B0F2B4 (NLGN4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neuroligin 4-like

Alternative name(s):
Neuroligin-4
Short name=NL-4

Gene names

Name:	Nlgn4l
Synonyms:	Nl4*, Nlgn4, Nlgn4x

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	945 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. Plays a role in the formation or maintenance of synaptic junctions via its interactions (via the extracellular domains) with neurexin family members. Plays a role in synaptic signal transmission. Ref.2 Ref.3
Subunit structure	Homodimer. Interacts with NRXN1. Interacts with GPHN and ARHGEF9. Ref.2 Ref.3
Subcellular location	Cell membrane; Single-pass type I membrane protein. Cell junction › synapse › postsynaptic cell membrane. Note: Detected at glycinergic postsynapses in retina. Detected on dendritic spines on cultured neurons. Ref.1 Ref.2 Ref.3
Tissue specificity	Detected in brain cortex, septum, hippocampus, striatum, olfactory bulb, retina, colliculi, brain stem, cerebellum, thymus and skeletal muscle. Detected at inhibitory synapses throughout the brain and spinal cord (at protein level). Detected in brain, spleen, lung, skeletal muscle and kidney. Ref.1 Ref.2 Ref.3
Disruption phenotype	Mice are viable and fertile with no obvious sensory deficits or major perturbations of behavior, but show subtle changes in synaptic signal transmission and signal processing. Mice display subtle deficits in reciprocal social interactions and communication. They have reduced brain volume. Ref.1 Ref.3
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brainstem development Inferred from mutant phenotype Ref.1. Source: BHF-UCL cerebellum development Inferred from mutant phenotype Ref.1. Source: BHF-UCL male courtship behavior Inferred from mutant phenotype Ref.1. Source: BHF-UCL negative regulation of excitatory postsynaptic membrane potential Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of organ growth Inferred from mutant phenotype Ref.1. Source: BHF-UCL presynaptic membrane assembly Inferred from sequence or structural similarity. Source: BHF-UCL social behavior Inferred from mutant phenotype Ref.1. Source: BHF-UCL territorial aggressive behavior Inferred from mutant phenotype Ref.1. Source: BHF-UCL vocalization behavior Inferred from mutant phenotype Ref.1. Source: BHF-UCL
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from sequence or structural similarity. Source: BHF-UCL dendrite 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 Biological aspect of Ancestor. Source: RefGenome postsynaptic membrane Inferred by curator Ref.1. Source: BHF-UCL
Molecular_function	neurexin family protein binding Inferred from sequence or structural similarity. 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 – 18	18	Potential
	Chain	19 – 945	927	Neuroligin 4-like		PRO_0000417951
Regions
	Topological domain	19 – 761	743	Extracellular Potential
	Transmembrane	762 – 782	21	Helical; Potential
	Topological domain	783 – 945	163	Cytoplasmic Potential
	Compositional bias	20 – 77	58	Pro-rich
	Compositional bias	391 – 550	160	Gly-rich
	Compositional bias	720 – 746	27	Ser-rich
	Compositional bias	796 – 821	26	Pro-rich
	Compositional bias	820 – 939	120	Gly-rich
Amino acid modifications
	Disulfide bond	93 ↔ 129		By similarity
	Disulfide bond	315 ↔ 338		By similarity
	Disulfide bond	527 ↔ 583		By similarity
Experimental info
	Sequence conflict	5	1	V → A in ABS19580. Ref.2
	Sequence conflict	5	1	V → A in ACA64246. Ref.2
	Sequence conflict	106	1	C → R in ABS19580. Ref.2
	Sequence conflict	106	1	C → R in ACA64246. Ref.2
	Sequence conflict	150	1	T → P in ACA64246. Ref.2
	Sequence conflict	154	1	H → P in ACA64246. Ref.2
	Sequence conflict	573	1	H → P in ABS19580. Ref.2
	Sequence conflict	573	1	H → P in ACA64246. Ref.2
	Sequence conflict	893	1	T → A in ABS19580. Ref.2
	Sequence conflict	893	1	T → A in ACA64246. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	B0F2B4 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: 03DFC91F1350ED6A	FASTA	945	97,348
	10 20 30 40 50 60 MPAPVPALLC LALALASAQP SPPPPPPFPV VATNYGKLRG VRAALPGDVL GPVTQFLGVP 70 80 90 100 110 120 YAAPPTGERR FQPPEPPSSW AGVRDATRFA PVCPQHLDER ALLRDCLPAW FAANLDAIAA 130 140 150 160 170 180 YVQDQSEDCL YLNLYVPGGA NGKKMADDVT GNDHGDDQDS RDPGVGGAAA AAARKPVMVY 190 200 210 220 230 240 IHGGSYMEGT ANIVDGSVLA SYGDVIVVTV NYRLGVLGFL STGDQAAKGN YGLLDQIQAL 250 260 270 280 290 300 RWVEENAGAF GGDPDRVTVF GSGAGASCVS LLTLSHYSEG LFQKAIIQSG TALSSWAVNY 310 320 330 340 350 360 QPARYARALG ERVGCATPDP GSPPGSPPGW DSASLVSCLR GKAAGELARA RVTPATYHVA 370 380 390 400 410 420 FGPTVDGDVI PDDPQILMEQ GEFLNYDIML GVNQGEGARF VDGLGGGHDG GYGGYGGGYG 430 440 450 460 470 480 GGVEDDEVQD GGPDGAAGGV SAGEFDLAVS GFINDLYGRP EGRGDALRET VKFMYTDWAD 490 500 510 520 530 540 RDSPEARRKT LVALFTDHQW VAPAVATADL HARYGSPTYF YAFYHRCHGG GGGGGGVDGV 550 560 570 580 590 600 AGGVAGGVGG EEARPAWADA AHGDEVPYVF GVHMAGPGDV FGCNFSRNDV MLSAVVMTYW 610 620 630 640 650 660 TNFAKTGDPN QPVAQDTRFV HTRPNRFEEV AWAKYDPRGQ LYLHIGLRPR VRDHYRAAKV 670 680 690 700 710 720 AFWLELVPHL HGLAADPGAY LSAAATRAAP SGDPDRDPGG GGGGRRRPRP ATRRPAVMTS 730 740 750 760 770 780 SSMASGSGMT SSSGSGMTSS SGSSASAVLI ETRRDYSTEL SVTIAVGASL LFLNVLAFAA 790 800 810 820 830 840 LYYKKDKRRH ETHRRPPPPR PPQAPPSAAA ADRNPRPDPG PAGRRGGECG AVVTAMAAEA 850 860 870 880 890 900 SAGGLGHDGV GGVGVGGVIG GVAGLRLACP PDYALTLRRS PDDVPRAGAG PGTMTLIPGA 910 920 930 940 LGGGGGGAVH GFNTFGSGVG VAGVAGVATS QAGPGLPHGH STTRV

References

[1]	"Reduced social interaction and ultrasonic communication in a mouse model of monogenic heritable autism." Jamain S., Radyushkin K., Hammerschmidt K., Granon S., Boretius S., Varoqueaux F., Ramanantsoa N., Gallego J., Ronnenberg A., Winter D., Frahm J., Fischer J., Bourgeron T., Ehrenreich H., Brose N. Proc. Natl. Acad. Sci. U.S.A. 105:1710-1715(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: C57BL/6J.
[2]	"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INTERACTION WITH NRXN1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Strain: 129/Sv and BALB/c. Tissue: Brain.
[3]	"Neuroligin-4 is localized to glycinergic postsynapses and regulates inhibition in the retina." Hoon M., Soykan T., Falkenburger B., Hammer M., Patrizi A., Schmidt K.F., Sassoe-Pognetto M., Lowel S., Moser T., Taschenberger H., Brose N., Varoqueaux F. Proc. Natl. Acad. Sci. U.S.A. 108:3053-3058(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH GPHN AND ARHGEF9, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EF694290 mRNA. Translation: ABV59297.1. EF692521 mRNA. Translation: ABS19580.1. EU350930 Genomic DNA. Translation: ACA64246.1.
IPI	IPI00858277.
UniGene	Mm.468446.
3D structure databases
ProteinModelPortal	B0F2B4.
SMR	B0F2B4. Positions 28-671.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:3775191. Nlgn4l.
Phylogenomic databases
HOVERGEN	HBG008839.
Gene expression databases
Genevestigator	B0F2B4.
Family and domain databases
InterPro	IPR002018. CarbesteraseB. IPR019819. Carboxylesterase_B_CS. [Graphical view]
Pfam	PF00135. COesterase. 1 hit. [Graphical view]
PROSITE	PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

NLGN4_MOUSE

Accession

Primary (citable) accession number: B0F2B4
Secondary accession number(s): A7LAI9, B1P942

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2012
Last sequence update:	February 26, 2008
Last modified:	March 6, 2013
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program