NLGN4_MOUSE
ID NLGN4_MOUSE Reviewed; 945 AA.
AC B0F2B4; A7LAI9; B1P942;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Neuroligin 4-like;
DE AltName: Full=Neuroligin-4;
DE Short=NL-4;
DE Flags: Precursor;
GN Name=Nlgn4l; Synonyms=Nl4*, Nlgn4, Nlgn4x;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=18227507; DOI=10.1073/pnas.0711555105;
RA Jamain S., Radyushkin K., Hammerschmidt K., Granon S., Boretius S.,
RA Varoqueaux F., Ramanantsoa N., Gallego J., Ronnenberg A., Winter D.,
RA Frahm J., Fischer J., Bourgeron T., Ehrenreich H., Brose N.;
RT "Reduced social interaction and ultrasonic communication in a mouse model
RT of monogenic heritable autism.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:1710-1715(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INTERACTION WITH NRXN1,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=129/Sv, and BALB/cJ; TISSUE=Brain;
RX PubMed=18434543; DOI=10.1073/pnas.0801383105;
RA Bolliger M.F., Pei J., Maxeiner S., Boucard A.A., Grishin N.V.,
RA Sudhof T.C.;
RT "Unusually rapid evolution of neuroligin-4 in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6421-6426(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH GPHN
RP AND ARHGEF9, AND TISSUE SPECIFICITY.
RX PubMed=21282647; DOI=10.1073/pnas.1006946108;
RA Hoon M., Soykan T., Falkenburger B., Hammer M., Patrizi A., Schmidt K.F.,
RA Sassoe-Pognetto M., Lowel S., Moser T., Taschenberger H., Brose N.,
RA Varoqueaux F.;
RT "Neuroligin-4 is localized to glycinergic postsynapses and regulates
RT inhibition in the retina.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3053-3058(2011).
CC -!- FUNCTION: Cell surface protein involved in cell-cell-interactions.
CC Plays a role in the formation or maintenance of synaptic junctions via
CC its interactions (via the extracellular domains) with neurexin family
CC members. Plays a role in synaptic signal transmission.
CC {ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:21282647}.
CC -!- SUBUNIT: Homodimer. Interacts with NRXN1. Interacts with GPHN and
CC ARHGEF9. {ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:21282647}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Postsynaptic cell membrane. Note=Detected at glycinergic
CC postsynapses in retina. Detected on dendritic spines on cultured
CC neurons.
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, septum, hippocampus,
CC striatum, olfactory bulb, retina, colliculi, brain stem, cerebellum,
CC thymus and skeletal muscle. Detected at inhibitory synapses throughout
CC the brain and spinal cord (at protein level). Detected in brain,
CC spleen, lung, skeletal muscle and kidney. {ECO:0000269|PubMed:18227507,
CC ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:21282647}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile with no obvious
CC sensory deficits or major perturbations of behavior, but show subtle
CC changes in synaptic signal transmission and signal processing. Mice
CC display subtle deficits in reciprocal social interactions and
CC communication. They have reduced brain volume.
CC {ECO:0000269|PubMed:18227507, ECO:0000269|PubMed:21282647}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; EF694290; ABV59297.1; -; mRNA.
DR EMBL; EF692521; ABS19580.1; -; mRNA.
DR EMBL; EU350930; ACA64246.1; -; Genomic_DNA.
DR AlphaFoldDB; B0F2B4; -.
DR SMR; B0F2B4; -.
DR IntAct; B0F2B4; 1.
DR ESTHER; mouse-4neur; Neuroligin.
DR MEROPS; S09.994; -.
DR SwissPalm; B0F2B4; -.
DR MaxQB; B0F2B4; -.
DR PeptideAtlas; B0F2B4; -.
DR PRIDE; B0F2B4; -.
DR ProteomicsDB; 293857; -.
DR ABCD; B0F2B4; 2 sequenced antibodies.
DR MGI; MGI:3775191; Nlgn4l.
DR InParanoid; B0F2B4; -.
DR PRO; PR:B0F2B4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; B0F2B4; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; ISS:BHF-UCL.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; IC:BHF-UCL.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IDA:BHF-UCL.
DR GO; GO:0031404; F:chloride ion binding; ISO:MGI.
DR GO; GO:0042043; F:neurexin family protein binding; ISS:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0003360; P:brainstem development; IMP:BHF-UCL.
DR GO; GO:0021549; P:cerebellum development; IMP:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0008049; P:male courtship behavior; IMP:BHF-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0035265; P:organ growth; IMP:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IBA:GO_Central.
DR GO; GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0002124; P:territorial aggressive behavior; IMP:BHF-UCL.
DR GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Membrane; Postsynaptic cell membrane;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..945
FT /note="Neuroligin 4-like"
FT /id="PRO_0000417951"
FT TOPO_DOM 19..761
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 762..782
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 783..945
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 145..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 93..129
FT /evidence="ECO:0000250"
FT DISULFID 315..338
FT /evidence="ECO:0000250"
FT DISULFID 527..583
FT /evidence="ECO:0000250"
FT CONFLICT 5
FT /note="V -> A (in Ref. 2; ABS19580/ACA64246)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="C -> R (in Ref. 2; ABS19580/ACA64246)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="T -> P (in Ref. 2; ACA64246)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="H -> P (in Ref. 2; ACA64246)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="H -> P (in Ref. 2; ABS19580/ACA64246)"
FT /evidence="ECO:0000305"
FT CONFLICT 893
FT /note="T -> A (in Ref. 2; ABS19580/ACA64246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 945 AA; 97348 MW; 03DFC91F1350ED6A CRC64;
MPAPVPALLC LALALASAQP SPPPPPPFPV VATNYGKLRG VRAALPGDVL GPVTQFLGVP
YAAPPTGERR FQPPEPPSSW AGVRDATRFA PVCPQHLDER ALLRDCLPAW FAANLDAIAA
YVQDQSEDCL YLNLYVPGGA NGKKMADDVT GNDHGDDQDS RDPGVGGAAA AAARKPVMVY
IHGGSYMEGT ANIVDGSVLA SYGDVIVVTV NYRLGVLGFL STGDQAAKGN YGLLDQIQAL
RWVEENAGAF GGDPDRVTVF GSGAGASCVS LLTLSHYSEG LFQKAIIQSG TALSSWAVNY
QPARYARALG ERVGCATPDP GSPPGSPPGW DSASLVSCLR GKAAGELARA RVTPATYHVA
FGPTVDGDVI PDDPQILMEQ GEFLNYDIML GVNQGEGARF VDGLGGGHDG GYGGYGGGYG
GGVEDDEVQD GGPDGAAGGV SAGEFDLAVS GFINDLYGRP EGRGDALRET VKFMYTDWAD
RDSPEARRKT LVALFTDHQW VAPAVATADL HARYGSPTYF YAFYHRCHGG GGGGGGVDGV
AGGVAGGVGG EEARPAWADA AHGDEVPYVF GVHMAGPGDV FGCNFSRNDV MLSAVVMTYW
TNFAKTGDPN QPVAQDTRFV HTRPNRFEEV AWAKYDPRGQ LYLHIGLRPR VRDHYRAAKV
AFWLELVPHL HGLAADPGAY LSAAATRAAP SGDPDRDPGG GGGGRRRPRP ATRRPAVMTS
SSMASGSGMT SSSGSGMTSS SGSSASAVLI ETRRDYSTEL SVTIAVGASL LFLNVLAFAA
LYYKKDKRRH ETHRRPPPPR PPQAPPSAAA ADRNPRPDPG PAGRRGGECG AVVTAMAAEA
SAGGLGHDGV GGVGVGGVIG GVAGLRLACP PDYALTLRRS PDDVPRAGAG PGTMTLIPGA
LGGGGGGAVH GFNTFGSGVG VAGVAGVATS QAGPGLPHGH STTRV
