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Protein

Neuroligin-1

Gene

Nlgn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Required to maintain wakefulness quality and normal synchrony of cerebral cortex activity during wakefulness and sleep (By similarity).By similarity2 Publications

GO - Molecular functioni

  • carboxylic ester hydrolase activity Source: GO_Central
  • cell adhesion molecule binding Source: BHF-UCL
  • neurexin family protein binding Source: UniProtKB
  • protein dimerization activity Source: BHF-UCL
  • receptor activity Source: BHF-UCL

GO - Biological processi

  • AMPA glutamate receptor clustering Source: BHF-UCL
  • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • cytoskeletal matrix organization at active zone Source: BHF-UCL
  • establishment of protein localization Source: BHF-UCL
  • excitatory synapse assembly Source: Ensembl
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: BHF-UCL
  • long-term synaptic potentiation Source: RGD
  • negative regulation of dendritic spine morphogenesis Source: BHF-UCL
  • nervous system development Source: UniProtKB
  • neurexin clustering involved in presynaptic membrane assembly Source: BHF-UCL
  • neuronal ion channel clustering Source: UniProtKB
  • neuron cell-cell adhesion Source: BHF-UCL
  • neuron projection development Source: Ensembl
  • NMDA glutamate receptor clustering Source: BHF-UCL
  • positive regulation of circadian sleep/wake cycle, wakefulness Source: UniProtKB
  • positive regulation of dendritic spine development Source: BHF-UCL
  • positive regulation of excitatory postsynaptic potential Source: BHF-UCL
  • positive regulation of filopodium assembly Source: BHF-UCL
  • positive regulation of intracellular signal transduction Source: BHF-UCL
  • positive regulation of presynaptic active zone assembly Source: BHF-UCL
  • positive regulation of protein localization to synapse Source: RGD
  • positive regulation of ruffle assembly Source: BHF-UCL
  • positive regulation of synapse assembly Source: BHF-UCL
  • positive regulation of synaptic transmission, GABAergic Source: BHF-UCL
  • positive regulation of synaptic transmission, glutamatergic Source: BHF-UCL
  • positive regulation of synaptic vesicle clustering Source: Ensembl
  • positive regulation of synaptic vesicle endocytosis Source: BHF-UCL
  • positive regulation of synaptic vesicle exocytosis Source: BHF-UCL
  • postsynaptic density protein 95 clustering Source: BHF-UCL
  • postsynaptic membrane assembly Source: BHF-UCL
  • presynaptic membrane assembly Source: BHF-UCL
  • protein heterotetramerization Source: RGD
  • protein homooligomerization Source: BHF-UCL
  • protein localization to synapse Source: BHF-UCL
  • protein targeting Source: UniProtKB
  • receptor localization to synapse Source: BHF-UCL
  • regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: BHF-UCL
  • regulation of neuron differentiation Source: UniProtKB
  • regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: BHF-UCL
  • regulation of respiratory gaseous exchange by neurological system process Source: Ensembl
  • rhythmic process Source: UniProtKB-KW
  • synapse assembly Source: UniProtKB
  • synapse organization Source: MGI
  • synaptic vesicle clustering Source: BHF-UCL
  • synaptic vesicle targeting Source: UniProtKB
  • synaptic vesicle transport Source: CACAO
  • terminal button organization Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Biological rhythms, Cell adhesion

Enzyme and pathway databases

ReactomeiR-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

Protein family/group databases

ESTHERiratno-1neur. Neuroligin.
MEROPSiS09.994.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroligin-1
Alternative name(s):
Neuroligin I
Gene namesi
Name:Nlgn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi621117. Nlgn1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini46 – 697ExtracellularSequence analysisAdd BLAST652
Transmembranei698 – 718HelicalSequence analysisAdd BLAST21
Topological domaini719 – 843CytoplasmicSequence analysisAdd BLAST125

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cell surface Source: BHF-UCL
  • dendrite Source: BHF-UCL
  • dendritic shaft Source: RGD
  • dendritic spine Source: BHF-UCL
  • excitatory synapse Source: BHF-UCL
  • external side of plasma membrane Source: Ensembl
  • filopodium tip Source: BHF-UCL
  • Golgi apparatus Source: BHF-UCL
  • integral component of plasma membrane Source: UniProtKB
  • integral component of postsynaptic membrane Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
  • postsynaptic density Source: UniProtKB-SubCell
  • presynapse Source: GOC
  • synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 45Sequence analysisAdd BLAST45
ChainiPRO_000000864246 – 843Neuroligin-1Add BLAST798

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi109N-linked (GlcNAc...) (complex)1 Publication1
Disulfide bondi117 ↔ 153
Disulfide bondi172 ↔ 181
Glycosylationi303N-linked (GlcNAc...) (complex)1 Publication1
Disulfide bondi342 ↔ 353
Glycosylationi343N-linked (GlcNAc...) (complex)1 Publication1
Disulfide bondi512 ↔ 546
Glycosylationi547N-linked (GlcNAc...)1 Publication1
Glycosylationi683O-linked (GalNAc...)1 Publication1
Glycosylationi686O-linked (GalNAc...)1 Publication1
Modified residuei733PhosphoserineBy similarity1
Modified residuei782PhosphotyrosineBy similarity1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ62765.
PRIDEiQ62765.

PTM databases

iPTMnetiQ62765.
PhosphoSitePlusiQ62765.
UniCarbKBiQ62765.

Expressioni

Tissue specificityi

Expressed in brain, almost exclusively in neurons, and spinal chord. Detected in pancreas islet beta cells.4 Publications

Developmental stagei

Expression is low in embryonic brains (E12-E16) but increases dramatically after birth (postnatal days P0-P3) and reaches a plateau during the period when most synapses are formed (P5-P8).1 Publication

Gene expression databases

BgeeiENSRNOG00000032576.
ExpressionAtlasiQ62765. baseline and differential.

Interactioni

Subunit structurei

Interacts with NRXN1, NRXN2 and NRXN3. Interacts with NLGN3. Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with GOPC (By similarity). Interacts with AIP1 and PDZRN3.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nrxn1Q633735EBI-7281118,EBI-1780696

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • neurexin family protein binding Source: UniProtKB
  • protein dimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi250532. 12 interactors.
DIPiDIP-44832N.
IntActiQ62765. 4 interactors.
MINTiMINT-1526995.
STRINGi10116.ENSRNOP00000049486.

Structurei

Secondary structure

1843
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi54 – 57Combined sources4
Beta strandi60 – 63Combined sources4
Beta strandi65 – 67Combined sources3
Beta strandi70 – 74Combined sources5
Beta strandi77 – 84Combined sources8
Helixi91 – 93Combined sources3
Beta strandi105 – 109Combined sources5
Beta strandi122 – 124Combined sources3
Turni128 – 130Combined sources3
Helixi133 – 136Combined sources4
Helixi139 – 145Combined sources7
Beta strandi146 – 149Combined sources4
Beta strandi155 – 161Combined sources7
Helixi169 – 174Combined sources6
Helixi179 – 182Combined sources4
Beta strandi193 – 198Combined sources6
Beta strandi202 – 206Combined sources5
Helixi209 – 211Combined sources3
Helixi215 – 221Combined sources7
Beta strandi224 – 228Combined sources5
Helixi233 – 237Combined sources5
Beta strandi241 – 244Combined sources4
Helixi249 – 264Combined sources16
Helixi265 – 268Combined sources4
Beta strandi270 – 280Combined sources11
Helixi282 – 291Combined sources10
Helixi294 – 296Combined sources3
Beta strandi311 – 316Combined sources6
Beta strandi319 – 321Combined sources3
Helixi329 – 340Combined sources12
Helixi347 – 354Combined sources8
Helixi359 – 363Combined sources5
Beta strandi375 – 377Combined sources3
Beta strandi382 – 385Combined sources4
Helixi389 – 394Combined sources6
Beta strandi402 – 408Combined sources7
Turni409 – 412Combined sources4
Helixi413 – 416Combined sources4
Turni417 – 419Combined sources3
Helixi428 – 443Combined sources16
Beta strandi445 – 448Combined sources4
Helixi452 – 459Combined sources8
Helixi463 – 465Combined sources3
Helixi469 – 484Combined sources16
Helixi486 – 498Combined sources13
Beta strandi503 – 508Combined sources6
Beta strandi515 – 517Combined sources3
Turni525 – 528Combined sources4
Helixi529 – 532Combined sources4
Helixi535 – 538Combined sources4
Beta strandi542 – 544Combined sources3
Helixi550 – 569Combined sources20
Beta strandi574 – 576Combined sources3
Helixi582 – 584Combined sources3
Turni589 – 592Combined sources4
Turni600 – 602Combined sources3
Beta strandi604 – 611Combined sources8
Beta strandi613 – 617Combined sources5
Helixi620 – 627Combined sources8
Helixi629 – 634Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BIWX-ray3.50A/B/C/D46-638[»]
3BIXX-ray1.80A/B/C/D46-638[»]
3VKFX-ray3.30A/B45-638[»]
ProteinModelPortaliQ62765.
SMRiQ62765.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62765.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000231424.
HOVERGENiHBG008839.
InParanoidiQ62765.
KOiK07378.
OMAiKFVELIV.
OrthoDBiEOG091G0CHW.
PhylomeDBiQ62765.
TreeFamiTF326187.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000460. Nlgn.
IPR030022. NLGN1.
[Graphical view]
PANTHERiPTHR11559:SF52. PTHR11559:SF52. 2 hits.
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR01090. NEUROLIGIN.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q62765-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALPRCMWPN YVWRAMMACV VHRGSGAPLT LCLLGCLLQT FHVLSQKLDD
60 70 80 90 100
VDPLVTTNFG KIRGIKKELN NEILGPVIQF LGVPYAAPPT GEHRFQPPEP
110 120 130 140 150
PSPWSDIRNA TQFAPVCPQN IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS
160 170 180 190 200
EDCLYLNIYV PTEDVKRISK ECARKPGKKI CRKGDIRDSG GPKPVMVYIH
210 220 230 240 250
GGSYMEGTGN LYDGSVLASY GNVIVITVNY RLGVLGFLST GDQAAKGNYG
260 270 280 290 300
LLDLIQALRW TSENIGFFGG DPLRITVFGS GAGGSCVNLL TLSHYSEGNR
310 320 330 340 350
WSNSTKGLFQ RAIAQSGTAL SSWAVSFQPA KYARILATKV GCNVSDTVEL
360 370 380 390 400
VECLQKKPYK ELVDQDVQPA RYHIAFGPVI DGDVIPDDPQ ILMEQGEFLN
410 420 430 440 450
YDIMLGVNQG EGLKFVENIV DSDDGVSASD FDFAVSNFVD NLYGYPEGKD
460 470 480 490 500
VLRETIKFMY TDWADRHNPE TRRKTLLALF TDHQWVAPAV ATADLHSNFG
510 520 530 540 550
SPTYFYAFYH HCQTDQVPAW ADAAHGDEVP YVLGIPMIGP TELFPCNFSK
560 570 580 590 600
NDVMLSAVVM TYWTNFAKTG DPNQPVPQDT KFIHTKPNRF EEVAWTRYSQ
610 620 630 640 650
KDQLYLHIGL KPRVKEHYRA NKVNLWLELV PHLHNLNDIS QYTSTTTKVP
660 670 680 690 700
STDITLRPTR KNSTPVTSAF PTAKQDDPKQ QPSPFSVDQR DYSTELSVTI
710 720 730 740 750
AVGASLLFLN ILAFAALYYK KDKRRHDVHR RCSPQRTTTN DLTHAPEEEI
760 770 780 790 800
MSLQMKHTDL DHECESIHPH EVVLRTACPP DYTLAMRRSP DDVPLMTPNT
810 820 830 840
ITMIPNTIPG IQPLHTFNTF TGGQNNTLPH PHPHPHSHST TRV
Length:843
Mass (Da):94,294
Last modified:November 1, 1996 - v1
Checksum:i90A18540245B789D
GO
Isoform 2 (identifier: Q62765-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     165-184: Missing.
     298-306: Missing.

Note: No experimental confirmation available.
Show »
Length:814
Mass (Da):90,995
Checksum:iBA0F19EB618C46F2
GO
Isoform 3 (identifier: Q62765-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     298-306: Missing.

Show »
Length:834
Mass (Da):93,263
Checksum:iC48D369CCB6AEAAA
GO
Isoform 4 (identifier: Q62765-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     165-184: Missing.

Show »
Length:823
Mass (Da):92,026
Checksum:iB3D07E1FF1AB1FD8
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_007531165 – 184Missing in isoform 2 and isoform 4. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_007532298 – 306Missing in isoform 2 and isoform 3. 1 Publication9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22952 mRNA. Translation: AAA85720.1.
RefSeqiNP_446320.1. NM_053868.2. [Q62765-1]
XP_017446072.1. XM_017590583.1. [Q62765-4]
XP_017446073.1. XM_017590584.1. [Q62765-4]
XP_017446074.1. XM_017590585.1. [Q62765-4]
XP_017446075.1. XM_017590586.1. [Q62765-4]
XP_017446076.1. XM_017590587.1. [Q62765-4]
XP_017446077.1. XM_017590588.1. [Q62765-4]
XP_017446078.1. XM_017590589.1. [Q62765-4]
XP_017446079.1. XM_017590590.1. [Q62765-2]
UniGeneiRn.10173.

Genome annotation databases

EnsembliENSRNOT00000092660; ENSRNOP00000075793; ENSRNOG00000032576. [Q62765-1]
GeneIDi116647.
KEGGirno:116647.
UCSCiRGD:621117. rat. [Q62765-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22952 mRNA. Translation: AAA85720.1.
RefSeqiNP_446320.1. NM_053868.2. [Q62765-1]
XP_017446072.1. XM_017590583.1. [Q62765-4]
XP_017446073.1. XM_017590584.1. [Q62765-4]
XP_017446074.1. XM_017590585.1. [Q62765-4]
XP_017446075.1. XM_017590586.1. [Q62765-4]
XP_017446076.1. XM_017590587.1. [Q62765-4]
XP_017446077.1. XM_017590588.1. [Q62765-4]
XP_017446078.1. XM_017590589.1. [Q62765-4]
XP_017446079.1. XM_017590590.1. [Q62765-2]
UniGeneiRn.10173.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BIWX-ray3.50A/B/C/D46-638[»]
3BIXX-ray1.80A/B/C/D46-638[»]
3VKFX-ray3.30A/B45-638[»]
ProteinModelPortaliQ62765.
SMRiQ62765.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250532. 12 interactors.
DIPiDIP-44832N.
IntActiQ62765. 4 interactors.
MINTiMINT-1526995.
STRINGi10116.ENSRNOP00000049486.

Protein family/group databases

ESTHERiratno-1neur. Neuroligin.
MEROPSiS09.994.

PTM databases

iPTMnetiQ62765.
PhosphoSitePlusiQ62765.
UniCarbKBiQ62765.

Proteomic databases

PaxDbiQ62765.
PRIDEiQ62765.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000092660; ENSRNOP00000075793; ENSRNOG00000032576. [Q62765-1]
GeneIDi116647.
KEGGirno:116647.
UCSCiRGD:621117. rat. [Q62765-1]

Organism-specific databases

CTDi22871.
RGDi621117. Nlgn1.

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000231424.
HOVERGENiHBG008839.
InParanoidiQ62765.
KOiK07378.
OMAiKFVELIV.
OrthoDBiEOG091G0CHW.
PhylomeDBiQ62765.
TreeFamiTF326187.

Enzyme and pathway databases

ReactomeiR-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

Miscellaneous databases

EvolutionaryTraceiQ62765.
PROiQ62765.

Gene expression databases

BgeeiENSRNOG00000032576.
ExpressionAtlasiQ62765. baseline and differential.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000460. Nlgn.
IPR030022. NLGN1.
[Graphical view]
PANTHERiPTHR11559:SF52. PTHR11559:SF52. 2 hits.
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR01090. NEUROLIGIN.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNLGN1_RAT
AccessioniPrimary (citable) accession number: Q62765
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.