DYC1_CAEEL
ID DYC1_CAEEL Reviewed; 887 AA.
AC Q8STF6; Q93325; Q9XZQ6;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Dystrophin-like protein 1;
DE AltName: Full=Dyb-1-binding and CAPON-related protein;
GN Name=dyc-1 {ECO:0000312|WormBase:C33G3.1b};
GN ORFNames=C33G3.1 {ECO:0000312|WormBase:C33G3.1b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB44432.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB44432.1};
RX PubMed=10996789; DOI=10.1016/s0960-9822(00)00691-6;
RA Gieseler K., Grisoni K., Segalat L.;
RT "Genetic suppression of phenotypes arising from mutations in dystrophin-
RT related genes in Caenorhabditis elegans.";
RL Curr. Biol. 10:1092-1097(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INTERACTION WITH ZYX-1.
RX PubMed=18094057; DOI=10.1091/mbc.e07-05-0497;
RA Lecroisey C., Martin E., Mariol M.C., Granger L., Schwab Y., Labouesse M.,
RA Segalat L., Gieseler K.;
RT "DYC-1, a protein functionally linked to dystrophin in Caenorhabditis
RT elegans is associated with the dense body, where it interacts with the
RT muscle LIM domain protein ZYX-1.";
RL Mol. Biol. Cell 19:785-796(2008).
CC -!- FUNCTION: Together with dys-1 and hlh-1, participates in a common
CC muscular function. {ECO:0000269|PubMed:10996789}.
CC -!- SUBUNIT: Component of the dystrophin glycoprotein complex (DGC)
CC (PubMed:10996789). Interacts with zyx-1 (PubMed:18094057).
CC {ECO:0000269|PubMed:18094057, ECO:0000303|PubMed:10996789,
CC ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000303|PubMed:9851916}; Synonyms=DYC-1S
CC {ECO:0000303|PubMed:18094057};
CC IsoId=Q8STF6-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:10996789}; Synonyms=DYC-1L
CC {ECO:0000303|PubMed:18094057};
CC IsoId=Q8STF6-2; Sequence=VSP_051611, VSP_051612;
CC -!- TISSUE SPECIFICITY: Expressed in muscles of the head, body wall and
CC vulva (PubMed:10996789, PubMed:18094057). In some animals, weaker
CC expression is observed in the intestinal muscles (at protein level)
CC (PubMed:10996789). Isoform a is expressed in lateral neurons SDQL and
CC SDQR (PubMed:18094057). {ECO:0000269|PubMed:10996789,
CC ECO:0000269|PubMed:18094057}.
CC -!- DISRUPTION PHENOTYPE: Mutants synergistically exhibit progressive
CC myopathy. Overexpression of dyc-1 in dys-1 and hlh-1 double mutants,
CC delays but does not prevent the progression of myopathy due to
CC reduction in the proportion of abnormal muscles (PubMed:10996789).
CC Also, reduces the locomotion and egg laying defects (PubMed:10996789).
CC RNAi-mediated knock-down of isoform b induces a dys-1-like behavioral
CC phenotype consisting of hyperactivity, exagerated head bending and a
CC tendency to hypercontract (PubMed:18094057).
CC {ECO:0000269|PubMed:10996789, ECO:0000269|PubMed:18094057}.
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DR EMBL; AJ133838; CAB44432.1; -; mRNA.
DR EMBL; Z78540; CAB01738.2; -; Genomic_DNA.
DR EMBL; Z78540; CAD30431.1; -; Genomic_DNA.
DR EMBL; Z72501; CAD30431.1; JOINED; Genomic_DNA.
DR PIR; T19690; T19690.
DR RefSeq; NP_001024439.1; NM_001029268.3. [Q8STF6-1]
DR RefSeq; NP_741925.2; NM_171796.3. [Q8STF6-2]
DR AlphaFoldDB; Q8STF6; -.
DR SMR; Q8STF6; -.
DR BioGRID; 46414; 5.
DR DIP; DIP-24627N; -.
DR IntAct; Q8STF6; 4.
DR STRING; 6239.C33G3.1b.1; -.
DR EPD; Q8STF6; -.
DR PaxDb; Q8STF6; -.
DR PeptideAtlas; Q8STF6; -.
DR EnsemblMetazoa; C33G3.1a.1; C33G3.1a.1; WBGene00001116. [Q8STF6-2]
DR EnsemblMetazoa; C33G3.1b.1; C33G3.1b.1; WBGene00001116. [Q8STF6-1]
DR EnsemblMetazoa; C33G3.1b.2; C33G3.1b.2; WBGene00001116. [Q8STF6-1]
DR GeneID; 181515; -.
DR KEGG; cel:CELE_C33G3.1; -.
DR UCSC; C33G3.1b.2; c. elegans. [Q8STF6-1]
DR CTD; 181515; -.
DR WormBase; C33G3.1a; CE24825; WBGene00001116; dyc-1. [Q8STF6-2]
DR WormBase; C33G3.1b; CE30500; WBGene00001116; dyc-1. [Q8STF6-1]
DR eggNOG; KOG4458; Eukaryota.
DR eggNOG; KOG4815; Eukaryota.
DR GeneTree; ENSGT00940000169335; -.
DR InParanoid; Q8STF6; -.
DR OMA; FSRMSFN; -.
DR OrthoDB; 1463813at2759; -.
DR PhylomeDB; Q8STF6; -.
DR SignaLink; Q8STF6; -.
DR PRO; PR:Q8STF6; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001116; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IGI:UniProtKB.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IBA:GO_Central.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; NAS:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; IDA:WormBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0046662; P:regulation of oviposition; IMP:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; IGI:WormBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Reference proteome.
FT CHAIN 1..887
FT /note="Dystrophin-like protein 1"
FT /id="PRO_0000086881"
FT DOMAIN 30..197
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 176..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..506
FT /evidence="ECO:0000255"
FT COMPBIAS 176..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:10996789,
FT ECO:0000303|PubMed:9851916"
FT /id="VSP_051611"
FT VAR_SEQ 95..151
FT /note="KEKGLSWDESKLLVMFHPIYRIFYVSHDSQDLQIFSYIARDGASNTFKCNVF
FT KCSKK -> MIRFDPDESSEMSEEKRFYYLRLMAKPGGKPIKTKFVTWSRDEDVASASN
FT ISDQQLE (in isoform a)"
FT /evidence="ECO:0000303|PubMed:10996789,
FT ECO:0000303|PubMed:9851916"
FT /id="VSP_051612"
SQ SEQUENCE 887 AA; 99568 MW; 4479D811513A9CA5 CRC64;
MPVRKKHGPY DIIADDVYDC RIPLHNELAY QHGIHFEAKY VGSMEIPRPG TRIEIVAAMR
RVRYEFKARG IKKRPVDITV SVDGVKVVLQ RKKQKEKGLS WDESKLLVMF HPIYRIFYVS
HDSQDLQIFS YIARDGASNT FKCNVFKCSK KSQAMRVVRT IGQAFEVCHK VAQDQMQEKH
EDEAAKSKIS MQSEDEAGPN ALDVIEERGG REEDSRSSSP MEAPPVGGPL YGKRLSLFQP
RKPSTTSSSG GTAIDTTAIP ENVLEIPNTS HPILQPKAPE LVPQLQPQTA LPYQQKPQSL
LNIQQQQFNT LPSQMPSTQT LPSLSENPGQ SHIPRMMTMP PNMPYPTATL PHPRTWAPQI
PSYPNSMQSL EQNVPMYYPQ MPGMLPSSSS LPFGLSSPVM VSPYATLQLN MQSQQLDQPD
HSGSQITMDQ YNQQLMRSQL DQAQQSVQVA GCQVQLLRDQ LTSETTARLE AQSRTHQLLS
ANRDLLEQVQ NLVSRLQMLE TKITSEIHHS SSQPPQHQPI YQPSTSTPLN PKMPLSIDHN
DPRIPGNSSI RLNYPYQVQP LADLRAGSLP PVKESKERRK DEGTRTEPES NAEDTTDYSS
SDQYERTSNV MKPSHFNILM SNPLVDINVP SGAAMSSRME QFDMGDTPGT SSTPPKKEKK
PSSGILRGEN FSRMSFNPKL GREKEREQQQ LMFEDTLEDD SPRSIPPSPP SKARNTTIDS
LFKPQDDPPT IADREPQQLP PQPSQQNQKK NTAVNLLMPT MPASSSLVTA MYPPMRQPAV
PVNKIQPKVD VFRKKTLKTL SMDIAEEPEP SEMDPNRNNL PSSTNSSMKR RGFLPPPNTD
VEIKEIEDYI NRNVDRSKLP ETSLLTRLTR QAQGDNSLGN LPNGYPQ
