Q8BYM5 (NLGN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neuroligin-3

Alternative name(s):
Gliotactin homolog

Gene names

Name:

Nlgn3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	825 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. May also play a role in glia-glia or glia-neuron interactions in the developing peripheral nervous system. Ref.4
Subunit structure	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. Ref.5
Subcellular location	Cell membrane; Single-pass type I membrane protein. Cell junction › synapse. Note: Detected at both glutamatergic and GABAergic synapses. Ref.5
Tissue specificity	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. Ref.3 Ref.4 Ref.5 Ref.7 Ref.9
Developmental stage	Detected at embryonic day E17 and postnatal day P1 in retinal astrocytes, spinal chord astrocytes and Schwann cells of the dorsal root ganglion. Ref.3
Disruption phenotype	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. Ref.4 Ref.8
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Membrane Synapse
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon extension Inferred from sequence or structural similarity. Source: BHF-UCL neuron cell-cell adhesion Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Inferred from mutant phenotype PubMed 21642956. Source: BHF-UCL positive regulation of excitatory postsynaptic membrane potential Inferred from mutant phenotype PubMed 21642956. Source: BHF-UCL positive regulation of synapse assembly Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of synaptic transmission, glutamatergic Inferred from mutant phenotype PubMed 21642956. Source: BHF-UCL postsynaptic membrane assembly Inferred from mutant phenotype PubMed 21642956. Source: BHF-UCL presynaptic membrane assembly Inferred from sequence or structural similarity. Source: BHF-UCL receptor-mediated endocytosis Inferred from sequence or structural similarity. Source: BHF-UCL regulation of N-methyl-D-aspartate selective glutamate receptor activity Inferred from mutant phenotype PubMed 21808020. Source: BHF-UCL regulation of dendritic spine morphogenesis Inferred from mutant phenotype PubMed 21808020. Source: BHF-UCL regulation of inhibitory postsynaptic membrane potential Inferred from mutant phenotype PubMed 21808020. Source: BHF-UCL regulation of long-term synaptic potentiation Inferred from mutant phenotype PubMed 21808020. Source: BHF-UCL regulation of respiratory gaseous exchange by neurological system process Inferred from genetic interaction Ref.4. Source: MGI regulation of terminal button organization Inferred from mutant phenotype PubMed 21808020. Source: BHF-UCL rhythmic synaptic transmission Inferred from sequence or structural similarity. Source: BHF-UCL social behavior Inferred from mutant phenotype PubMed 21808020. Source: BHF-UCL visual learning Inferred from mutant phenotype PubMed 17823315. Source: MGI
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from sequence or structural similarity. Source: BHF-UCL endocytic vesicle Inferred from sequence or structural similarity. Source: BHF-UCL excitatory synapse Inferred from sequence or structural similarity. Source: BHF-UCL integral to plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	cell adhesion molecule binding Inferred from sequence or structural similarity. Source: BHF-UCL neurexin family protein binding Inferred from Biological aspect of Ancestor. Source: RefGenome receptor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 34	34	Potential
	Chain	35 – 825	791	Neuroligin-3		PRO_0000008646
Regions
	Topological domain	35 – 686	652	Extracellular Potential
	Transmembrane	687 – 707	21	Helical; Potential
	Topological domain	708 – 825	118	Cytoplasmic Potential
Amino acid modifications
	Modified residue	769	1	Phosphotyrosine Ref.6
	Glycosylation	95	1	N-linked (GlcNAc...) Potential
	Glycosylation	522	1	N-linked (GlcNAc...) Potential
	Disulfide bond	103 ↔ 138		By similarity
	Disulfide bond	317 ↔ 328		By similarity
	Disulfide bond	487 ↔ 521		By similarity
Experimental info
	Sequence conflict	64	1	D → E in BAC30207. Ref.1
	Sequence conflict	459	1	Q → K in BAC31918. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8BYM5 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: CEF160C63E0A71A4	FASTA	825	91,162
	10 20 30 40 50 60 MWLQPSLSLS PTPTVGRSLC LTLGFLSLVL RASTQAPAPT VNTHFGKLRG ARVPLPSEIL 70 80 90 100 110 120 GPVDQYLGVP YAAPPIGEKR FLPPEPPPSW SGIRNATHFP PVCPQNIHTA VPEVMLPVWF 130 140 150 160 170 180 TANLDIVATY IQEPNEDCLY LNVYVPTEDG SGAKKQGEDL ADNDGDEDED IRDSGAKPVM 190 200 210 220 230 240 VYIHGGSYME GTGNMIDGSV LASYGNVIVI TLNYRVGVLG FLSTGDQAAK GNYGLLDQIQ 250 260 270 280 290 300 ALRWVSENIA FFGGDPRRIT VFGSGIGASC VSLLTLSHHS EGLFQRAIIQ SGSALSSWAV 310 320 330 340 350 360 NYQPVKYTSL LADKVGCNVL DTVDMVDCLR QKSAKELVEQ DIQPARYHVA FGPVIDGDVI 370 380 390 400 410 420 PDDPEILMEQ GEFLNYDIML GVNQGEGLKF VEGVVDPEDG VSGTDFDYSV SNFVDNLYGY 430 440 450 460 470 480 PEGKDTLRET IKFMYTDWAD RDNPETRRKT LVALFTDHQW VEPSVVTADL HARYGSPTYF 490 500 510 520 530 540 YAFYHHCQSL MKPAWSDAAH GDEVPYVFGV PMVGPTDLFP CNFSKNDVML SAVVMTYWTN 550 560 570 580 590 600 FAKTGDPNKP VPQDTKFIHT KANRFEEVAW SKYNPRDQLY LHIGLKPRVR DHYRATKVAF 610 620 630 640 650 660 WKHLVPHLYN LHDMFHYTST TTKVPPPDTT HSSHITRRPN GKTWSTKRPA ISPAYSNENA 670 680 690 700 710 720 PGSWNGDQDA GPLLVENPRD YSTELSVTIA VGASLLFLNV LAFAALYYRK DKRRQEPLRQ 730 740 750 760 770 780 PSPQRGTGAP ELGTAPEEEL AALQLGPTHH ECEAGPPHDT LRLTALPDYT LTLRRSPDDI 790 800 810 820 PLMTPNTITM IPNSLVGLQT LHPYNTFAAG FNSTGLPHSH STTRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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]	"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.
[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, MASS SPECTROMETRY. Tissue: Brain.
[7]	"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.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK039018 mRNA. Translation: BAC30207.1. AK044438 mRNA. Translation: BAC31918.1. AL683892 Genomic DNA. Translation: CAM24450.1.
IPI	IPI00227168.
RefSeq	NP_766520.2. NM_172932.4.
UniGene	Mm.121508.
3D structure databases
ProteinModelPortal	Q8BYM5.
SMR	Q8BYM5. Positions 39-606.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8BYM5. 1 interaction.
Protein family/group databases
MEROPS	S09.987.
PTM databases
PhosphoSite	Q8BYM5.
Proteomic databases
PaxDb	Q8BYM5.
PRIDE	Q8BYM5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000065858; ENSMUSP00000066304; ENSMUSG00000031302.
GeneID	245537.
KEGG	mmu:245537.
Organism-specific databases
CTD	54413.
MGI	MGI:2444609. Nlgn3.
Phylogenomic databases
eggNOG	COG2272.
GeneTree	ENSGT00690000101920.
HOGENOM	HOG000231424.
HOVERGEN	HBG008839.
KO	K07378.
OrthoDB	EOG4CZBF6.
Gene expression databases
ArrayExpress	Q8BYM5.
Bgee	Q8BYM5.
CleanEx	MM_NLGN3.
Genevestigator	Q8BYM5.
GermOnline	ENSMUSG00000031302. Mus musculus.
Family and domain databases
InterPro	IPR002018. CarbesteraseB. IPR019819. Carboxylesterase_B_CS. IPR000460. Neuroligin. [Graphical view]
Pfam	PF00135. COesterase. 1 hit. [Graphical view]
PRINTS	PR01090. NEUROLIGIN.
PROSITE	PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NLGN3. mouse.
NextBio	386794.
SOURCE	Search...

Entry information

Entry name

NLGN3_MOUSE

Accession

Primary (citable) accession number: Q8BYM5
Secondary accession number(s): A2AGI1, Q8BXR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 23, 2003
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program