DLG1_DANRE
ID DLG1_DANRE Reviewed; 873 AA.
AC Q5PYH6; Q7ZUM2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Disks large homolog 1;
DE AltName: Full=Synapse-associated protein 97A;
DE Short=SAP-97A;
DE Short=SAP97A;
GN Name=dlg1;
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] (ISOFORM 2), 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential multidomain scaffolding protein required for normal
CC development. Recruits channels, receptors and signaling molecules to
CC discrete plasma membrane domains in polarized cells. May play a role in
CC adherens junction assembly, signal transduction and cell proliferation
CC (By similarity). May play a role in synapse assembly and function.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q12959};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q12959}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q62696}. Cell junction
CC {ECO:0000250|UniProtKB:Q12959}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q12959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q5PYH6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5PYH6-2; Sequence=VSP_014168, VSP_014169, VSP_014170,
CC VSP_014171;
CC -!- DEVELOPMENTAL STAGE: At 4 days-post-fertilization (dpf), expressed in
CC the inner and outer plexiform layers and the ganglion cell layer of the
CC retina, the marginal zone of the tegmentum, and in the developing
CC craniofacial cartilage. {ECO:0000269|PubMed:15660367}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AY819034; AAV68499.1; -; mRNA.
DR EMBL; BC048066; AAH48066.1; -; mRNA.
DR RefSeq; NP_955820.1; NM_199526.1. [Q5PYH6-1]
DR AlphaFoldDB; Q5PYH6; -.
DR SMR; Q5PYH6; -.
DR STRING; 7955.ENSDARP00000036537; -.
DR PRIDE; Q5PYH6; -.
DR ABCD; Q5PYH6; 1 sequenced antibody.
DR GeneID; 114446; -.
DR KEGG; dre:114446; -.
DR CTD; 114446; -.
DR ZFIN; ZDB-GENE-010724-8; dlg1a.
DR eggNOG; KOG0708; Eukaryota.
DR InParanoid; Q5PYH6; -.
DR OMA; RNAFSEC; -.
DR OrthoDB; 807583at2759; -.
DR PhylomeDB; Q5PYH6; -.
DR PRO; PR:Q5PYH6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase 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: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 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 PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM01277; MAGUK_N_PEST; 1.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF101288; SSF101288; 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.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell junction; Cell membrane; Endoplasmic reticulum;
KW Membrane; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..873
FT /note="Disks large homolog 1"
FT /id="PRO_0000094551"
FT DOMAIN 4..64
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 230..317
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 325..412
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 474..555
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 683..858
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 62..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15660367"
FT /id="VSP_014168"
FT VAR_SEQ 101..109
FT /note="PINLPQTEE -> MEDSDQGFN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15660367"
FT /id="VSP_014169"
FT VAR_SEQ 166..200
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15660367"
FT /id="VSP_014170"
FT VAR_SEQ 605..663
FT /note="TVKFNSKSRDKASLNDKRRKTLFSRKFLFSKNKDSGEQDTSDVDQHVTSNAS
FT DSESSFR -> DSGLPSQGLNFRFGDILHVLNASDEEWWQARHVTTDGEMEEMGVIPSK
FT KRVERKERARLKTVKFNSKSRDKADLSDDKGLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15660367"
FT /id="VSP_014171"
SQ SEQUENCE 873 AA; 96981 MW; F7DC1F3FE5E1B04F CRC64;
MPVRQKDAQR ALQLLEEYQT KLSQTGDPHL RLSIERVINI FKSTLFQALV DIQEYYEVSL
QDTEDKPIED SSLKSRESFP PVNEWNLSVP PSTTGPTEPV PINLPQTEEK YRYQDEDTTS
PPEHSSPHIP GDARPPELVQ VSEKNISQIE NVHGYVSHSH ISPMKQADVI PPPSAPIIPV
IPISPVPAET TAIIPAPASQ ASPAPVVVNT ESLDSSPYVN GTEADYEYEE ITLERGNSGL
GFSIAGGTDN PHIGEDPSIF ITKIIPGGAA AQDGRLRVND CILRVNDVDV RDVTHSNAVE
ALKEAGCIVR LYVRRRKPLS EKIMDVKLVK GPKGLGFSIA GGVGNQHIPG DNSIYITKII
EGGAAHKDGR LQIGDKLLAV NAVCLEEVTH EDAVAALKNT PDVVYLKVAK PTSVFMNDSY
APPDVTSSYS QHMENHISTQ SYLSQPLTPA TPSRYSPVSK GMLGDDEITR EPRKIVLHRG
TTGLGFNIVG GEDGEGIFIS FILAGGPADL CGELRKGDRI VSVNGVDLRS ATHEQAAAAL
KNAGQTVTII AQYRPEEYSR FEAKIHDLRE QMMNSSISSG SGSLRTSQKR TLYVRALFDY
DITKTVKFNS KSRDKASLND KRRKTLFSRK FLFSKNKDSG EQDTSDVDQH VTSNASDSES
SFRGQEDYVL SYETVTQQEV SYSRPVIILG PMKDRINDDL ISEFPDKFGS CVPHTTRPKR
DYEVDGRDYH FVNSREQMEK DIQDHKFIEA GQYNNHLYGT SVQSVREVAE KGKHCILDVS
GNAIKRLQLA QLYPIAVFIK PKSVENILEM NKRLMEEQGR KTYDRAMKLE QEFLEHFTAI
VQGDTLEEIY NQVKQIIEEQ SGPFIWVPVK EKL
