RefSeq; NP_493596.1; NM_061195.4.
DR PDB; 6QDJ; X-ray; 1.88 A; A=1-790.
DR PDBsum; 6QDJ; -.
DR AlphaFoldDB; P02566; -.
DR SMR; P02566; -.
DR BioGRID; 56866; 27.
DR DIP; DIP-26548N; -.
DR IntAct; P02566; 6.
DR MINT; P02566; -.
DR STRING; 6239.F11C3.3.1; -.
DR iPTMnet; P02566; -.
DR EPD; P02566; -.
DR PaxDb; P02566; -.
DR PeptideAtlas; P02566; -.
DR PRIDE; P02566; -.
DR EnsemblMetazoa; F11C3.3.1; F11C3.3.1; WBGene00006789.
DR GeneID; 259839; -.
DR KEGG; cel:CELE_F11C3.3; -.
DR UCSC; F11C3.3.1; c. elegans.
DR CTD; 259839; -.
DR WormBase; F11C3.3; CE09349; WBGene00006789; unc-54.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00970000196537; -.
DR HOGENOM; CLU_000192_8_0_1; -.
DR InParanoid; P02566; -.
DR OMA; YFVSQGK; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P02566; -.
DR PRO; PR:P02566; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006789; Expressed in larva and 6 other tissues.
DR GO; GO:0031672; C:A band; IDA:UniProtKB.
DR GO; GO:0005859; C:muscle myosin complex; IDA: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:0005863; C:striated muscle myosin thick filament; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:WormBase.
DR GO; GO:0008307; F:structural constituent of muscle; IDA:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0006936; P:muscle contraction; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IMP:WormBase.
DR Gene3D; 1.20.5.370; -; 4.
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 3D-structure; Actin-binding; ATP-binding; Coiled coil; Cytoplasm;
KW Methylation; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW Reference proteome; Thick filament; Ubl conjugation.
FT CHAIN 1..1963
FT /note="Myosin-4"
FT /id="PRO_0000123383"
FT DOMAIN 28..77
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 81..787
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 662..684
FT /note="Actin-binding"
FT REGION 766..780
FT /note="Actin-binding"
FT REGION 848..1161
FT /note="Alpha-helical tailpiece (S2)"
FT REGION 970..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1963
FT /note="Light meromyosin (LMM)"
FT REGION 1162..1173
FT /note="Hinge"
FT REGION 1317..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..1963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 848..1963
FT /evidence="ECO:0000255"
FT COMPBIAS 970..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1928..1952
FT /note="Polar 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 1334
FT /note="E -> R (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1877
FT /note="I -> L (in Ref. 3)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:6QDJ"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:6QDJ"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 214..229
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 293..298
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:6QDJ"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 341..357
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 377..386
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 390..398
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 415..444
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 472..503
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 512..516
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 517..524
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 529..536
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 544..555
FT /evidence="ECO:0007829|PDB:6QDJ"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 593..598
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 603..610
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 616..621
FT /evidence="ECO:0007829|PDB:6QDJ"
FT TURN 622..624
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 628..631
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 654..669
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 672..680
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 693..702
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 705..714
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 722..729
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 730..732
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 734..737
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 743..757
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 762..764
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 765..767
FT /evidence="ECO:0007829|PDB:6QDJ"
FT STRAND 769..774
FT /evidence="ECO:0007829|PDB:6QDJ"
FT HELIX 778..789
FT /evidence="ECO:0007829|PDB:6QDJ"
SQ SEQUENCE 1963 AA; 224755 MW; D653C86050E846C6 CRC64;
MEHEKDPGWQ YLRRTREQVL EDQSKPYDSK KNVWIPDPEE GYLAGEITAT KGDQVTIVTA
RGNEVTLKKE LVQEMNPPKF EKTEDMSNLS FLNDASVLHN LRSRYAAMLI YTYSGLFCVV
INPYKRLPIY TDSCARMFMG KRKTEMPPHL FAVSDEAYRN MLQDHENQSM LITGESGAGK
TENTKKVICY FAAVGASQQE GGAEVDPNKK KVTLEDQIVQ TNPVLEAFGN AKTVRNNNSS
RFGKFIRIHF NKHGRLASCD IEHYLLEKSR VIRQAPGERC YHIFYQIYSD FRPELKKELL
LDLPIKDYWF VAQAELIIDG IDDVEEFQLT DEAFDILNFS AVEKQDCYRL MSAHMHMGNM
KFKQRPREEQ AEPDGTDEAE KASNMYGIGC EEFLKALTKP RVKVGTEWVS KGQNCEQVNW
AVGAMAKGLY SRVFNWLVKK CNLTLDQKGI DRDYFIGVLD IAGFEIFDFN SFEQLWINFV
NEKLQQFFNH HMFVLEQEEY AREGIQWVFI DFGLDLQACI ELIEKPLGII SMLDEECIVP
KATDLTLASK LVDQHLGKHP NFEKPKPPKG KQGEAHFAMR HYAGTVRYNC LNWLEKNKDP
LNDTVVSAMK QSKGNDLLVE IWQDYTTQEE AAAKAKEGGG GGKKKGKSGS FMTVSMLYRE
SLNNLMTMLN KTHPHFIRCI IPNEKKQSGM IDAALVLNQL TCNGVLEGIR ICRKGFPNRT
LHPDFVQRYA ILAAKEAKSD DDKKKCAEAI MSKLVNDGSL SEEMFRIGLT KVFFKAGVLA
HLEDIRDEKL ATILTGFQSQ IRWHLGLKDR KRRMEQRAGL LIVQRNVRSW CTLRTWEWFK
LYGKVKPMLK AGKEAEELEK INDKVKALED SLAKEEKLRK ELEESSAKLV EEKTSLFTNL
ESTKTQLSDA EERLAKLEAQ QKDASKQLSE LNDQLADNED RTADVQRAKK KIEAEVEALK
KQIQDLEMSL RKAESEKQSK DHQIRSLQDE MQQQDEAIAK LNKEKKHQEE INRKLMEDLQ
SEEDKGNHQN KVKAKLEQTL DDLEDSLERE KRARADLDKQ KRKVEGELKI AQENIDESGR
QRHDLENNLK KKESELHSVS SRLEDEQALV SKLQRQIKDG QSRISELEEE LENERQSRSK
ADRAKSDLQR ELEELGEKLD EQGGATAAQV EVNKKREAEL AKLRRDLEEA NMNHENQLGG
LRKKHTDAVA ELTDQLDQLN KAKAKVEKDK AQAVRDAEDL AAQLDQETSG KLNNEKLAKQ
FELQLTELQS KADEQSRQLQ DFTSLKGRLH SENGDLVRQL EDAESQVNQL TRLKSQLTSQ
LEEARRTADE EARERQTVAA QAKNYQHEAE QLQESLEEEI EGKNEILRQL SKANADIQQW
KARFEGEGLL KADELEDAKR RQAQKINELQ EALDAANSKN ASLEKTKSRL VGDLDDAQVD
VERANGVASA LEKKQKGFDK IIDEWRKKTD DLAAELDGAQ RDLRNTSTDL FKAKNAQEEL
AEVVEGLRRE NKSLSQEIKD LTDQLGEGGR SVHEMQKIIR RLEIEKEELQ HALDEAEAAL
EAEESKVLRA QVEVSQIRSE IEKRIQEKEE EFENTRKNHA RALESMQASL ETEAKGKAEL
LRIKKKLEGD INELEIALDH ANKANADAQK NLKRYQEQVR ELQLQVEEEQ RNGADTREQF
FNAEKRATLL QSEKEELLVA NEAAERARKQ AEYEAADARD QANEANAQVS SLTSAKRKLE
GEIQAIHADL DETLNEYKAA EERSKKAIAD ATRLAEELRQ EQEHSQHVDR LRKGLEQQLK
EIQVRLDEAE AAALKGGKKV IAKLEQRVRE LESELDGEQR RFQDANKNLG RADRRVRELQ
FQVDEDKKNF ERLQDLIDKL QQKLKTQKKQ VEEAEELANL NLQKYKQLTH QLEDAEERAD
QAENSLSKMR SKSRASASVA PGLQSSASAA VIRSPSRARA SDF
