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Q99K10

- NLGN1_MOUSE

UniProt

Q99K10 - NLGN1_MOUSE

Protein

Neuroligin-1

Gene

Nlgn1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (23 May 2003)
      Previous versions | rss
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    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.3 Publications

    GO - Molecular functioni

    1. neurexin family protein binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. protein dimerization activity Source: BHF-UCL
    4. receptor activity Source: RefGenome

    GO - Biological processi

    1. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering Source: BHF-UCL
    2. calcium-dependent cell-cell adhesion Source: UniProtKB
    3. cytoskeletal matrix organization at active zone Source: BHF-UCL
    4. establishment of protein localization Source: BHF-UCL
    5. heterophilic cell-cell adhesion Source: BHF-UCL
    6. nervous system development Source: UniProtKB
    7. neurexin clustering Source: BHF-UCL
    8. neuron cell-cell adhesion Source: BHF-UCL
    9. N-methyl-D-aspartate receptor clustering Source: BHF-UCL
    10. positive regulation of dendritic spine development Source: BHF-UCL
    11. positive regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
    12. positive regulation of filopodium assembly Source: BHF-UCL
    13. positive regulation of ruffle assembly Source: Ensembl
    14. positive regulation of synapse assembly Source: BHF-UCL
    15. positive regulation of synaptic transmission, GABAergic Source: BHF-UCL
    16. positive regulation of synaptic transmission, glutamatergic Source: BHF-UCL
    17. positive regulation of synaptic vesicle endocytosis Source: BHF-UCL
    18. positive regulation of synaptic vesicle exocytosis Source: BHF-UCL
    19. postsynaptic density protein 95 clustering Source: BHF-UCL
    20. postsynaptic membrane assembly Source: BHF-UCL
    21. presynaptic membrane assembly Source: BHF-UCL
    22. protein heterotetramerization Source: Ensembl
    23. protein homooligomerization Source: BHF-UCL
    24. protein localization to synapse Source: BHF-UCL
    25. protein targeting Source: Ensembl
    26. receptor localization to synapse Source: BHF-UCL
    27. regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: BHF-UCL
    28. regulation of neuron differentiation Source: UniProtKB
    29. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: BHF-UCL
    30. regulation of respiratory gaseous exchange by neurological system process Source: MGI
    31. regulation of synaptic transmission Source: MGI
    32. synapse assembly Source: UniProtKB
    33. synapse organization Source: MGI
    34. synaptic vesicle clustering Source: BHF-UCL
    35. synaptic vesicle targeting Source: UniProtKB
    36. terminal button organization Source: BHF-UCL

    Keywords - Biological processi

    Cell adhesion

    Protein family/group databases

    MEROPSiS09.994.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuroligin-1
    Gene namesi
    Name:Nlgn1
    Synonyms:Kiaa1070
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:2179435. Nlgn1.

    Subcellular locationi

    Cell membrane By similarity; 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.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell surface Source: BHF-UCL
    3. dendrite Source: BHF-UCL
    4. excitatory synapse Source: BHF-UCL
    5. external side of plasma membrane Source: MGI
    6. filopodium tip Source: BHF-UCL
    7. integral component of plasma membrane Source: UniProtKB
    8. N-methyl-D-aspartate selective glutamate receptor complex Source: Ensembl
    9. postsynaptic density Source: UniProtKB-SubCell
    10. postsynaptic membrane Source: UniProtKB-KW
    11. synapse Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4545Sequence AnalysisAdd
    BLAST
    Chaini46 – 843798Neuroligin-1PRO_0000008641Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi109 – 1091N-linked (GlcNAc...) (complex)1 Publication
    Disulfide bondi117 ↔ 1531 Publication
    Glycosylationi303 – 3031N-linked (GlcNAc...) (complex)By similarity
    Disulfide bondi342 ↔ 3531 Publication
    Glycosylationi343 – 3431N-linked (GlcNAc...) (complex)By similarity
    Disulfide bondi512 ↔ 5461 Publication
    Glycosylationi547 – 5471N-linked (GlcNAc...)1 Publication
    Glycosylationi683 – 6831O-linked (GalNAc...)By similarity
    Glycosylationi686 – 6861O-linked (GalNAc...)By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ99K10.
    PRIDEiQ99K10.

    PTM databases

    PhosphoSiteiQ99K10.

    Expressioni

    Tissue specificityi

    Brain and arteries (at protein level). Expressed in olfactory bulb. Detected in brain.4 Publications

    Gene expression databases

    BgeeiQ99K10.
    CleanExiMM_NLGN1.
    GenevestigatoriQ99K10.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PTPRTO145222EBI-775037,EBI-728180From a different organism.

    Protein-protein interaction databases

    DIPiDIP-32027N.
    IntActiQ99K10. 2 interactions.
    MINTiMINT-5104301.
    STRINGi10090.ENSMUSP00000074565.

    Structurei

    Secondary structure

    1
    843
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi54 – 574
    Beta strandi60 – 634
    Beta strandi65 – 673
    Beta strandi77 – 848
    Helixi91 – 933
    Beta strandi105 – 1095
    Beta strandi122 – 1243
    Turni128 – 1303
    Helixi133 – 1375
    Helixi139 – 1457
    Beta strandi147 – 1493
    Beta strandi155 – 1606
    Beta strandi193 – 1986
    Beta strandi202 – 2065
    Helixi209 – 2113
    Helixi215 – 2217
    Beta strandi224 – 2285
    Helixi233 – 2375
    Beta strandi241 – 2455
    Helixi249 – 26416
    Helixi266 – 2683
    Beta strandi270 – 28011
    Helixi282 – 2909
    Beta strandi310 – 3167
    Beta strandi319 – 3213
    Beta strandi324 – 3274
    Helixi329 – 33911
    Helixi347 – 35610
    Helixi359 – 3635
    Beta strandi375 – 3773
    Beta strandi382 – 3854
    Helixi389 – 3957
    Beta strandi402 – 4087
    Turni409 – 4124
    Helixi413 – 4164
    Helixi417 – 4193
    Beta strandi422 – 4243
    Helixi428 – 44316
    Helixi451 – 4599
    Helixi469 – 48416
    Helixi486 – 49813
    Beta strandi503 – 5086
    Turni525 – 5284
    Helixi529 – 5324
    Turni536 – 5383
    Beta strandi542 – 5443
    Helixi550 – 56920
    Beta strandi572 – 5765
    Turni600 – 6023
    Beta strandi604 – 6118
    Beta strandi613 – 6175
    Helixi620 – 6278
    Helixi630 – 6334

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3B3QX-ray2.40A/B46-635[»]
    ProteinModelPortaliQ99K10.
    SMRiQ99K10. Positions 52-631.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99K10.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini46 – 697652ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini719 – 843125CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei698 – 71821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2272.
    GeneTreeiENSGT00690000101920.
    HOGENOMiHOG000231424.
    HOVERGENiHBG008839.
    InParanoidiQ99K10.
    KOiK07378.
    OMAiKFVELIV.
    PhylomeDBiQ99K10.
    TreeFamiTF326187.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    IPR019819. Carboxylesterase_B_CS.
    IPR000460. Neuroligin.
    [Graphical view]
    PfamiPF00135. COesterase. 1 hit.
    [Graphical view]
    PRINTSiPR01090. NEUROLIGIN.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99K10-1) [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

    MALPRCMWPN YVWRAMMACV VHRGSGAPLT LCLLGCLLQT FHVLSQKLDD    50
    VDPLVTTNFG KIRGIKKELN NEILGPVIQF LGVPYAAPPT GEHRFQPPEP 100
    PSPWSDIRNA TQFAPVCPQN IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS 150
    EDCLYLNIYV PTEDGPLTKK HTDDLGDNDG AEDEDIRDSG GPKPVMVYIH 200
    GGSYMEGTGN LYDGSVLASY GNVIVITVNY RLGVLGFLST GDQAAKGNYG 250
    LLDLIQALRW TSENIGFFGG DPLRITVFGS GAGGSCVNLL TLSHYSEGNR 300
    WSNSTKGLFQ RAIAQSGTAL SSWAVSFQPA KYARILATKV GCNVSDTVEL 350
    VECLQKKPYK ELVDQDVQPA RYHIAFGPVI DGDVIPDDPQ ILMEQGEFLN 400
    YDIMLGVNQG EGLKFVENIV DSDDGVSASD FDFAVSNFVD NLYGYPEGKD 450
    VLRETIKFMY TDWADRHNPE TRRKTLLALF TDHQWVAPAV ATADLHSNFG 500
    SPTYFYAFYH HCQTDQVPAW ADAAHGDEVP YVLGIPMIGP TELFPCNFSK 550
    NDVMLSAVVM TYWTNFAKTG DPNQPVPQDT KFIHTKPNRF EEVAWTRYSQ 600
    KDQLYLHIGL KPRVKEHYRA NKVNLWLELV PHLHNLNDIS QYTSTTTKVP 650
    STDITLRPTR KNSTPVTSAF PTAKQDDPKQ QPSPFSVDQR DYSTELSVTI 700
    AVGASLLFLN ILAFAALYYK KDKRRHDVHR RCSPQRTTTN DLTHAPEEEI 750
    MSLQMKHTDL DHECESIHPH EVVLRTACPP DYTLAMRRSP DDIPLMTPNT 800
    ITMIPNTIPG IQPLHTFNTF TGGQNNTLPH PHPHPHSHST TRV 843

    Note: No experimental confirmation available.

    Length:843
    Mass (Da):94,149
    Last modified:May 23, 2003 - v2
    Checksum:i69E50709CF7D2E1F
    GO
    Isoform 2 (identifier: Q99K10-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:249
    Mass (Da):27,602
    Checksum:i1D87ADF1EAFF2F0B
    GO

    Sequence cautioni

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei165 – 18420Missing in isoform 2. 1 PublicationVSP_007528Add
    BLAST
    Alternative sequencei236 – 26934GFLST…IGFFG → EKETIKETISVALQALRTKG GGFIPKQATYKRCE in isoform 2. 1 PublicationVSP_007529Add
    BLAST
    Alternative sequencei270 – 843574Missing in isoform 2. 1 PublicationVSP_007530Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK122433 mRNA. Translation: BAC65715.1. Different initiation.
    BC005523 mRNA. Translation: AAH05523.1.
    CCDSiCCDS17268.1. [Q99K10-1]
    RefSeqiNP_619607.2. NM_138666.3. [Q99K10-1]
    UniGeneiMm.316080.

    Genome annotation databases

    EnsembliENSMUST00000075054; ENSMUSP00000074565; ENSMUSG00000063887. [Q99K10-1]
    GeneIDi192167.
    KEGGimmu:192167.
    UCSCiuc008otc.1. mouse. [Q99K10-1]
    uc008otd.1. mouse. [Q99K10-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK122433 mRNA. Translation: BAC65715.1 . Different initiation.
    BC005523 mRNA. Translation: AAH05523.1 .
    CCDSi CCDS17268.1. [Q99K10-1 ]
    RefSeqi NP_619607.2. NM_138666.3. [Q99K10-1 ]
    UniGenei Mm.316080.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3B3Q X-ray 2.40 A/B 46-635 [» ]
    ProteinModelPortali Q99K10.
    SMRi Q99K10. Positions 52-631.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-32027N.
    IntActi Q99K10. 2 interactions.
    MINTi MINT-5104301.
    STRINGi 10090.ENSMUSP00000074565.

    Protein family/group databases

    MEROPSi S09.994.

    PTM databases

    PhosphoSitei Q99K10.

    Proteomic databases

    PaxDbi Q99K10.
    PRIDEi Q99K10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000075054 ; ENSMUSP00000074565 ; ENSMUSG00000063887 . [Q99K10-1 ]
    GeneIDi 192167.
    KEGGi mmu:192167.
    UCSCi uc008otc.1. mouse. [Q99K10-1 ]
    uc008otd.1. mouse. [Q99K10-2 ]

    Organism-specific databases

    CTDi 22871.
    MGIi MGI:2179435. Nlgn1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG2272.
    GeneTreei ENSGT00690000101920.
    HOGENOMi HOG000231424.
    HOVERGENi HBG008839.
    InParanoidi Q99K10.
    KOi K07378.
    OMAi KFVELIV.
    PhylomeDBi Q99K10.
    TreeFami TF326187.

    Miscellaneous databases

    EvolutionaryTracei Q99K10.
    NextBioi 371168.
    PROi Q99K10.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99K10.
    CleanExi MM_NLGN1.
    Genevestigatori Q99K10.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    IPR019819. Carboxylesterase_B_CS.
    IPR000460. Neuroligin.
    [Graphical view ]
    Pfami PF00135. COesterase. 1 hit.
    [Graphical view ]
    PRINTSi PR01090. NEUROLIGIN.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiNLGN1_MOUSE
    AccessioniPrimary (citable) accession number: Q99K10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 23, 2003
    Last sequence update: May 23, 2003
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3