NLGN3_RAT
ID NLGN3_RAT Reviewed; 848 AA.
AC Q62889;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Neuroligin-3;
DE AltName: Full=Gliotactin homolog;
DE Flags: Precursor;
GN Name=Nlgn3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), BLOCKAGE OF
RP N-TERMINUS, TISSUE SPECIFICITY, AND INTERACTION WITH NEUREXIN 1-BETA;
RP NEUREXIN 2-BETA AND NEUREXIN 3-BETA.
RC TISSUE=Forebrain;
RX PubMed=8576240; DOI=10.1074/jbc.271.5.2676;
RA Ichtchenko K., Nguyen T., Suedhof T.C.;
RT "Structures, alternative splicing, and neurexin binding of multiple
RT neuroligins.";
RL J. Biol. Chem. 271:2676-2682(1996).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=11329178; DOI=10.1002/glia.1050;
RA Gilbert M., Smith J., Roskams A.J., Auld V.J.;
RT "Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory
RT ensheathing glia, a growth-promoting class of macroglia.";
RL Glia 34:151-164(2001).
RN [3]
RP MUTAGENESIS OF ARG-451, SUBCELLULAR LOCATION, INTERACTION WITH NRXN1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15152050; DOI=10.1523/jneurosci.0468-04.2004;
RA Comoletti D., De Jaco A., Jennings L.L., Flynn R.E., Gaietta G.,
RA Tsigelny I., Ellisman M.H., Taylor P.;
RT "The Arg451Cys-neuroligin-3 mutation associated with autism reveals a
RT defect in protein processing.";
RL J. Neurosci. 24:4889-4893(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16982420; DOI=10.1016/j.neuron.2006.09.003;
RA Varoqueaux F., Aramuni G., Rawson R.L., Mohrmann R., Missler M.,
RA Gottmann K., Zhang W., Sudhof T.C., Brose N.;
RT "Neuroligins determine synapse maturation and function.";
RL Neuron 51:741-754(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17897391; DOI=10.1111/j.1460-9568.2007.05842.x;
RA Budreck E.C., Scheiffele P.;
RT "Neuroligin-3 is a neuronal adhesion protein at GABAergic and glutamatergic
RT synapses.";
RL Eur. J. Neurosci. 26:1738-1748(2007).
RN [6]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=18755801; DOI=10.1210/en.2008-0274;
RA Suckow A.T., Comoletti D., Waldrop M.A., Mosedale M., Egodage S.,
RA Taylor P., Chessler S.D.;
RT "Expression of neurexin, neuroligin, and their cytoplasmic binding partners
RT in the pancreatic beta-cells and the involvement of neuroligin in insulin
RT secretion.";
RL Endocrinology 149:6006-6017(2008).
RN [7]
RP INTERACTION WITH NRXN1.
RX PubMed=20624592; DOI=10.1016/j.neuron.2010.06.001;
RA Koehnke J., Katsamba P.S., Ahlsen G., Bahna F., Vendome J., Honig B.,
RA Shapiro L., Jin X.;
RT "Splice form dependence of beta-neurexin/neuroligin binding interactions.";
RL Neuron 67:61-74(2010).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19914352; DOI=10.1016/j.neuroscience.2009.11.016;
RA Levinson J.N., Li R., Kang R., Moukhles H., El-Husseini A., Bamji S.X.;
RT "Postsynaptic scaffolding molecules modulate the localization of
RT neuroligins.";
RL Neuroscience 165:782-793(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Cell surface protein involved in cell-cell-interactions via
CC its interactions with neurexin family members. Plays a role in synapse
CC function and synaptic signal transmission, and probably mediates its
CC effects by recruiting and clustering other synaptic proteins. May
CC promote the initial formation of synapses, but is not essential for
CC this. May also play a role in glia-glia or glia-neuron interactions in
CC the developing peripheral nervous system.
CC {ECO:0000269|PubMed:17897391}.
CC -!- SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-
CC terminus) with DLG4/PSD-95 (via PDZ domain 3) (By similarity).
CC Homodimer, and heterodimer with NLGN1 and NLGN2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Synapse. Note=Detected at both glutamatergic and GABAergic
CC synapses.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q62889-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62889-2; Sequence=VSP_007535, VSP_007536;
CC Name=3;
CC IsoId=Q62889-3; Sequence=VSP_007536;
CC Name=4;
CC IsoId=Q62889-4; Sequence=VSP_007535;
CC -!- TISSUE SPECIFICITY: Detected in brain and on hippocampus neurons,
CC especially at excitatory synapses. Detected in retina (at protein
CC level). Expressed in brain, spinal cord and dorsal root ganglion.
CC {ECO:0000269|PubMed:11329178, ECO:0000269|PubMed:16982420,
CC ECO:0000269|PubMed:17897391, ECO:0000269|PubMed:18755801,
CC ECO:0000269|PubMed:19914352, ECO:0000269|PubMed:8576240}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U41663; AAA97871.1; -; mRNA.
DR RefSeq; NP_599163.2; NM_134336.2.
DR AlphaFoldDB; Q62889; -.
DR SMR; Q62889; -.
DR BioGRID; 251173; 2.
DR IntAct; Q62889; 1.
DR MINT; Q62889; -.
DR STRING; 10116.ENSRNOP00000005077; -.
DR ESTHER; ratno-3neur; Neuroligin.
DR MEROPS; S09.987; -.
DR GlyGen; Q62889; 2 sites.
DR iPTMnet; Q62889; -.
DR PhosphoSitePlus; Q62889; -.
DR PaxDb; Q62889; -.
DR PRIDE; Q62889; -.
DR ABCD; Q62889; 1 sequenced antibody.
DR GeneID; 171297; -.
DR KEGG; rno:171297; -.
DR UCSC; RGD:621119; rat. [Q62889-1]
DR CTD; 54413; -.
DR RGD; 621119; Nlgn3.
DR eggNOG; KOG1516; Eukaryota.
DR InParanoid; Q62889; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q62889; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR PRO; PR:Q62889; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030139; C:endocytic vesicle; IDA:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0042043; F:neurexin family protein binding; IPI:BHF-UCL.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0048675; P:axon extension; IMP:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0042745; P:circadian sleep/wake cycle; IMP:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; IDA:BHF-UCL.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:BHF-UCL.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; ISO:RGD.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; ISS:BHF-UCL.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; IDA:RGD.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; IMP:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; ISO:RGD.
DR GO; GO:0097104; P:postsynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0098698; P:postsynaptic specialization assembly; IDA:SynGO.
DR GO; GO:0060134; P:prepulse inhibition; IMP:RGD.
DR GO; GO:0097105; P:presynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:BHF-UCL.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:BHF-UCL.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISS:BHF-UCL.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:BHF-UCL.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; ISS:BHF-UCL.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR GO; GO:2000331; P:regulation of terminal button organization; ISS:BHF-UCL.
DR GO; GO:0060024; P:rhythmic synaptic transmission; IMP:BHF-UCL.
DR GO; GO:0035176; P:social behavior; ISS:BHF-UCL.
DR GO; GO:0007416; P:synapse assembly; IDA:BHF-UCL.
DR GO; GO:0050808; P:synapse organization; IDA:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR GO; GO:0071625; P:vocalization behavior; ISO:RGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000460; Nlgn.
DR InterPro; IPR030024; NLGN3.
DR PANTHER; PTHR43903:SF4; PTHR43903:SF4; 1.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR01090; NEUROLIGIN.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..848
FT /note="Neuroligin-3"
FT /id="PRO_0000008647"
FT TOPO_DOM 38..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..848
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 169..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 792
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYM5"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..141
FT /evidence="ECO:0000250"
FT DISULFID 340..351
FT /evidence="ECO:0000250"
FT DISULFID 510..544
FT /evidence="ECO:0000250"
FT VAR_SEQ 153..172
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8576240"
FT /id="VSP_007535"
FT VAR_SEQ 173..192
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:8576240"
FT /id="VSP_007536"
FT MUTAGEN 451
FT /note="R->C: Impaired cell surface expression, and reduced
FT interaction with NRXN1."
FT /evidence="ECO:0000269|PubMed:15152050"
SQ SEQUENCE 848 AA; 93888 MW; 7520653B3253E750 CRC64;
MWLQLGLPSL SLSPTPTVGR SLCLILWFLS LVLRASTQAP APTVNTHFGK LRGARVPLPS
EILGPVDQYL GVPYAAPPIG EKRFLPPEPP PSWSGIRNAT HFPPVCPQNI HTAVPEVMLP
VWFTANLDIV ATYIQEPNED CLYLNVYVPT EDVKRISKEC ARKPNKKICR KGGSGAKKQG
EDLADNDGDE DEDIRDSGAK PVMVYIHGGS YMEGTGNMID GSVLASYGNV IVITLNYRVG
VLGFLSTGDQ AAKGNYGLLD QIQALRWVSE NIAFFGGDPR RITVFGSGIG ASCVSLLTLS
HHSEGLFQRA IIQSGSALSS WAVNYQPVKY TSLLADKVGC NVLDTVDMVD CLRQKSAKEL
VEQDIQPARY HVAFGPVIDG DVIPDDPEIL MEQGEFLNYD IMLGVNQGEG LKFVEGVVDP
EDGVSGTDFD YSVSNFVDNL YGYPEGKDTL RETIKFMYTD WADRDNPETR RKTLVALFTD
HQWVEPSVVT ADLHARYGSP TYFYAFYHHC QSLMKPAWSD AAHGDEVPYV FGVPMVGPTD
LFPCNFSKND VMLSAVVMTY WTNFAKTGDP NKPVPQDTKF IHTKANRFEE VAWSKYNPRD
QLYLHIGLKP RVRDHYRATK VAFWKHLVPH LYNLHDMFHY TSTTTKVPPP DTTHSSHITR
RPNGKTWSTK RPAISPAYSN ENAPGSWNGD QDAGPLLVEN PRDYSTELSV TIAVGASLLF
LNVLAFAALY YRKDKRRQEP LRQPSPQRGT GAPELGTAPE EELAALQLGP THHECEAGPP
HDTLRLTALP DYTLTLRRSP DDIPLMTPNT ITMIPNSLVG LQTLHPYNTF AAGFNSTGLP
NSHSTTRV
