MYSP_CAEEL
ID MYSP_CAEEL Reviewed; 872 AA.
AC P10567; B3WFV3; Q93214; Q93439;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Paramyosin;
DE AltName: Full=Uncoordinated protein 15;
GN Name=unc-15; ORFNames=F07A5.7;
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], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=2754728; DOI=10.1016/0022-2836(89)90257-x;
RA Kagawa H., Gengyo K., McLachlan A.D., Brenner S., Karn J.;
RT "Paramyosin gene (unc-15) of Caenorhabditis elegans. Molecular cloning,
RT nucleotide sequence and models for thick filament structure.";
RL J. Mol. Biol. 207:311-333(1989).
RN [2]
RP ERRATUM OF PUBMED:2754728.
RA Kagawa H., Gengyo K., McLachlan A.D., Brenner S., Karn J.;
RL J. Mol. Biol. 211:665-665(1990).
RN [3]
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 [4]
RP PHOSPHORYLATION.
RX PubMed=2754733; DOI=10.1016/0022-2836(89)90267-2;
RA Schriefer L.A., Waterston R.H.;
RT "Phosphorylation of the N-terminal region of Caenorhabditis elegans
RT paramyosin.";
RL J. Mol. Biol. 207:451-454(1989).
RN [5]
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).
RN [6]
RP FUNCTION, INTERACTION WITH UNC-89, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND REGION.
RX PubMed=27009202; DOI=10.1091/mbc.e15-09-0675;
RA Qadota H., Mayans O., Matsunaga Y., McMurry J.L., Wilson K.J., Kwon G.E.,
RA Stanford R., Deehan K., Tinley T.L., Ngwa V.M., Benian G.M.;
RT "The SH3 domain of UNC-89 (obscurin) interacts with paramyosin, a coiled-
RT coil protein, in Caenorhabditis elegans muscle.";
RL Mol. Biol. Cell 27:1606-1620(2016).
RN [7]
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).
CC -!- FUNCTION: Structural component of the muscle thick filaments which is
CC involved in assembly and organization of sarcomere myofilaments
CC (PubMed:2754728, PubMed:27009202). Involved in ovulation
CC (PubMed:17326220). Plays a role in the formation of muscle connections,
CC also called muscle arm extensions, between the body wall and the motor
CC axons in the dorsal and ventral cord (PubMed:27123983).
CC {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:27009202,
CC ECO:0000269|PubMed:27123983, ECO:0000269|PubMed:2754728}.
CC -!- SUBUNIT: Homodimer (Probable). May interact with unc-89 (via SH3
CC domain) (PubMed:27009202). {ECO:0000269|PubMed:27009202, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band
CC {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:27009202}.
CC Note=Localizes in punctate patterns along the myosin heavy chain myo-3
CC filaments in myoepithelial sheath cells. {ECO:0000269|PubMed:17326220}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F07A5.7a};
CC IsoId=P10567-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F07A5.7b};
CC IsoId=P10567-2; Sequence=VSP_058762;
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles of larvae and adults
CC (at protein level) (PubMed:27009202). Expressed in gonadal
CC myoepithelial sheath cells (at protein level) (PubMed:17326220).
CC {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:27009202}.
CC -!- DOMAIN: For most of its length, paramyosin appears to form an alpha-
CC helical coiled coil and shows the heptad repeat of hydrophobic amino
CC acid residues and the 28-residue repeat of charged amino acids
CC characteristic of myosin heavy chains. However, paramyosin differs from
CC myosin in having non-helical extensions at both termini and an
CC additional 'skip' residue that interrupts the 28-residue repeat. The
CC distribution of charged residues is also different from myosin heavy
CC chains.
CC -!- PTM: Phosphorylated on serine residues in the N-terminal non-helical
CC region. {ECO:0000269|PubMed:2754733}.
CC -!- DISRUPTION PHENOTYPE: Defective extension of body wall muscle
CC connections or arms towards the ventral nerve cord (PubMed:27123983).
CC Double knockout with madd-3 results in severe muscle arm extension
CC defects (PubMed:27123983). RNAi-mediated knockdown causes an
CC accumulation in the proximal gonad of endomitotic mature oocytes in 22
CC percent of animals (PubMed:17326220). {ECO:0000269|PubMed:17326220,
CC ECO:0000269|PubMed:27123983}.
CC -!- SIMILARITY: Belongs to the paramyosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30857.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X08068; CAA30857.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z72506; CAA96622.1; -; Genomic_DNA.
DR EMBL; Z79694; CAA96622.1; JOINED; Genomic_DNA.
DR EMBL; BX284601; CAQ76467.1; -; Genomic_DNA.
DR PIR; S04027; S04027.
DR PIR; T19296; T19296.
DR RefSeq; NP_001129763.1; NM_001136291.2.
DR RefSeq; NP_492085.1; NM_059684.5. [P10567-1]
DR AlphaFoldDB; P10567; -.
DR SMR; P10567; -.
DR BioGRID; 37933; 28.
DR DIP; DIP-24443N; -.
DR IntAct; P10567; 14.
DR MINT; P10567; -.
DR STRING; 6239.F07A5.7a.4; -.
DR EPD; P10567; -.
DR PaxDb; P10567; -.
DR PeptideAtlas; P10567; -.
DR EnsemblMetazoa; F07A5.7a.1; F07A5.7a.1; WBGene00006754. [P10567-1]
DR EnsemblMetazoa; F07A5.7a.2; F07A5.7a.2; WBGene00006754. [P10567-1]
DR EnsemblMetazoa; F07A5.7b.1; F07A5.7b.1; WBGene00006754. [P10567-2]
DR GeneID; 172491; -.
DR KEGG; cel:CELE_F07A5.7; -.
DR UCSC; F07A5.7.1; c. elegans. [P10567-1]
DR CTD; 172491; -.
DR WormBase; F07A5.7a; CE09197; WBGene00006754; unc-15. [P10567-1]
DR WormBase; F07A5.7b; CE42754; WBGene00006754; unc-15. [P10567-2]
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000173651; -.
DR HOGENOM; CLU_000192_13_6_1; -.
DR InParanoid; P10567; -.
DR OMA; FELPYSH; -.
DR OrthoDB; 251768at2759; -.
DR PhylomeDB; P10567; -.
DR SignaLink; P10567; -.
DR PRO; PR:P10567; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006754; Expressed in larva and 4 other tissues.
DR GO; GO:0031672; C:A band; IDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IDA:WormBase.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IMP:UniProtKB.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:WormBase.
DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IMP:WormBase.
DR Gene3D; 1.20.5.370; -; 1.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF01576; Myosin_tail_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Motor protein; Muscle protein; Myosin; Phosphoprotein;
KW Reference proteome; Thick filament.
FT CHAIN 1..872
FT /note="Paramyosin"
FT /id="PRO_0000211246"
FT REGION 1..31
FT /note="Nonhelical region"
FT /evidence="ECO:0000255"
FT REGION 294..376
FT /note="Interaction with unc-89"
FT /evidence="ECO:0000269|PubMed:27009202"
FT REGION 856..866
FT /note="Nonhelical region"
FT /evidence="ECO:0000255"
FT COILED 32..851
FT /evidence="ECO:0000255"
FT DISULFID 127
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 616
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..319
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058762"
SQ SEQUENCE 872 AA; 100634 MW; D3146CC6547EBD75 CRC64;
MSLYRSPSAA LLKSPSQAAF GAPFGSMSVA DLGSLTRLED KIRLLQEDLE SERELRNRVE
RERADLSVQV IALTDRLEDA EGTTDSQIES NRKREGELSK LRKLLEESQL ESEDAMNVLR
KKHQDSCLDY QDQIEQLQKK NAKIDRERQR VQHEVIELTA TIDQLQKDKH TAEKAAERFE
AQANELANKV EDLNKHVNDL AQQRQRLQAE NNDLLKEVHD QKVQLDNLQH VKYTLAQQLE
EARRRLEDAE RERSQLQSQL HQVQLELDSV RTALDEESIA RSDAEHKLNL ANTEITQWKS
KFDAEVALHH EEVEDLRKKM LQKQAEYEEQ IEIMLQKISQ LEKAKSRLQS EVEVLIVDLE
KAQNTIALLE RAREQLERQV GELKVRIDEI TVELEAAQRE LRAVNAELQK MKHLYEKAVE
QKEALARENK KLHDELHEAK EALADANRKL HELDLENARL AGEIRELQTA LKEADAQRRD
AENRAQRALA ELQALRIEME RRLQEKEEEM EALRKNLQFE IDRLIAALAD AEARMKSEIS
RLKKKYQAEI AELEMTVDNL NRANIEAQKT IKKQSEQLKI LQASLEDTQR QLQQVLDQYA
LAQRKVAALS AELEECKTAL DNAIRARKQA EVDLEEANGR ISDLISINNN LTSIKNKLET
ELSTAQADLD EVTKELHAAD ERANRALADA ARAVEQLHEE QEHSMKIDAL RKSLEEQVKQ
LQVQIQEAEA AALLGGKRVI AKLETRIRDL ETALDEETRR HKETQNALRK KDRRIKEVQQ
LVDEEHKNFV MAQDTADRLT EKLNIQKRQL AESESVTMQN LQRVRRYQHE LEDAEGRADQ
AESSLHLIRA KHRSSVVTGK SSSKIFVTED DY
