DLG1_CAEEL
ID DLG1_CAEEL Reviewed; 967 AA.
AC G5ECY0; Q7Z124;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Disks large homolog 1 {ECO:0000305};
DE AltName: Full=MAGUK protein DLG-1;
DE AltName: Full=SAP97-like protein DLG-1;
GN Name=dlg-1 {ECO:0000312|WormBase:C25F6.2a};
GN ORFNames=C25F6.2 {ECO:0000312|WormBase:C25F6.2a}, CELE_C25F6.2;
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 [MRNA].
RX PubMed=11493666; DOI=10.1242/jcs.114.12.2265;
RA McMahon L., Legouis R., Vonesch J.L., Labouesse M.;
RT "Assembly of C. elegans apical junctions involves positioning and
RT compaction by LET-413 and protein aggregation by the MAGUK protein DLG-1.";
RL J. Cell Sci. 114:2265-2277(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11694581; DOI=10.1091/mbc.12.11.3465;
RA Firestein B.L., Rongo C.;
RT "DLG-1 is a MAGUK similar to SAP97 and is required for adherens junction
RT formation.";
RL Mol. Biol. Cell 12:3465-3475(2001).
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH AJM-1,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=11715019; DOI=10.1038/ncb1101-983;
RA Koeppen M., Simske J.S., Sims P.A., Firestein B.L., Hall D.H., Radice A.D.,
RA Rongo C., Hardin J.D.;
RT "Cooperative regulation of AJM-1 controls junctional integrity in
RT Caenorhabditis elegans epithelia.";
RL Nat. Cell Biol. 3:983-991(2001).
RN [5]
RP FUNCTION, SUBUNIT, INTERACTION WITH AJM-1, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=18411252; DOI=10.1242/jcs.017137;
RA Lockwood C.A., Lynch A.M., Hardin J.;
RT "Dynamic analysis identifies novel roles for DLG-1 subdomains in AJM-1
RT recruitment and LET-413-dependent apical focusing.";
RL J. Cell Sci. 121:1477-1487(2008).
CC -!- FUNCTION: Essential multidomain scaffolding protein required for normal
CC development (Probable). Recruits channels, receptors and signaling
CC molecules to discrete plasma membrane domains in polarized cells (By
CC similarity). Required for proper embryonic elongation. Acts upstream of
CC ajm-1 and becomes localized to apical junctions independently of ajm-1.
CC With let-413, cooperatively regulates ajm-1 localization to apical
CC junctions (PubMed:11715019, PubMed:18411252).
CC {ECO:0000250|UniProtKB:Q12959, ECO:0000269|PubMed:11715019,
CC ECO:0000305|PubMed:11715019, ECO:0000305|PubMed:18411252}.
CC -!- SUBUNIT: Homooligomerizes; requires L27 domain (PubMed:18411252).
CC Interacts (via L27 domain) with ajm-1; the interaction regulates ajm-1
CC apical junction location (PubMed:11715019, PubMed:18411252).
CC {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:18411252}.
CC -!- INTERACTION:
CC G5ECY0; Q95ZY7: ajm-1; NbExp=3; IntAct=EBI-312458, EBI-11468703;
CC G5ECY0; H2L055: CELE_F53A10.2; NbExp=2; IntAct=EBI-312458, EBI-2413872;
CC G5ECY0; Q18426: prx-5; NbExp=4; IntAct=EBI-312458, EBI-316187;
CC G5ECY0; G5ECG0: tac-1; NbExp=3; IntAct=EBI-312458, EBI-320612;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11715019,
CC ECO:0000269|PubMed:18411252}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q12959}. Apical cell membrane
CC {ECO:0000269|PubMed:11715019}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:18411252}. Lateral
CC cell membrane {ECO:0000269|PubMed:18411252}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q12959}. Note=Localizes at the apical junctions
CC (PubMed:11715019, PubMed:18411252). Localization at the adherens
CC junctions requires PDZ domains, lateral distribution requires SH3
CC domain and is let-413 dependent (PubMed:18411252).
CC {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:18411252}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=G5ECY0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=G5ECY0-2; Sequence=VSP_059295, VSP_059296, VSP_059297;
CC -!- TISSUE SPECIFICITY: Expressed in the apical junctions in the
CC hypodermis. {ECO:0000269|PubMed:11715019}.
CC -!- DOMAIN: PDZ domains are required for localization at the adherens
CC junctions. SH3 domain is necessary for let-413 dependent lateral
CC distribution. L27 domain is responsible for homooligomerization and
CC interaction with ajm-1. {ECO:0000269|PubMed:18411252}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos have elongation arrested
CC immediately before or at the 2-fold stage. They display a large vacuole
CC in the posterior region. {ECO:0000269|PubMed:11715019,
CC ECO:0000269|PubMed:18411252}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000255}.
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DR EMBL; AJ295228; CAC35153.1; -; mRNA.
DR EMBL; AF406786; AAL01376.1; -; mRNA.
DR EMBL; BX284606; CCD65680.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD65681.1; -; Genomic_DNA.
DR RefSeq; NP_001024431.1; NM_001029260.2. [G5ECY0-1]
DR RefSeq; NP_001024432.1; NM_001029261.3.
DR AlphaFoldDB; G5ECY0; -.
DR SMR; G5ECY0; -.
DR IntAct; G5ECY0; 41.
DR STRING; 6239.C25F6.2a; -.
DR EPD; G5ECY0; -.
DR PaxDb; G5ECY0; -.
DR PeptideAtlas; G5ECY0; -.
DR ABCD; G5ECY0; 1 sequenced antibody.
DR EnsemblMetazoa; C25F6.2.1; C25F6.2.1; WBGene00001006. [G5ECY0-1]
DR GeneID; 180819; -.
DR KEGG; cel:CELE_C25F6.2; -.
DR CTD; 180819; -.
DR WormBase; C25F6.2a; CE36524; WBGene00001006; dlg-1. [G5ECY0-1]
DR WormBase; C25F6.2b; CE34261; WBGene00001006; dlg-1. [G5ECY0-2]
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000167723; -.
DR HOGENOM; CLU_001715_4_2_1; -.
DR InParanoid; G5ECY0; -.
DR OMA; TQHMENH; -.
DR OrthoDB; 807583at2759; -.
DR PhylomeDB; G5ECY0; -.
DR Reactome; R-CEL-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-CEL-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-CEL-5625900; RHO GTPases activate CIT.
DR Reactome; R-CEL-6794361; Neurexins and neuroligins.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8849932; Synaptic adhesion-like molecules.
DR SignaLink; G5ECY0; -.
DR PRO; PR:G5ECY0; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001006; Expressed in pharyngeal muscle cell (C elegans) and 10 other tissues.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0043296; C:apical junction complex; IDA:WormBase.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004385; F:guanylate kinase activity; ISS:WormBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
DR GO; GO:0045186; P:zonula adherens assembly; IMP:WormBase.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR015143; L27_1.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF09058; L27_1; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; SSF101288; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..967
FT /note="Disks large homolog 1"
FT /id="PRO_0000442929"
FT DOMAIN 5..65
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 202..289
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 361..448
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 510..591
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 619..690
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 769..955
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 324..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 2)"
FT /id="VSP_059295"
FT VAR_SEQ 434..438
FT /note="KNTGN -> NSLLT (in isoform 2)"
FT /id="VSP_059296"
FT VAR_SEQ 439..967
FT /note="Missing (in isoform 2)"
FT /id="VSP_059297"
SQ SEQUENCE 967 AA; 106992 MW; 44CDF119D6C6B368 CRC64;
MSHESSEKAH KAIENVEDYC QTLTRHGNEE LRTNLERVIT TFKSNLMHSL LDIHDLYEQT
LLSERKSDAE KNMEVRRVIE RLEGGPHSYN SRPAATTSTS NYNLSSTTPL ISDLRDRGGF
SYLNGGGLGN GLGNGLGNGL LSSPYNSSST HYLHERQRQT SHDGTWRETT TRTVDTPSGL
ERRVVEHTGV IDDHGRKWEL ENIVLEKGHT GLGFSITGGM DQPTEDGDTS IYVTNIIEGG
AALADGRMRK NDIITAVNNT NCENVKHEVA VNALKSSGNV VSLSLKRRKD EAFLPIGGNF
GGSTSYLRSG VTPSVSAGNL QHAIHSPSAP IHPPPPPPVH HGSLSQLSVG QYRSTRPNTS
VIDLVKGARG LGFSIAGGQG NEHVKGDTDI YVTKIIEEGA AELDGRLRVG DKILEVDHHS
LINTTHENAV NVLKNTGNRV RLLIQQGTGA IFNDSASQQF MPTTPILRPS SVQDYNRSQM
GSQSHLSYGG PLNTSYSSQA PIAIPLEPRP VQLVKGQNGL GFNIVGGEDN EPIYISFVLP
GGVADLSGNV KTGDVLLEVN GVVLRNATHK EAAEALRNAG NPVYLTLQYR PQEYQIFESK
IEKLRNDVIA QSRMGTLSRK SEYVRALFDY DPSRENSVAP HRSMGFNYGD ILHIINSSDD
EWWTARKVHE NGEETAEGVI PSKKRVEKRE RLRRKQVNFN SGSQSLGRNS STTGLENRRG
SRSQLSFSRK FPFVKSTDRL NDLNEESSNV AEEPVWSYQA VEQQAINYVR PVIILGALKD
RINDELVNRD PSKFSSCVPH TSRPPREGEV NGRDYYFVNK HNMEEDVKNN LFIEAGQFQN
NLYGTSIQSV RDVANQGRHC ILDVSGNAIR RLQSNANIQP ISIFIKPSSA QQILELDSQL
ATNRQDDRAM SGEEAQAQYS RCHRIEQTFG DLFTQEISNV HSANDVLSKV YSIISRESQT
PIWVPRH
