ID DLG1L_DANRE Reviewed; 827 AA.
AC Q5PYH5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Discs large homolog 1-like protein;
DE AltName: Full=Synapse-associated protein 97B;
DE Short=SAP-97B;
DE Short=SAP97B;
GN Name=dlg1l;
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], 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: May play a role in synapse assembly and function.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: At 4 days-post-fertilization (dpf), expressed in
CC the inner and outer plexiform layers of the retina, the marginal zone
CC of the tegmentum, the developing craniofacial cartilage and in the
CC ventral spinal cord. {ECO:0000269|PubMed:15660367}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AY819035; AAV68500.1; -; mRNA.
DR RefSeq; NP_001012388.1; NM_001012388.1.
DR AlphaFoldDB; Q5PYH5; -.
DR SMR; Q5PYH5; -.
DR STRING; 7955.ENSDARP00000132280; -.
DR PaxDb; 7955-ENSDARP00000061428; -.
DR GeneID; 497648; -.
DR KEGG; dre:497648; -.
DR AGR; ZFIN:ZDB-GENE-050222-3; -.
DR CTD; 497648; -.
DR ZFIN; ZDB-GENE-050222-3; dlg1b.
DR eggNOG; KOG0708; Eukaryota.
DR HOGENOM; CLU_001715_4_2_1; -.
DR InParanoid; Q5PYH5; -.
DR OrthoDB; 2879721at2759; -.
DR PhylomeDB; Q5PYH5; -.
DR TreeFam; TF323171; -.
DR Reactome; R-DRE-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-DRE-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DRE-8849932; Synaptic adhesion-like molecules.
DR PRO; PR:Q5PYH5; -.
DR Proteomes; UP000000437; Chromosome 2.
DR Bgee; ENSDARG00000102216; Expressed in muscle tissue and 28 other cell types or tissues.
DR ExpressionAtlas; Q5PYH5; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0001935; P:endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IBA:GO_Central.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; NAS:UniProtKB.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 3.
DR CDD; cd12031; SH3_DLG1; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR019583; DLG1-4_PDZ_assoc.
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; 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 PANTHER; PTHR23119; DISCS LARGE; 1.
DR PANTHER; PTHR23119:SF5; DISKS LARGE HOMOLOG 1; 1.
DR Pfam; PF00625; Guanylate_kin; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..827
FT /note="Discs large homolog 1-like protein"
FT /id="PRO_0000094552"
FT DOMAIN 159..246
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 254..341
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 403..484
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 518..588
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 637..812
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 38..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 91496 MW; B5219DA9E4541AC9 CRC64;
MSPSIKKLDC FSPMLCHCKV ACTNSTISLM FGCKKYRHQD EDTGSPQEPS SPQFTDDTPG
PELVQVAEKS LSQIENVHGF VAHSHISPMK VESLECIFDG PSPVVKEESP PSPSTPLSNP
YPQSPVSVQA NPPPVVVNTE SLDSAPYVNG TEADFEYEEI TLERGNSGLG FSIAGGTDNP
HIGEDPSIFI TKVIPGGAAA QDGRLRVNDV ILRVNEVDVR DVTHSKAVEA LKEAGSLVRL
YVRRRKSASE KVMEIKLIKG PKGLGFSIAG GVGNQHIPGD NSIYVTKIIE GGAAHKDGRL
QIGDKLLAVN SSCLEEVTHE HAVTALKNTP DVVYLKVAKP NSVFMNDSFA PPDITNSYSQ
HMENHISPPS YLSQPLPPVH SGRFSPTPKT TVGDDDVTRE PRKVVLHRGT TGLGFNIVGG
EDGEGIFISF ILAGGPADLC GELRKGDRLV SVNGIDLRGA THEQAAAALK NAGQTVTIVA
QYRPEEYSRF EAKIHDLREQ MMNSSISSGS GSLRTSQKRS LYVRALFDYD KTKDSGLPSQ
GLNFKFGDIL HVVNASDDEW WQARQVTAQG EVEEMGVIPS KRRVEKKERA RLKTVKFNSK
SREKGDNPDD MLSKGQSGQE EYVLSYEPVS QQEVNYSRPV IILGPMKDRV NDDLISEFPD
KFGSCVPHTT RPKRDYEVDG RDYHFVVSRE QMERDIQEHK FIEAGQYNSH LYGTSVQSVR
EVAEKGKHCI LDVSGNAIKR LQVAMLYPIG IFIKPKSVEN IMEMNKRLTE EQGRKTYDRA
MKLEQEFMEH FTAIVQGDTL EEIYDQVKQI IEEQSGPYIW VQSKEKL
//
