SpermatogenesisOnline 1.0
 

Tag Content
SG ID
SG00000128 
UniProt Accession
Theoretical PI
6.31  
Molecular Weight
106673 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
dlg1 
Gene Synonyms/Alias
l(1)dlg1 
Protein Name
Disks large 1 tumor suppressor protein 
Protein Synonyms/Alias
 
Organism
Drosophila melanogaster (Fruit fly) 
NCBI Taxonomy ID
7227 
Chromosome Location
chr:X;11263670-11302371;1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Temporarily unavailable 
The information of related literatures
1. F. Papagiannouli and B. M. Mechler (2009) discs large regulates somatic cyst cell survival and expansion in Drosophila testis. Cell Res 19(10): 1139-49. 

Abstract
Gonad development requires a coordinated soma-germline interaction that ensures renewal and differentiation of germline and somatic stem cells to ultimately produce mature gametes. The Drosophila tumour suppressor gene discs large (dlg) encodes a septate junction protein functioning during epithelial polarization, asymmetric neuroblast division, and formation of neuromuscular junctions. Here, we report the role of dlg in testis development and its critical function in somatic cyst cells (SCCs). In these cells dlg is primarily required for their survival and expansion, and contributes to spermatocyte cyst differentiation. Cell death primarily occurred in SCCs at the end of spermatogonial amplification at a time when Dlg becomes restricted in wild-type (wt) testes to the distal somatic cells capping the growing spermatocyte cysts. RNAi depletion of dlg transcripts in early SCCs fully prevented testis development, whereas depletion in late SCCs resulted in a breakdown of spermatocyte cyst structure and germ cell individualization. Specific dlg expression in SCCs resulted in developmental rescue of dlg mutant testes, whereas its expression in germ cells exerted no such effect. dlg overexpression in wt testes led to spermatocyte cyst expansion at the expense of spermatogonial cysts. Our data demonstrate that dlg is essentially required in SCCs for their survival, expansion, and differentiation, and for the encapsulation of the germline cells. PMID: [19546890] 

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Figures for illustrating the function of this protein/gene
Ref: F. Papagiannouli and B. M. Mechler (2009) discs large regulates somatic cyst cell survival and expansion in Drosophila testis. Cell Res 19(10): 1139-49. PMID: [19546890]
Ref: F. Papagiannouli and B. M. Mechler (2009) discs large regulates somatic cyst cell survival and expansion in Drosophila testis. Cell Res 19(10): 1139-49. PMID: [19546890]
Ref: F. Papagiannouli and B. M. Mechler (2009) discs large regulates somatic cyst cell survival and expansion in Drosophila testis. Cell Res 19(10): 1139-49. PMID: [19546890]
Ref: F. Papagiannouli and B. M. Mechler (2009) discs large regulates somatic cyst cell survival and expansion in Drosophila testis. Cell Res 19(10): 1139-49. PMID: [19546890]
Ref: F. Papagiannouli and B. M. Mechler (2009) discs large regulates somatic cyst cell survival and expansion in Drosophila testis. Cell Res 19(10): 1139-49. PMID: [19546890]
Ref: F. Papagiannouli and B. M. Mechler (2009) discs large regulates somatic cyst cell survival and expansion in Drosophila testis. Cell Res 19(10): 1139-49. PMID: [19546890]
Ref: F. Papagiannouli and B. M. Mechler (2009) discs large regulates somatic cyst cell survival and expansion in Drosophila testis. Cell Res 19(10): 1139-49. PMID: [19546890]
Function
During embryonic development, some isoforms areessential for proper neuronal differentiation and organization.Required for cell polarity; maintenance of apicobasal polarity.Plays a critical role at septate junctions in cellular growthcontrol during larval development. The presence of a guanylatekinase domain suggests involvement in cellular adhesion as well assignal transduction to control cellular proliferation. 
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Subcellular Location
Cytoplasm. Cell membrane; Peripheralmembrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Celljunction, septate junction. Note=Cytoskeleton- and membrane-associated. Located at the cytoplasmic face of the membrane in thecellular blastoderm and becomes associated with septate junctionswhich begin to form between epithelial cells at the time of dorsalclosure. In adult flies, located at the apical-lateral membraneboundary of epithelial cells. 
Tissue Specificity
During the cellular blastoderm stage, isoformB, isoform F, isoform H, isoform I and isoform L expression islocalized to the cell borders. From stage 11 onwards, expressionis found predominantly in the developing nervous system: axonbundles in the ventral cord and the brain. Stage 14 and 15 embryosexhibit expression in the developing body wall muscle. Expressionin neuropil regions of the CNS and at NMJs persists through tolarval development. Other isoforms show expression in embryonicepithelial cells. In larvae, expression is seen as a belt aroundsalivary glands, imaginal disks and proventriculus. Expressed inadult reproductive tissues. In epithelia, coexpressed with scribthroughout development. 
Gene Ontology
GO IDGO termEvidence
GO:0045179 C:apical cortex IDA:FlyBase.
GO:0016323 C:basolateral plasma membrane TAS:FlyBase.
GO:0005856 C:cytoskeleton IEA:UniProtKB-SubCell.
GO:0016328 C:lateral plasma membrane IDA:FlyBase.
GO:0031594 C:neuromuscular junction IDA:FlyBase.
GO:0048471 C:perinuclear region of cytoplasm IDA:FlyBase.
GO:0045211 C:postsynaptic membrane IDA:FlyBase.
GO:0005918 C:septate junction NAS:FlyBase.
GO:0043195 C:terminal button IDA:FlyBase.
GO:0004385 F:guanylate kinase activity TAS:FlyBase.
GO:0004871 F:signal transducer activity IEA:UniProtKB-KW.
GO:0005198 F:structural molecule activity TAS:FlyBase.
GO:0030714 P:anterior/posterior axis specification, follicular epithelium IMP:BHF-UCL.
GO:0045167 P:asymmetric protein localization involved in cell fate determination TAS:FlyBase.
GO:0045175 P:basal protein localization IMP:FlyBase.
GO:0007155 P:cell adhesion IEA:UniProtKB-KW.
GO:0060581 P:cell fate commitment involved in pattern specification IMP:BHF-UCL.
GO:0001708 P:cell fate specification IMP:BHF-UCL.
GO:0008283 P:cell proliferation TAS:FlyBase.
GO:0007391 P:dorsal closure NAS:FlyBase.
GO:0051294 P:establishment of spindle orientation IMP:FlyBase.
GO:0045197 P:establishment or maintenance of epithelial cell apical/basal polarity NAS:FlyBase.
GO:0045196 P:establishment or maintenance of neuroblast polarity TAS:FlyBase.
GO:0016332 P:establishment or maintenance of polarity of embryonic epithelium TAS:FlyBase.
GO:0016336 P:establishment or maintenance of polarity of larval imaginal disc epithelium NAS:FlyBase.
GO:0045475 P:locomotor rhythm IMP:FlyBase.
GO:0008049 P:male courtship behavior IMP:FlyBase.
GO:0001738 P:morphogenesis of a polarized epithelium TAS:FlyBase.
GO:0008285 P:negative regulation of cell proliferation TAS:FlyBase.
GO:0000122 P:negative regulation of transcription from RNA polymerase II promoter IMP:BHF-UCL.
GO:0007318 P:pole plasm protein localization IMP:BHF-UCL.
GO:0046956 P:positive phototaxis IMP:FlyBase.
GO:0030710 P:regulation of border follicle cell delamination TAS:FlyBase.
GO:0051726 P:regulation of cell cycle NAS:FlyBase.
GO:0042058 P:regulation of epidermal growth factor receptor signaling pathway IMP:BHF-UCL.
GO:0046425 P:regulation of JAK-STAT cascade IMP:BHF-UCL.
GO:0008593 P:regulation of Notch signaling pathway IMP:BHF-UCL.
GO:0019991 P:septate junction assembly TAS:FlyBase.
GO:0051124 P:synaptic growth at neuromuscular junction IMP:FlyBase.
GO:0007268 P:synaptic transmission IMP:FlyBase.
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Interpro
IPR008144;    Guanylate_kin.
IPR008145;    Guanylate_kin/L-typ_Ca_channel.
IPR020590;    Guanylate_kinase_CS.
IPR004172;    L27.
IPR015143;    L27_1.
IPR001478;    PDZ.
IPR001452;    SH3_domain.
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Pfam
PF00625;    Guanylate_kin;    1.
PF09058;    L27_1;    1.
PF00595;    PDZ;    3.
PF00018;    SH3_1;    1.
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SMART
SM00072;    GuKc;    1.
SM00569;    L27;    1.
SM00228;    PDZ;    3.
SM00326;    SH3;    1.
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PROSITE
PS00856;    GUANYLATE_KINASE_1;    1.
PS50052;    GUANYLATE_KINASE_2;    1.
PS51022;    L27;    1.
PS50106;    PDZ;    3.
PS50002;    SH3;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
CHAIN         1    970       Disks large 1 tumor suppressor protein.
                             /FTId=PRO_0000094538.
DOMAIN        4     64       L27.
DOMAIN      216    303       PDZ 1.
DOMAIN      330    421       PDZ 2.
DOMAIN      506    587       PDZ 3.
DOMAIN      620    690       SH3.
DOMAIN      780    955       Guanylate kinase-like.
MOD_RES     496    496       Phosphoserine.
MOD_RES     714    714       Phosphothreonine.
VAR_SEQ       1     92       MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIF
                             KSRLFQALLDIQEFYELTLLDDSKSIQQKTAETLQIATKWE
                             KDGQAVKIAD -> MIDWVSIVRHSRRRFSNYVGSRSPVRM
                             RRRRRQLTAPPPQQQQQQHYHQQQQQDQHQSRERQKKDKEK
                             EKETEKDNESGGGIGSRYACCCAN (in isoform K).
                             /FTId=VSP_039402.
VAR_SEQ       1     37       MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERV ->
                             MTTRKKKRDGGGSGGGFIKKVSSLFNLDSLHKASSTK (in
                             isoform A).
                             /FTId=VSP_011403.
VAR_SEQ       1     29       MPVKKQEAHRALELLEDYHARLSEPQDRA -> MTTRKKKR
                             DGGGSGGGFIKKVSSLFNLDS (in isoform E and
                             isoform G).
                             /FTId=VSP_011402.
VAR_SEQ       1      7       MPVKKQE -> MDSDTDSEREKSSDPNEGLLSSDDKTFHDD
                             DEPAEDSSPADDEEEPEEEECLLPQKKAQIRCDQDQPPLVV
                             LVQPSAEAIEVRQEIDDTNPVAVAAKASDMDGDSQLEVMEH
                             QMETVTEPDPEPPKCPTSLRDSVRESVECFYSAQDLLEYGH
                             MLSSTSMVRTPDVESGYFEKSESDASRDEWEGPSSSSSGAA
                             RCRLLSGISGLSVSSSSRHSAEGLRMELSRFRTMIETLERE
                             SLEKSQSELQLKAKSKAKPKPKQRSHVQDAAGESGSEQGSE
                             RGFWSTIFGQAGLAISQDEEERIADIQK (in isoform
                             F).
                             /FTId=VSP_011401.
VAR_SEQ      30    205       Missing (in isoform E and isoform G).
                             /FTId=VSP_011404.
VAR_SEQ      38    205       Missing (in isoform A).
                             /FTId=VSP_011405.
VAR_SEQ      93    151       Missing (in isoform I, isoform H, isoform
                             K and isoform L).
                             /FTId=VSP_011406.
VAR_SEQ     205    205       T -> TLHKASSTK (in isoform L).
                             /FTId=VSP_011407.
VAR_SEQ     206    267       VNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIY
                             ITKLISGGAAAADGRLSINDI -> SQIQIQSLTQTYPNAH
                             QRKRVLVSLHPHQHQHQSQIQHQHHYQLRHNNGIQAKMLKR
                             AFEST (in isoform I).
                             /FTId=VSP_011408.
VAR_SEQ     268    970       Missing (in isoform I).
                             /FTId=VSP_011409.
VAR_SEQ     473    519       EPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGP
                             QGLGFN -> AFMLCYTQDDANAEGGEIIYRVELPDMEQIT
                             LIYLENNDADYRKSSI (in isoform F).
                             /FTId=VSP_011411.
VAR_SEQ     473    473       E -> GALNSMGQTVVDSPSIPQAAAAVAAAANASASASVI
                             ASNNTISNTTVTTVTATATASNSSSKLPPSLGANSSISISN
                             SNSNSNSNNINNINSINNNNSSSSSTTATVAAATPTAASAA
                             AAAASSPPANSFYNNASMPALPVESNQTNNRSQSPQPRQ
                             (in isoform A, isoform E and isoform G).
                             /FTId=VSP_011410.
VAR_SEQ     520    970       Missing (in isoform F).
                             /FTId=VSP_011412.
VAR_SEQ     746    746       P -> PNGVVSSTSEIDINNVNNNQSNEPQP (in
                             isoform G).
                             /FTId=VSP_011413.
VAR_SEQ     747    761       FMLCYTQDDANAEGA -> NGVVSSTSEIDINNVNNNQSNE
                             PQP (in isoform A and isoform E).
                             /FTId=VSP_011414.
VAR_SEQ     761    761       A -> GEIIYRVELPDMEQITLIYLENNDADYP (in
                             isoform L).
                             /FTId=VSP_011415.
CONFLICT    365    365       M -> T (in Ref. 1; AAA28468 and 2;
                             AAQ01226).
CONFLICT    369    369       A -> R (in Ref. 1; AAA28468 and 2;
                             AAQ01226).
CONFLICT    395    395       E -> G (in Ref. 6; ACV53090).
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Nucleotide Sequence
Length: 3263 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 970 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
sec24BioGRID 
CG13373BioGRID 
armBioGRID 
Sh-RDBioGRID 
crbBioGRID 
sec24IntAct 
armBioGRID 
Sh-RDBioGRID 
CG30387BioGRID 
CG30387BioGRID 
CG30387BioGRID 
CG30387BioGRID 
crbBioGRID 
Dlgap1IntAct 
Dlgap2IntAct 
Dlgap3IntAct 
Dlgap4IntAct 
CG30387BioGRID 
scribBioGRID 
scribBioGRID 
scribBioGRID 
ShBioGRID 
CG9572-RBBioGRID 
Fcp3CIntAct 
CaMKIIIntAct 
eagIntAct 
ShBioGRID 
knrlBioGRID 
scribBioGRID 
MiroBioGRID 
MoeIntAct 
bazBioGRID 
gukhMINT 
CG12179IntAct 
parkIntAct 
CG30387BioGRID 
CG30387BioGRID 
Irk2IntAct 
CG17666BioGRID 
rolsIntAct 
EG:BACR37P7.5MINT 
CG9986BioGRID 
CG8301BioGRID 
CG17826BioGRID 
CG17666BioGRID 
Cpr73DBioGRID 
bazBioGRID 
CG30387BioGRID 
CG13373IntAct 
CG9572-RABioGRID 
XpacIntAct 
scribBioGRID 
scribBioGRID 
scribBioGRID 
ShBioGRID 
Fas2IntAct 
Fcp3CMINT 
ShBioGRID 
knrlMINT 
scribBioGRID 
MiroMINT 
VangIntAct 
bazBioGRID 
gukhMINT 
CG12179BioGRID 
X11LbetaIntAct 
parkBioGRID 
CG17666IntAct 
gukhIntAct 
rapsIntAct 
EG:BACR37P7.5BioGRID 
_MINT 
CG9986IntAct 
CG31345-RAIntAct 
CG8301MINT 
_MINT 
CG17826MINT 
Cpr73DMINT 
bazBioGRID 
CG30387MINT 
_MINT 
CG13373BioGRID 
CG9572-RAIntAct 
XpacBioGRID 
Other Protein-Protein interaction resources
String database  
View Microarray data
Temporarily unavailable 
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