DLG4_DANRE
ID DLG4_DANRE Reviewed; 801 AA.
AC Q6R005;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Disks large homolog 4;
DE AltName: Full=Postsynaptic density protein 95;
DE Short=PSD-95;
GN Name=dlg4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Retina;
RX PubMed=14758365; DOI=10.1038/nn1191;
RA Niell C.M., Meyer M.P., Smith S.J.;
RT "In vivo imaging of synapse formation on a growing dendritic arbor.";
RL Nat. Neurosci. 7:254-260(2004).
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15660367; DOI=10.1002/neu.20118;
RA Meyer M.P., Trimmer J.S., Gilthorpe J.D., Smith S.J.;
RT "Characterization of zebrafish PSD-95 gene family members.";
RL J. Neurobiol. 63:91-105(2005).
CC -!- FUNCTION: Postsynaptic scaffolding protein that plays a critical role
CC in synaptogenesis and synaptic plasticity by providing a platform for
CC the postsynaptic clustering of crucial synaptic proteins.
CC {ECO:0000269|PubMed:15660367}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14758365};
CC Peripheral membrane protein {ECO:0000269|PubMed:14758365}. Postsynaptic
CC density {ECO:0000269|PubMed:14758365}. Synapse
CC {ECO:0000269|PubMed:14758365}. Note=High levels in postsynaptic density
CC of neuronal cells.
CC -!- DEVELOPMENTAL STAGE: At 3 days-post-fertilization (dpf), expressed
CC strongly in neurons in the ventral hindbrain and tegmentum and
CC diffusely in the dorsal hindbrain and optic tectum. Also expressed in
CC the diencephalon and the prospective olfactory bulb. Expression in non-
CC spiny type-XIV tectal neurons is mostly diffuse. Over the next 7 days,
CC as the dendritic arbor develops, expression becomes progressively more
CC punctate, becoming localized to sites of synapse formation. At 4 dpf,
CC expressed in the inner and outer plexiform layers of the retina and in
CC the optic chiasm. {ECO:0000269|PubMed:14758365,
CC ECO:0000269|PubMed:15660367}.
CC -!- DOMAIN: L27 domain is required for targeting to postsynaptic density.
CC {ECO:0000250|UniProtKB:P31016}.
CC -!- PTM: Ubiquitinated by MDM2 in response to NMDA receptor activation,
CC leading to proteasome-mediated degradation of DLG4 which is required
CC for AMPA receptor endocytosis. {ECO:0000250|UniProtKB:P31016}.
CC -!- PTM: Palmitoylated. Palmitoylation is required for targeting to
CC postsynaptic density, plasma membrane and synapses.
CC {ECO:0000250|UniProtKB:P31016}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AY520570; AAS00608.1; -; mRNA.
DR RefSeq; NP_999893.1; NM_214728.1.
DR AlphaFoldDB; Q6R005; -.
DR SMR; Q6R005; -.
DR STRING; 7955.ENSDARP00000042429; -.
DR PaxDb; Q6R005; -.
DR ABCD; Q6R005; 1 sequenced antibody.
DR GeneID; 405796; -.
DR KEGG; dre:405796; -.
DR CTD; 405796; -.
DR ZFIN; ZDB-GENE-040628-3; dlg4b.
DR eggNOG; KOG0708; Eukaryota.
DR InParanoid; Q6R005; -.
DR OrthoDB; 807583at2759; -.
DR PhylomeDB; Q6R005; -.
DR PRO; PR:Q6R005; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ZFIN.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0098970; P:postsynaptic neurotransmitter receptor diffusion trapping; 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:0050808; P:synapse organization; NAS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016313; DLG1-like.
DR InterPro; IPR019590; DLG1_PEST_dom.
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; IPR019583; PDZ_assoc.
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; PF10608; MAGUK_N_PEST; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF10600; PDZ_assoc; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM01277; MAGUK_N_PEST; 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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Repeat; SH3 domain; Synapse;
KW Ubl conjugation.
FT CHAIN 1..801
FT /note="Disks large homolog 4"
FT /id="PRO_0000094563"
FT DOMAIN 4..60
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 153..240
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 248..335
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 393..474
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 507..577
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 610..786
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 339..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 89140 MW; F8BF0E103904C668 CRC64;
MPLKREDTER ALQAMEACQS AGDEGFRTRA ERLLTIFQSD LFQALLDIQE FYELTVFENQ
TAGRALTPGL KYRYHDEETP PLQHSPAHLS TGKSAEMLHL GDSGHAPIDG IHAYTPQMHV
SPAKPVLLPS GHAPYYATST LMNGMDGDVE YEEITLERGN SGLGFSIAGG TDNPHIGDDP
SIFITKIIPG GAAAQDGRLR VNDSILFVND VDVREVTHSF AVEALKEAGP IVRLYVLRHK
PSAEKITELK LIKGPKGLGF SIAGGVGNQH VPGDNSIYVT KIIEGGAAHK DGRLQIGDKI
LAVNNMYLEE VMHEDAVAAL KNTGDVVFLR VAKTLHQHHH QDAYNPPDIT SSYSPHMDMS
DYPQALSPSS PRRYSPIPKG LFLDDDISRE PRRVVIHRGS TGLGFNIVGG EDGEGIFISF
ILAGGAADLS GELRKGDQIL SVNGVDLRHA THEQAAAALK NAGQTVTIIT QYRPEEYSRF
EAKIHDLREQ LMNSSLVSAA ASLRSGKRSF FIRALFDYDK TADGGFLSQA VSFRFGDVLQ
VFDCSDEEWW QAGKLAPHGE LEETGYIPSK RRVERKEWSR LKTRGREPVS GRSDYIVSYE
TVTQSEVHYA RPVIILGPSK DRVNDDLLSE FPDKFGSCVP HTTRPKREYE MDGRDYHFVS
SREQMEKDIQ SHRFIEAGQY NSHLYGTSVQ SVRQVAEQQG KHCILDVSAN AVRRLQAAQL
YPIAIFIRPS SLQNVLNISK RLTEEQARRA LDRAVKLEQD FIECFSAIVE GESFEEIYHH
VKSVIEEQSG PYIWIPARER L
