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Q99K10 (NLGN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuroligin-1
Gene names
Name:Nlgn1
Synonyms:Kiaa1070
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Ref.3 Ref.5 Ref.6

Subunit structure

Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with AIP1, GOPC and PDZRN3 By similarity. Interacts with NLGN3. Ref.7

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Cell junctionsynapse By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Note: Enriched in synaptic plasma membranes and clustered in synaptic clefts and postsynaptic densities. Detected at dendritic spines. Colocalized with DLG4/PSD-95 and GRIN1/NMDAR1 By similarity. Ref.5

Tissue specificity

Brain and arteries (at protein level). Expressed in olfactory bulb. Detected in brain. Ref.4 Ref.6 Ref.8 Ref.9

Disruption phenotype

No obvious phenotype, but mice present subtle behavorial changes with some deficits in spatial learning and memory. In addition, mice have reduced brain volume. Mice lacking both NLGN1 and NLGN2, or NLGN1 and NLGN3, are viable, but have impaired breathing, drastically reduced reproduction rates and striking deficits in raising their offspring. Mice lacking NLGN1, NLGN2 and NLGN3 are born at the expected Mendelian rate, but die shortly after birth due to respiratory failure. They do not show a significant change in the number of synapses, but synapse function is strongly impaired. Ref.6 Ref.10

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Sequence caution

The sequence BAC65715.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-methyl-D-aspartate receptor clustering

Inferred from sequence or structural similarity. Source: BHF-UCL

alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering

Inferred from direct assay PubMed 12796785. Source: BHF-UCL

calcium-dependent cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeletal matrix organization at active zone

Inferred from mutant phenotype PubMed 19628693. Source: BHF-UCL

establishment of protein localization

Inferred from mutant phenotype PubMed 12796785. Source: BHF-UCL

heterophilic cell-cell adhesion

Inferred from direct assay PubMed 12796785. Source: BHF-UCL

nervous system development

Inferred from direct assay Ref.3. Source: UniProtKB

neurexin clustering

Inferred from direct assay PubMed 12796785. Source: BHF-UCL

neuron cell-cell adhesion

Inferred from direct assay PubMed 12796785. Source: BHF-UCL

positive regulation of dendritic spine development

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of excitatory postsynaptic membrane potential

Inferred from direct assay PubMed 17582332. Source: BHF-UCL

positive regulation of filopodium assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of ruffle assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of synapse assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of synaptic transmission, GABAergic

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of synaptic transmission, glutamatergic

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of synaptic vesicle endocytosis

Inferred from mutant phenotype PubMed 19628693. Source: BHF-UCL

positive regulation of synaptic vesicle exocytosis

Inferred from mutant phenotype PubMed 19628693. Source: BHF-UCL

postsynaptic density protein 95 clustering

Inferred from direct assay PubMed 12796785Ref.5. Source: BHF-UCL

postsynaptic membrane assembly

Inferred from direct assay PubMed 12796785Ref.5. Source: BHF-UCL

presynaptic membrane assembly

Inferred from direct assay Ref.3PubMed 12796785Ref.5. Source: BHF-UCL

protein heterotetramerization

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from direct assay PubMed 12796785. Source: BHF-UCL

protein localization to synapse

Inferred from direct assay Ref.5. Source: BHF-UCL

protein targeting

Inferred from electronic annotation. Source: Ensembl

receptor localization to synapse

Inferred from direct assay PubMed 12796785. Source: BHF-UCL

regulation of N-methyl-D-aspartate selective glutamate receptor activity

Inferred from direct assay PubMed 17582332. Source: BHF-UCL

regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of neuron differentiation

Inferred from direct assay Ref.3. Source: UniProtKB

regulation of respiratory gaseous exchange by neurological system process

Inferred from genetic interaction Ref.6. Source: MGI

regulation of synaptic transmission

Inferred from genetic interaction Ref.6. Source: MGI

synapse assembly

Inferred from direct assay Ref.3. Source: UniProtKB

synapse organization

Inferred from genetic interaction PubMed 21788371. Source: MGI

synaptic vesicle clustering

Inferred from direct assay Ref.3PubMed 12796785. Source: BHF-UCL

synaptic vesicle targeting

Inferred from mutant phenotype Ref.3. Source: UniProtKB

terminal button organization

Inferred from mutant phenotype PubMed 19628693. Source: BHF-UCL

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from electronic annotation. Source: Ensembl

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from sequence or structural similarity. Source: BHF-UCL

dendrite

Inferred from sequence or structural similarity. Source: BHF-UCL

excitatory synapse

Inferred by curator Ref.5PubMed 17582332. Source: BHF-UCL

external side of plasma membrane

Inferred from direct assay PubMed 20573900. Source: MGI

filopodium tip

Inferred from sequence or structural similarity. Source: BHF-UCL

integral component of plasma membrane

Inferred from mutant phenotype Ref.3. Source: UniProtKB

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionneurexin family protein binding

Inferred from mutant phenotype Ref.3. Source: UniProtKB

protein dimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTPRTO145222EBI-775037,EBI-728180From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99K10-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q99K10-2)

The sequence of this isoform differs from the canonical sequence as follows:
     165-184: Missing.
     236-269: GFLSTGDQAAKGNYGLLDLIQALRWTSENIGFFG → EKETIKETISVALQALRTKGGGFIPKQATYKRCE
     270-843: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4545 Potential
Chain46 – 843798Neuroligin-1
PRO_0000008641

Regions

Topological domain46 – 697652Extracellular Potential
Transmembrane698 – 71821Helical; Potential
Topological domain719 – 843125Cytoplasmic Potential

Amino acid modifications

Glycosylation1091N-linked (GlcNAc...) (complex) Ref.11
Glycosylation3031N-linked (GlcNAc...) (complex) By similarity
Glycosylation3431N-linked (GlcNAc...) (complex) By similarity
Glycosylation5471N-linked (GlcNAc...) Ref.11
Glycosylation6831O-linked (GalNAc...) By similarity
Glycosylation6861O-linked (GalNAc...) By similarity
Disulfide bond117 ↔ 153 Ref.11
Disulfide bond342 ↔ 353 Ref.11
Disulfide bond512 ↔ 546 Ref.11

Natural variations

Alternative sequence165 – 18420Missing in isoform 2.
VSP_007528
Alternative sequence236 – 26934GFLST…IGFFG → EKETIKETISVALQALRTKG GGFIPKQATYKRCE in isoform 2.
VSP_007529
Alternative sequence270 – 843574Missing in isoform 2.
VSP_007530

Secondary structure

....................................................................................................... 843
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 23, 2003. Version 2.
Checksum: 69E50709CF7D2E1F

FASTA84394,149
        10         20         30         40         50         60 
MALPRCMWPN YVWRAMMACV VHRGSGAPLT LCLLGCLLQT FHVLSQKLDD VDPLVTTNFG 

        70         80         90        100        110        120 
KIRGIKKELN NEILGPVIQF LGVPYAAPPT GEHRFQPPEP PSPWSDIRNA TQFAPVCPQN 

       130        140        150        160        170        180 
IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS EDCLYLNIYV PTEDGPLTKK HTDDLGDNDG 

       190        200        210        220        230        240 
AEDEDIRDSG GPKPVMVYIH GGSYMEGTGN LYDGSVLASY GNVIVITVNY RLGVLGFLST 

       250        260        270        280        290        300 
GDQAAKGNYG LLDLIQALRW TSENIGFFGG DPLRITVFGS GAGGSCVNLL TLSHYSEGNR 

       310        320        330        340        350        360 
WSNSTKGLFQ RAIAQSGTAL SSWAVSFQPA KYARILATKV GCNVSDTVEL VECLQKKPYK 

       370        380        390        400        410        420 
ELVDQDVQPA RYHIAFGPVI DGDVIPDDPQ ILMEQGEFLN YDIMLGVNQG EGLKFVENIV 

       430        440        450        460        470        480 
DSDDGVSASD FDFAVSNFVD NLYGYPEGKD VLRETIKFMY TDWADRHNPE TRRKTLLALF 

       490        500        510        520        530        540 
TDHQWVAPAV ATADLHSNFG SPTYFYAFYH HCQTDQVPAW ADAAHGDEVP YVLGIPMIGP 

       550        560        570        580        590        600 
TELFPCNFSK NDVMLSAVVM TYWTNFAKTG DPNQPVPQDT KFIHTKPNRF EEVAWTRYSQ 

       610        620        630        640        650        660 
KDQLYLHIGL KPRVKEHYRA NKVNLWLELV PHLHNLNDIS QYTSTTTKVP STDITLRPTR 

       670        680        690        700        710        720 
KNSTPVTSAF PTAKQDDPKQ QPSPFSVDQR DYSTELSVTI AVGASLLFLN ILAFAALYYK 

       730        740        750        760        770        780 
KDKRRHDVHR RCSPQRTTTN DLTHAPEEEI MSLQMKHTDL DHECESIHPH EVVLRTACPP 

       790        800        810        820        830        840 
DYTLAMRRSP DDIPLMTPNT ITMIPNTIPG IQPLHTFNTF TGGQNNTLPH PHPHPHSHST 


TRV 

« Hide

Isoform 2 [UniParc].

Checksum: 1D87ADF1EAFF2F0B
Show »

FASTA24927,602

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons."
Scheiffele P., Fan J., Choih J., Fetter R., Serafini T.
Cell 101:657-669(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory ensheathing glia, a growth-promoting class of macroglia."
Gilbert M., Smith J., Roskams A.J., Auld V.J.
Glia 34:151-164(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins."
Graf E.R., Zhang X., Jin S.X., Linhoff M.W., Craig A.M.
Cell 119:1013-1026(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Neuroligins determine synapse maturation and function."
Varoqueaux F., Aramuni G., Rawson R.L., Mohrmann R., Missler M., Gottmann K., Zhang W., Sudhof T.C., Brose N.
Neuron 51:741-754(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
[7]"Neuroligin-3 is a neuronal adhesion protein at GABAergic and glutamatergic synapses."
Budreck E.C., Scheiffele P.
Eur. J. Neurosci. 26:1738-1748(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NLGN3.
[8]"Unusually rapid evolution of neuroligin-4 in mice."
Bolliger M.F., Pei J., Maxeiner S., Boucard A.A., Grishin N.V., Sudhof T.C.
Proc. Natl. Acad. Sci. U.S.A. 105:6421-6426(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"The synaptic proteins neurexins and neuroligins are widely expressed in the vascular system and contribute to its functions."
Bottos A., Destro E., Rissone A., Graziano S., Cordara G., Assenzio B., Cera M.R., Mascia L., Bussolino F., Arese M.
Proc. Natl. Acad. Sci. U.S.A. 106:20782-20787(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"Neuroligin-1 deletion results in impaired spatial memory and increased repetitive behavior."
Blundell J., Blaiss C.A., Etherton M.R., Espinosa F., Tabuchi K., Walz C., Bolliger M.F., Sudhof T.C., Powell C.M.
J. Neurosci. 30:2115-2129(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[11]"Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions."
Chen X., Liu H., Shim A.H., Focia P.J., He X.
Nat. Struct. Mol. Biol. 15:50-56(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 39-635 IN COMPLEX WITH HUMAN NRX1B, DISULFIDE BONDS, GLYCOSYLATION AT ASN-109 AND ASN-547.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK122433 mRNA. Translation: BAC65715.1. Different initiation.
BC005523 mRNA. Translation: AAH05523.1.
RefSeqNP_619607.2. NM_138666.3.
UniGeneMm.316080.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3B3QX-ray2.40A/B46-635[»]
ProteinModelPortalQ99K10.
SMRQ99K10. Positions 52-631.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-32027N.
IntActQ99K10. 2 interactions.
MINTMINT-5104301.
STRING10090.ENSMUSP00000074565.

Protein family/group databases

MEROPSS09.994.

PTM databases

PhosphoSiteQ99K10.

Proteomic databases

PaxDbQ99K10.
PRIDEQ99K10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075054; ENSMUSP00000074565; ENSMUSG00000063887. [Q99K10-1]
GeneID192167.
KEGGmmu:192167.
UCSCuc008otc.1. mouse. [Q99K10-1]
uc008otd.1. mouse. [Q99K10-2]

Organism-specific databases

CTD22871.
MGIMGI:2179435. Nlgn1.
RougeSearch...

Phylogenomic databases

eggNOGCOG2272.
GeneTreeENSGT00690000101920.
HOGENOMHOG000231424.
HOVERGENHBG008839.
InParanoidQ99K10.
KOK07378.
OMAKFVELIV.
PhylomeDBQ99K10.
TreeFamTF326187.

Gene expression databases

BgeeQ99K10.
CleanExMM_NLGN1.
GenevestigatorQ99K10.

Family and domain databases

InterProIPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000460. Neuroligin.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR01090. NEUROLIGIN.
PROSITEPS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ99K10.
NextBio371168.
PROQ99K10.
SOURCESearch...

Entry information

Entry nameNLGN1_MOUSE
AccessionPrimary (citable) accession number: Q99K10
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: April 16, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot