Q69ZK9 (NLGN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neuroligin-2

Gene names

Name:	Nlgn2
Synonyms:	Kiaa1366

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	836 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	Neuronal cell surface protein thought to be involved in cell-cell-interactions by forming intercellular junctions through binding to beta-neurexins. Seems to play role in formation or maintenance of synaptic junctions. In vitro, triggers the de novo formation of presynaptic structures By similarity.
Subunit structure	Interacts with neurexin 1-beta, neurexin 2-beta and neurexin 3-beta. Interacts with INADL. Probably interacts through its C-terminus with DLG4 third PDZ domain By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein Potential.
Tissue specificity	Brain and arteries (at protein level). Ref.4
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.
Sequence caution	The sequence BAD32437.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	gephyrin clustering Inferred from direct assay. Source: BHF-UCL jump response Inferred from sequence or structural similarity. Source: BHF-UCL locomotory exploration behavior Inferred from mutant phenotype. Source: BHF-UCL neuromuscular process controlling balance Inferred from mutant phenotype. Source: BHF-UCL neuron cell-cell adhesion Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of excitatory postsynaptic membrane potential Inferred from mutant phenotype. Source: BHF-UCL positive regulation of inhibitory postsynaptic membrane potential Inferred from mutant phenotype. Source: BHF-UCL positive regulation of synapse assembly Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of synaptic transmission, GABAergic Inferred from mutant phenotype. Source: BHF-UCL positive regulation of synaptic transmission, glutamatergic Inferred from mutant phenotype. Source: BHF-UCL postsynaptic density protein 95 clustering Inferred from direct assay. Source: BHF-UCL postsynaptic membrane assembly Inferred from direct assay. Source: BHF-UCL presynaptic membrane assembly Inferred from direct assay. Source: BHF-UCL protein localization to synapse Inferred from direct assay. Source: BHF-UCL regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Inferred from mutant phenotype. Source: BHF-UCL regulation of respiratory gaseous exchange by neurological system process Inferred from genetic interaction. Source: MGI sensory perception of pain Inferred from mutant phenotype. Source: BHF-UCL social behavior Inferred from sequence or structural similarity. Source: BHF-UCL terminal button organization Inferred from sequence or structural similarity. Source: BHF-UCL thigmotaxis Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	cell surface Inferred from sequence or structural similarity. Source: BHF-UCL excitatory synapse Inferred by curator. Source: BHF-UCL inhibitory synapse Inferred by curator. Source: BHF-UCL integral to plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	cell adhesion molecule binding Inferred from physical interaction. Source: BHF-UCL neurexin family protein binding Inferred from physical interaction. Source: BHF-UCL 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 – 14

14

By similarity

Chain

15 – 836

822

Neuroligin-2

PRO_0000041879

Regions

Topological domain

15 – 678

664

Extracellular Potential

Transmembrane

679 – 699

21

Helical; Potential

Topological domain

700 – 836

137

Cytoplasmic Potential

Amino acid modifications

Modified residue

714

1

Phosphoserine Ref.3

Glycosylation

98

1

N-linked (GlcNAc...) Ref.5

Glycosylation

136

1

N-linked (GlcNAc...) Potential

Glycosylation

522

1

N-linked (GlcNAc...) Potential

Disulfide bond

106 ↔ 141

Ref.5

Disulfide bond

317 ↔ 328

Ref.5

Disulfide bond

487 ↔ 521

Ref.5

Experimental info

Sequence conflict

210

1

V → A in BAD32437. Ref.1

Secondary structure

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836

Helix Strand Turn

Details...

Beta strand

59 – 63

5

Beta strand

66 – 73

8

Turn

81 – 84

4

Beta strand

94 – 97

4

Beta strand

110 – 112

3

Turn

116 – 118

3

Helix

121 – 125

5

Helix

127 – 131

5

Helix

132 – 134

3

Beta strand

135 – 137

3

Beta strand

143 – 149

7

Beta strand

151 – 154

4

Beta strand

177 – 183

7

Beta strand

186 – 190

5

Helix

193 – 195

3

Helix

199 – 205

7

Beta strand

207 – 212

6

Helix

217 – 221

5

Helix

233 – 248

16

Helix

249 – 252

4

Beta strand

254 – 264

11

Helix

266 – 276

11

Beta strand

281 – 283

3

Beta strand

286 – 291

6

Beta strand

294 – 296

3

Turn

297 – 299

3

Helix

304 – 315

12

Helix

322 – 329

8

Helix

334 – 338

5

Beta strand

350 – 352

3

Beta strand

357 – 360

4

Helix

364 – 370

7

Beta strand

377 – 383

7

Helix

390 – 394

5

Beta strand

396 – 400

5

Helix

403 – 416

14

Helix

424 – 435

12

Helix

444 – 459

16

Helix

461 – 473

13

Beta strand

478 – 484

7

Turn

500 – 503

4

Helix

504 – 508

5

Helix

510 – 513

4

Beta strand

517 – 519

3

Helix

525 – 544

20

Beta strand

549 – 551

3

Helix

564 – 566

3

Beta strand

575 – 577

3

Beta strand

579 – 586

8

Beta strand

589 – 592

4

Helix

595 – 602

8

Turn

603 – 605

3

Helix

606 – 608

3

Sequences

	Sequence		Length	Mass (Da)
	Q69ZK9 [UniParc]. Last modified September 13, 2005. Version 2. Checksum: 4C03297F4F1A1F14	FASTA	836	90,989
	10 20 30 40 50 60 MWLLALCLVG LAGAQRGGGG PGGGAPGGPG LGLGSLGEER FPVVNTAYGR VRGVRRELNN 70 80 90 100 110 120 EILGPVVQFL GVPYATPPLG ARRFQPPEAP ASWPGVRNAT TLPPACPQNL HGALPAIMLP 130 140 150 160 170 180 VWFTDNLEAA ATYVQNQSED CLYLNLYVPT EDGPLTKKRD EATLNPPDTD IRDSGKKPVM 190 200 210 220 230 240 LFLHGGSYME GTGNMFDGSV LAAYGNVIVV TLNYRLGVLG FLSTGDQAAK GNYGLLDQIQ 250 260 270 280 290 300 ALRWLSENIA HFGGDPERIT IFGSGAGASC VNLLILSHHS EGLFQKAIAQ SGTAISSWSV 310 320 330 340 350 360 NYQPLKYTRL LAAKVGCDRE DSTEAVECLR RKSSRELVDQ DVQPARYHIA FGPVVDGDVV 370 380 390 400 410 420 PDDPEILMQQ GEFLNYDMLI GVNQGEGLKF VEDSAESEDG VSASAFDFTV SNFVDNLYGY 430 440 450 460 470 480 PEGKDVLRET IKFMYTDWAD RDNGEMRRKT LLALFTDHQW VAPAVATAKL HADYQSPVYF 490 500 510 520 530 540 YTFYHHCQAE GRPEWADAAH GDELPYVFGV PMVGATDLFP CNFSKNDVML SAVVMTYWTN 550 560 570 580 590 600 FAKTGDPNQP VPQDTKFIHT KPNRFEEVVW SKFNSKEKQY LHIGLKPRVR DNYRANKVAF 610 620 630 640 650 660 WLELVPHLHN LHTELFTTTT RLPPYATRWP PRTPGPGTSG TRRPPPPATL PPESDIDLGP 670 680 690 700 710 720 RAYDRFPGDS RDYSTELSVT VAVGASLLFL NILAFAALYY KRDRRQELRC RRLSPPGGSG 730 740 750 760 770 780 SGVPGGGPLL PTAGRELPPE EELVSLQLKR GGGVGADPAE ALRPACPPDY TLALRRAPDD 790 800 810 820 830 VPLLAPGALT LLPSGLGPPP PPPPPSLHPF GPFPPPPPTA TSHNNTLPHP HSTTRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 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., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H. DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryonic tail.
[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: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714, MASS SPECTROMETRY. Tissue: Brain cortex.
[4]	"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: 19926856] [Abstract] Cited for: TISSUE SPECIFICITY.
[5]	"Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2." Koehnke J., Jin X., Budreck E.C., Posy S., Scheiffele P., Honig B., Shapiro L. Proc. Natl. Acad. Sci. U.S.A. 105:1873-1878(2008) [PubMed: 18250328] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 42-612, DISULFIDE BONDS, GLYCOSYLATION AT ASN-98.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK173159 mRNA. Translation: BAD32437.1. Different initiation.
AL603707 Genomic DNA. Translation: CAI51964.1.

IPI

IPI00468605.

RefSeq

NP_942562.2. NM_198862.2.

UniGene

Mm.151293.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BL8	X-ray	3.30	A/B/C/D	42-612	[»]

ProteinModelPortal

Q69ZK9.

SMR

Q69ZK9. Positions 42-609.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29702N.

IntAct

Q69ZK9. 2 interactions.

STRING

Q69ZK9.

PTM databases

PhosphoSite

Q69ZK9.

Proteomic databases

PRIDE

Q69ZK9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000056484; ENSMUSP00000053097; ENSMUSG00000051790.
ENSMUST00000108634; ENSMUSP00000104274; ENSMUSG00000051790.

GeneID

216856.

KEGG

mmu:216856.

UCSC

uc007jrw.1. mouse.

Organism-specific databases

CTD

57555.

MGI

MGI:2681835. Nlgn2.

Rouge

Search...

Phylogenomic databases

HOGENOM

HBG716688.

HOVERGEN

HBG008839.

InParanoid

Q69ZK9.

OMA

DIRDPGK.

OrthoDB

EOG4ZPDTP.

Gene expression databases

ArrayExpress

Q69ZK9.

Bgee

Q69ZK9.

CleanEx

MM_NLGN2.

Genevestigator

Q69ZK9.

GermOnline

ENSMUSG00000051790. Mus musculus.

Family and domain databases

InterPro

IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000460. Neuroligin.
[Graphical view]

KO

K07378.

Pfam

PF00135. COesterase. 1 hit.
[Graphical view]

PRINTS

PR01090. NEUROLIGIN.

PROSITE

PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

375400.

SOURCE

Search...

Entry information

Entry name

NLGN2_MOUSE

Accession

Primary (citable) accession number: Q69ZK9
Secondary accession number(s): Q5F288

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	September 13, 2005
Last modified:	November 16, 2011
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program