NLGN1_CAEEL
ID NLGN1_CAEEL Reviewed; 798 AA.
AC Q9XTG1; Q8I0R2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Neuroligin-1;
DE Flags: Precursor;
GN Name=nlg-1; ORFNames=C40C9.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-315, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-315, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [4]
RP FUNCTION, INTERACTION WITH MADD-4 AND UNC-49, SUBCELLULAR LOCATION, DOMAIN,
RP AND MUTAGENESIS OF 786-THR--VAL-798.
RX PubMed=26028575; DOI=10.1016/j.neuron.2015.05.013;
RA Tu H., Pinan-Lucarre B., Ji T., Jospin M., Bessereau J.L.;
RT "C. elegans Punctin Clusters GABA(A) Receptors via Neuroligin Binding and
RT UNC-40/DCC Recruitment.";
RL Neuron 86:1407-1419(2015).
RN [5]
RP FUNCTION, INTERACTION WITH MADD-4, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF 796-ILE--VAL-798.
RX PubMed=26028574; DOI=10.1016/j.neuron.2015.05.015;
RA Maro G.S., Gao S., Olechwier A.M., Hung W.L., Liu M., Oezkan E., Zhen M.,
RA Shen K.;
RT "MADD-4/Punctin and Neurexin Organize C. elegans GABAergic Postsynapses
RT through Neuroligin.";
RL Neuron 86:1420-1432(2015).
CC -!- FUNCTION: Probable neuronal cell surface protein thought to be involved
CC in cell-cell-interactions by forming intercellular junctions through
CC binding to beta-neurexins (By similarity). Plays a role in the
CC clustering of the GABA(A) receptor unc-49 at postsynaptic sites in
CC neuromuscular junctions (NMJs) via the interaction with madd-4 and
CC neurexin nrx-1 and is thereby required for normal GABAergic synaptic
CC transmission (PubMed:26028574, PubMed:26028575).
CC {ECO:0000250|UniProtKB:Q99K10, ECO:0000269|PubMed:26028574,
CC ECO:0000269|PubMed:26028575}.
CC -!- SUBUNIT: Interacts (via extracellular domain) with isoform b of madd-4;
CC the interaction is required for the localization to postsynaptic
CC domains (PubMed:26028575, PubMed:26028574). Interacts with unc-49
CC (PubMed:26028575). {ECO:0000269|PubMed:26028574,
CC ECO:0000269|PubMed:26028575}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Synapse {ECO:0000269|PubMed:26028574,
CC ECO:0000269|PubMed:26028575}. Note=Localizes specifically to GABAergic
CC synapses. {ECO:0000269|PubMed:26028574, ECO:0000269|PubMed:26028575}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q9XTG1-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9XTG1-2; Sequence=VSP_020296;
CC -!- DOMAIN: The cytoplasmic region is required for GABA(A) receptor
CC clustering. {ECO:0000269|PubMed:26028574, ECO:0000269|PubMed:26028575}.
CC -!- DOMAIN: The extracellular region is required for the localization to
CC synapses and for GABA(A) receptor clustering.
CC {ECO:0000269|PubMed:26028574, ECO:0000269|PubMed:26028575}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; Z70266; CAD57691.1; -; Genomic_DNA.
DR EMBL; AL023827; CAD57691.1; JOINED; Genomic_DNA.
DR EMBL; Z70266; CAA94208.1; -; Genomic_DNA.
DR EMBL; AL023827; CAA94208.1; JOINED; Genomic_DNA.
DR PIR; T19864; T19864.
DR RefSeq; NP_510283.1; NM_077882.3. [Q9XTG1-1]
DR RefSeq; NP_872254.1; NM_182454.3. [Q9XTG1-2]
DR AlphaFoldDB; Q9XTG1; -.
DR SMR; Q9XTG1; -.
DR BioGRID; 46385; 4.
DR DIP; DIP-26014N; -.
DR STRING; 6239.C40C9.5e; -.
DR ESTHER; caeel-NLGN1; Neuroligin.
DR TCDB; 8.A.117.1.5; the neuroligin (nlg) family.
DR iPTMnet; Q9XTG1; -.
DR PRIDE; Q9XTG1; -.
DR EnsemblMetazoa; C40C9.5a.1; C40C9.5a.1; WBGene00006412. [Q9XTG1-1]
DR EnsemblMetazoa; C40C9.5b.1; C40C9.5b.1; WBGene00006412. [Q9XTG1-2]
DR GeneID; 181484; -.
DR UCSC; C40C9.5a; c. elegans. [Q9XTG1-1]
DR CTD; 181484; -.
DR WormBase; C40C9.5a; CE18546; WBGene00006412; nlg-1. [Q9XTG1-1]
DR WormBase; C40C9.5b; CE32604; WBGene00006412; nlg-1. [Q9XTG1-2]
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000169220; -.
DR InParanoid; Q9XTG1; -.
DR PhylomeDB; Q9XTG1; -.
DR Reactome; R-CEL-192456; Digestion of dietary lipid.
DR Reactome; R-CEL-6794361; Neurexins and neuroligins.
DR PRO; PR:Q9XTG1; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006412; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q9XTG1; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:WormBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0042043; F:neurexin family protein binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IMP:CACAO.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IBA:GO_Central.
DR GO; GO:0097105; P:presynaptic membrane assembly; IBA:GO_Central.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Reference proteome; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..798
FT /note="Neuroligin-1"
FT /id="PRO_0000248519"
FT TOPO_DOM 18..685
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 636..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..657
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT DISULFID 86..125
FT /evidence="ECO:0000250"
FT DISULFID 288..307
FT /evidence="ECO:0000250"
FT VAR_SEQ 782..784
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020296"
FT MUTAGEN 786..798
FT /note="Missing: Disruption of GABA(A) receptor clustering."
FT /evidence="ECO:0000269|PubMed:26028575"
FT MUTAGEN 796..798
FT /note="Missing: Disruption of GABA(A) receptor clustering."
FT /evidence="ECO:0000269|PubMed:26028574"
SQ SEQUENCE 798 AA; 89018 MW; 5EFE50035AD4E349 CRC64;
MERIYLLLLL FLPRIRSYDV RSVTTSWGMV RGEVVSPEGD DLPPVAQYLG IPYGVAPTGQ
YRFNMAISAA KWTHMPKDAR KVSPVCIQTD MPELSETKAF KHTSAQRFDF NHRLLPHLKK
QSEDCLYMNI YVPERLEISR DNYLPVMVIV HGEEYGWGTG NAFNGTTLAA YGHIIVVTLN
YRLGVFGFLG RCESSSCSGN SGISDLVSAL TMLNVILPSF GGDSKSVTLA GWGSGASLVS
LLMASPLTQP GRRLFRRAIL LDGSALSPWA ISQNPQQYFM QLAEELACAP KNRTSSFNDN
VDTIVRCMQV HSSENITKAV LKIDVPTFLS GFAPIVDGQL IPNKPQVSFS TQYGSLFREI
DLLVGISSNP SHHMISNEDL KVGISKEKRM RIFRSLVRNL YDFHREEILA SIINEYTDWE
NPRDHPKSIR NGVLNALSDV LYTAPLIETL RSHSADEVRK EANTFMFAFA HETRSWSQEQ
PNSGIRGSLS GDIVPYIFGY PLAQGDSEER LYSGFNTDDK GISKVMMHYV SNFVKSGDPS
KPNPMSKNFP MGDVFHSTAW PQFDQPNREA YLEITDRPRV KNYYRNAQVG FWNNFIPQLH
KNGKETEPVG EEHHLLSDHF RKDSYFGKTR HFSSYANLPF PPPPMPPSPP PELTTKPKPS
ESPTTLQTTT ESEKAAAGSF TGKALGGVIF IGCGFLIMNV CLLIAVRREW GKKRRNEKKF
QLQYQTYNSN HGGGAEQYNS LNSPEPLLSA SHKNSTSMRP AGISPTCPRH GRAALALQNS
RGNSLTAAQA PTLEEIQV
