DLGP3_HUMAN
ID DLGP3_HUMAN Reviewed; 979 AA.
AC O95886; Q5TDD5; Q9H3X7;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Disks large-associated protein 3;
DE Short=DAP-3;
DE AltName: Full=PSD-95/SAP90-binding protein 3;
DE AltName: Full=SAP90/PSD-95-associated protein 3;
DE Short=SAPAP3;
GN Name=DLGAP3; Synonyms=DAP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 655-979.
RC TISSUE=Brain;
RA Mei G., Yu W., Gibbs R.A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP VARIANT PRO-763.
RX PubMed=28294470; DOI=10.1111/cas.13233;
RA Tode N., Kikuchi T., Sakakibara T., Hirano T., Inoue A., Ohkouchi S.,
RA Tamada T., Okazaki T., Koarai A., Sugiura H., Niihori T., Aoki Y.,
RA Nakayama K., Matsumoto K., Matsubara Y., Yamamoto M., Watanabe A.,
RA Nukiwa T., Ichinose M.;
RT "Exome sequencing deciphers a germline MET mutation in familial epidermal
RT growth factor receptor-mutant lung cancer.";
RL Cancer Sci. 108:1263-1270(2017).
CC -!- FUNCTION: May play a role in the molecular organization of synapses and
CC neuronal cell signaling. Could be an adapter protein linking ion
CC channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-
CC 95/SAP90 at the plasma membrane.
CC -!- SUBUNIT: Interacts with DLG4/PSD-95. {ECO:0000250}.
CC -!- INTERACTION:
CC O95886; Q15700: DLG2; NbExp=3; IntAct=EBI-1752541, EBI-80426;
CC O95886; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1752541, EBI-618309;
CC O95886; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-1752541, EBI-2556193;
CC O95886; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1752541, EBI-11749135;
CC O95886; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-1752541, EBI-11958178;
CC O95886; P43360: MAGEA6; NbExp=3; IntAct=EBI-1752541, EBI-1045155;
CC O95886; Q86UL8-2: MAGI2; NbExp=3; IntAct=EBI-1752541, EBI-12081182;
CC O95886; P16333: NCK1; NbExp=2; IntAct=EBI-1752541, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse
CC {ECO:0000250}. Note=Postsynaptic density of neuronal cells.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20042.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC114490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL122010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF131778; AAD20042.1; ALT_FRAME; mRNA.
DR CCDS; CCDS30670.1; -.
DR RefSeq; NP_001073887.1; NM_001080418.2.
DR RefSeq; XP_011540181.1; XM_011541879.2.
DR AlphaFoldDB; O95886; -.
DR SMR; O95886; -.
DR BioGRID; 121839; 20.
DR IntAct; O95886; 22.
DR MINT; O95886; -.
DR STRING; 9606.ENSP00000362444; -.
DR iPTMnet; O95886; -.
DR PhosphoSitePlus; O95886; -.
DR SwissPalm; O95886; -.
DR BioMuta; DLGAP3; -.
DR MassIVE; O95886; -.
DR PaxDb; O95886; -.
DR PeptideAtlas; O95886; -.
DR PRIDE; O95886; -.
DR ProteomicsDB; 51118; -.
DR Antibodypedia; 17231; 129 antibodies from 28 providers.
DR DNASU; 58512; -.
DR Ensembl; ENST00000235180.4; ENSP00000235180.4; ENSG00000116544.12.
DR Ensembl; ENST00000373347.6; ENSP00000362444.1; ENSG00000116544.12.
DR GeneID; 58512; -.
DR KEGG; hsa:58512; -.
DR MANE-Select; ENST00000373347.6; ENSP00000362444.1; NM_001080418.3; NP_001073887.1.
DR UCSC; uc001byc.3; human.
DR CTD; 58512; -.
DR DisGeNET; 58512; -.
DR GeneCards; DLGAP3; -.
DR HGNC; HGNC:30368; DLGAP3.
DR HPA; ENSG00000116544; Tissue enriched (brain).
DR MIM; 611413; gene.
DR neXtProt; NX_O95886; -.
DR OpenTargets; ENSG00000116544; -.
DR PharmGKB; PA134923893; -.
DR VEuPathDB; HostDB:ENSG00000116544; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT00940000159513; -.
DR HOGENOM; CLU_010880_0_0_1; -.
DR InParanoid; O95886; -.
DR OMA; EDYQLQY; -.
DR OrthoDB; 197925at2759; -.
DR PhylomeDB; O95886; -.
DR TreeFam; TF321382; -.
DR PathwayCommons; O95886; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; O95886; -.
DR SIGNOR; O95886; -.
DR BioGRID-ORCS; 58512; 16 hits in 1070 CRISPR screens.
DR GenomeRNAi; 58512; -.
DR Pharos; O95886; Tbio.
DR PRO; PR:O95886; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95886; protein.
DR Bgee; ENSG00000116544; Expressed in right frontal lobe and 103 other tissues.
DR Genevisible; O95886; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0099563; P:modification of synaptic structure; IEA:Ensembl.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; IEA:InterPro.
DR InterPro; IPR030526; DLGAP3.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR PANTHER; PTHR12353:SF4; PTHR12353:SF4; 1.
DR Pfam; PF03359; GKAP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..979
FT /note="Disks large-associated protein 3"
FT /id="PRO_0000174294"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..247
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..765
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97838"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97838"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT VARIANT 763
FT /note="T -> P (in dbSNP:rs758215471)"
FT /evidence="ECO:0000269|PubMed:28294470"
FT /id="VAR_079371"
SQ SEQUENCE 979 AA; 106040 MW; 34A010D792CFFB9D CRC64;
MRGYHGDRGS HPRPARFADQ QHMDVGPAAR APYLLGSREA FSTEPRFCAP RAGLGHISPE
GPLSLSEGPS VGPEGGPAGA GVGGGSSTFP RMYPGQGPFD TCEDCVGHPQ GKGAPRLPPT
LLDQFEKQLP VQQDGFHTLP YQRGPAGAGP GPAPGTGTAP EPRSESPSRI RHLVHSVQKL
FAKSHSLEAP GKRDYNGPKA EGRGGSGGDS YPGPGSGGPH TSHHHHHHHH HHHHQSRHGK
RSKSKDRKGD GRHQAKSTGW WSSDDNLDSD SGFLAGGRPP GEPGGPFCLE GPDGSYRDLS
FKGRSGGSEG RCLACTGMSM SLDGQSVKRS AWHTMMVSQG RDGYPGAGPG KGLLGPETKA
KARTYHYLQV PQDDWGGYPT GGKDGEIPCR RMRSGSYIKA MGDEESGDSD GSPKTSPKAV
ARRFTTRRSS SVDQARINCC VPPRIHPRSS IPGYSRSLTT GQLSDELNQQ LEAVCGSVFG
ELESQAVDAL DLPGCFRMRS HSYLRAIQAG CSQDDDCLPL LATPAAVSGR PGSSFNFRKA
PPPIPPGSQA PPRISITAQS STDSAHESFT AAEGPARRCS SADGLDGPAM GARTLELAPV
PPRASPKPPT LIIKTIPGRE ELRSLARQRK WRPSIGVQVE TISDSDTENR SRREFHSIGV
QVEEDKRRAR FKRSNSVTAG VQADLELEGL AGLATVATED KALQFGRSFQ RHASEPQPGP
RAPTYSVFRT VHTQGQWAYR EGYPLPYEPP ATDGSPGPAP APTPGPGAGR RDSWIERGSR
SLPDSGRASP CPRDGEWFIK MLRAEVEKLE HWCQQMEREA EDYELPEEIL EKIRSAVGST
QLLLSQKVQQ FFRLCQQSMD PTAFPVPTFQ DLAGFWDLLQ LSIEDVTLKF LELQQLKANS
WKLLEPKEEK KVPPPIPKKP LRGRGVPVKE RSLDSVDRQR QEARKRLLAA KRAASFRHSS
ATESADSIEI YIPEAQTRL
