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Q8BYM5

- NLGN3_MOUSE

UniProt

Q8BYM5 - NLGN3_MOUSE

Protein

Neuroligin-3

Gene

Nlgn3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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. May also play a role in glia-glia or glia-neuron interactions in the developing peripheral nervous system.1 Publication

    GO - Molecular functioni

    1. cell adhesion molecule binding Source: BHF-UCL
    2. neurexin family protein binding Source: BHF-UCL
    3. receptor activity Source: RefGenome

    GO - Biological processi

    1. adult behavior Source: Ensembl
    2. axon extension Source: BHF-UCL
    3. neuron cell-cell adhesion Source: BHF-UCL
    4. oligodendrocyte differentiation Source: MGI
    5. positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: BHF-UCL
    6. positive regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
    7. positive regulation of synapse assembly Source: BHF-UCL
    8. positive regulation of synaptic transmission, glutamatergic Source: BHF-UCL
    9. postsynaptic membrane assembly Source: BHF-UCL
    10. presynaptic membrane assembly Source: BHF-UCL
    11. receptor-mediated endocytosis Source: BHF-UCL
    12. regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: BHF-UCL
    13. regulation of dendritic spine morphogenesis Source: BHF-UCL
    14. regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
    15. regulation of inhibitory postsynaptic membrane potential Source: BHF-UCL
    16. regulation of long-term synaptic potentiation Source: BHF-UCL
    17. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: BHF-UCL
    18. regulation of respiratory gaseous exchange by neurological system process Source: MGI
    19. regulation of synaptic transmission Source: MGI
    20. regulation of synaptic transmission, glutamatergic Source: BHF-UCL
    21. regulation of terminal button organization Source: BHF-UCL
    22. rhythmic synaptic transmission Source: BHF-UCL
    23. social behavior Source: BHF-UCL
    24. synapse assembly Source: RefGenome
    25. synapse organization Source: MGI
    26. visual learning Source: MGI
    27. vocalization behavior Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Protein family/group databases

    MEROPSiS09.987.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuroligin-3
    Alternative name(s):
    Gliotactin homolog
    Gene namesi
    Name:Nlgn3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:2444609. Nlgn3.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cell junctionsynapse 1 Publication
    Note: Detected at both glutamatergic and GABAergic synapses.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell surface Source: BHF-UCL
    3. endocytic vesicle Source: BHF-UCL
    4. excitatory synapse Source: BHF-UCL
    5. integral component of plasma membrane Source: BHF-UCL
    6. synapse Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Synapse

    Pathology & Biotechi

    Disruption phenotypei

    No obvious phenotype, but mice present subtle behavorial changes with reduced ultrasound vocalization and impaired response to olfactory cues. In addition, mice have reduced brain volume. Mice lacking both NLGN1 and NLGN3, or NLGN2 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 – 3434Sequence AnalysisAdd
    BLAST
    Chaini35 – 825791Neuroligin-3PRO_0000008646Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi103 ↔ 138By similarity
    Disulfide bondi317 ↔ 328By similarity
    Disulfide bondi487 ↔ 521By similarity
    Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence Analysis
    Modified residuei769 – 7691Phosphotyrosine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ8BYM5.
    PaxDbiQ8BYM5.
    PRIDEiQ8BYM5.

    PTM databases

    PhosphoSiteiQ8BYM5.

    Expressioni

    Tissue specificityi

    Brain and arteries (at protein level). Detected in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Expressed in olfactory bulb and olfactory epithelium. Found in olfactory ensheathing glia but not in olfactory neurons, and in developing peripheral glia.5 Publications

    Developmental stagei

    Detected at embryonic day E17 and postnatal day P1 in retinal astrocytes, spinal chord astrocytes and Schwann cells of the dorsal root ganglion.1 Publication

    Gene expression databases

    BgeeiQ8BYM5.
    CleanExiMM_NLGN3.
    GenevestigatoriQ8BYM5.

    Interactioni

    Subunit structurei

    Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3) By similarity. Homodimer, and heterodimer with NLGN1 and NLGN2 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ8BYM5. 2 interactions.
    MINTiMINT-4103912.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BYM5.
    SMRiQ8BYM5. Positions 39-606.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini35 – 686652ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini708 – 825118CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei687 – 70721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2272.
    GeneTreeiENSGT00690000101920.
    HOGENOMiHOG000231424.
    HOVERGENiHBG008839.
    KOiK07378.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q8BYM5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWLQPSLSLS PTPTVGRSLC LTLGFLSLVL RASTQAPAPT VNTHFGKLRG    50
    ARVPLPSEIL GPVDQYLGVP YAAPPIGEKR FLPPEPPPSW SGIRNATHFP 100
    PVCPQNIHTA VPEVMLPVWF TANLDIVATY IQEPNEDCLY LNVYVPTEDG 150
    SGAKKQGEDL ADNDGDEDED IRDSGAKPVM VYIHGGSYME GTGNMIDGSV 200
    LASYGNVIVI TLNYRVGVLG FLSTGDQAAK GNYGLLDQIQ ALRWVSENIA 250
    FFGGDPRRIT VFGSGIGASC VSLLTLSHHS EGLFQRAIIQ SGSALSSWAV 300
    NYQPVKYTSL LADKVGCNVL DTVDMVDCLR QKSAKELVEQ DIQPARYHVA 350
    FGPVIDGDVI PDDPEILMEQ GEFLNYDIML GVNQGEGLKF VEGVVDPEDG 400
    VSGTDFDYSV SNFVDNLYGY PEGKDTLRET IKFMYTDWAD RDNPETRRKT 450
    LVALFTDHQW VEPSVVTADL HARYGSPTYF YAFYHHCQSL MKPAWSDAAH 500
    GDEVPYVFGV PMVGPTDLFP CNFSKNDVML SAVVMTYWTN FAKTGDPNKP 550
    VPQDTKFIHT KANRFEEVAW SKYNPRDQLY LHIGLKPRVR DHYRATKVAF 600
    WKHLVPHLYN LHDMFHYTST TTKVPPPDTT HSSHITRRPN GKTWSTKRPA 650
    ISPAYSNENA PGSWNGDQDA GPLLVENPRD YSTELSVTIA VGASLLFLNV 700
    LAFAALYYRK DKRRQEPLRQ PSPQRGTGAP ELGTAPEEEL AALQLGPTHH 750
    ECEAGPPHDT LRLTALPDYT LTLRRSPDDI PLMTPNTITM IPNSLVGLQT 800
    LHPYNTFAAG FNSTGLPHSH STTRV 825
    Length:825
    Mass (Da):91,162
    Last modified:July 27, 2011 - v2
    Checksum:iCEF160C63E0A71A4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641D → E in BAC30207. (PubMed:16141072)Curated
    Sequence conflicti459 – 4591Q → K in BAC31918. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK039018 mRNA. Translation: BAC30207.1.
    AK044438 mRNA. Translation: BAC31918.1.
    AL683892 Genomic DNA. Translation: CAM24450.1.
    CCDSiCCDS30313.1.
    RefSeqiNP_766520.2. NM_172932.4.
    UniGeneiMm.121508.

    Genome annotation databases

    EnsembliENSMUST00000065858; ENSMUSP00000066304; ENSMUSG00000031302.
    GeneIDi245537.
    KEGGimmu:245537.
    UCSCiuc009txj.3. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK039018 mRNA. Translation: BAC30207.1 .
    AK044438 mRNA. Translation: BAC31918.1 .
    AL683892 Genomic DNA. Translation: CAM24450.1 .
    CCDSi CCDS30313.1.
    RefSeqi NP_766520.2. NM_172932.4.
    UniGenei Mm.121508.

    3D structure databases

    ProteinModelPortali Q8BYM5.
    SMRi Q8BYM5. Positions 39-606.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BYM5. 2 interactions.
    MINTi MINT-4103912.

    Protein family/group databases

    MEROPSi S09.987.

    PTM databases

    PhosphoSitei Q8BYM5.

    Proteomic databases

    MaxQBi Q8BYM5.
    PaxDbi Q8BYM5.
    PRIDEi Q8BYM5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000065858 ; ENSMUSP00000066304 ; ENSMUSG00000031302 .
    GeneIDi 245537.
    KEGGi mmu:245537.
    UCSCi uc009txj.3. mouse.

    Organism-specific databases

    CTDi 54413.
    MGIi MGI:2444609. Nlgn3.

    Phylogenomic databases

    eggNOGi COG2272.
    GeneTreei ENSGT00690000101920.
    HOGENOMi HOG000231424.
    HOVERGENi HBG008839.
    KOi K07378.
    TreeFami TF326187.

    Miscellaneous databases

    ChiTaRSi NLGN3. mouse.
    NextBioi 386794.
    PROi Q8BYM5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BYM5.
    CleanExi MM_NLGN3.
    Genevestigatori Q8BYM5.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Hypothalamus and Retina.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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, DEVELOPMENTAL STAGE.
    4. Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
    5. "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 NLGN1 AND NLGN2, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    7. Cited for: TISSUE SPECIFICITY.
    8. "Neuroligin-3-deficient mice: model of a monogenic heritable form of autism with an olfactory deficit."
      Radyushkin K., Hammerschmidt K., Boretius S., Varoqueaux F., El-Kordi A., Ronnenberg A., Winter D., Frahm J., Fischer J., Brose N., Ehrenreich H.
      Genes Brain Behav. 8:416-425(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    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.

    Entry informationi

    Entry nameiNLGN3_MOUSE
    AccessioniPrimary (citable) accession number: Q8BYM5
    Secondary accession number(s): A2AGI1, Q8BXR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 23, 2003
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 110 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3