ID   A2AGI2_MOUSE            Unreviewed;       845 AA.
AC   A2AGI2;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 136.
DE   SubName: Full=Neuroligin 3 {ECO:0000313|Ensembl:ENSMUSP00000123283.2};
GN   Name=Nlgn3 {ECO:0000313|Ensembl:ENSMUSP00000123283.2,
GN   ECO:0000313|MGI:MGI:2444609};
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 {ECO:0000313|Ensembl:ENSMUSP00000123283.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:18034455}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000123283.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000123283.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RG   Mouse Genome Sequencing Consortium;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] {ECO:0000313|Ensembl:ENSMUSP00000123283.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000123283.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=21750661;
RA   Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N.,
RA   Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D.,
RA   Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L.,
RA   Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J.,
RA   Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P.,
RA   Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G.,
RA   Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.;
RT   "Modernizing reference genome assemblies.";
RL   PLoS Biol. 9:e1001091-e1001091(2011).
RN   [5] {ECO:0000313|Ensembl:ENSMUSP00000123283.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000123283.2};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Synapse
CC       {ECO:0000256|ARBA:ARBA00034103}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000256|ARBA:ARBA00005964}.
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DR   AlphaFoldDB; A2AGI2; -.
DR   SMR; A2AGI2; -.
DR   IntAct; A2AGI2; 1.
DR   ESTHER; mouse-3neur; Neuroligin.
DR   SwissPalm; A2AGI2; -.
DR   PeptideAtlas; A2AGI2; -.
DR   ProteomicsDB; 326987; -.
DR   Antibodypedia; 561; 299 antibodies from 37 providers.
DR   Ensembl; ENSMUST00000151528.8; ENSMUSP00000123283.2; ENSMUSG00000031302.17.
DR   UCSC; uc009txi.2; mouse.
DR   AGR; MGI:2444609; -.
DR   MGI; MGI:2444609; Nlgn3.
DR   VEuPathDB; HostDB:ENSMUSG00000031302; -.
DR   GeneTree; ENSGT00940000159580; -.
DR   OMA; MNCTIPE; -.
DR   OrthoDB; 6846267at2759; -.
DR   PhylomeDB; A2AGI2; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   Bgee; ENSMUSG00000031302; Expressed in dentate gyrus of hippocampal formation granule cell and 116 other cell types or tissues.
DR   ExpressionAtlas; A2AGI2; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042043; F:neurexin family protein binding; IEA:InterPro.
DR   GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR   GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR   GO; GO:0007612; P:learning; IEA:Ensembl.
DR   GO; GO:0071709; P:membrane assembly; IEA:UniProtKB-ARBA.
DR   GO; GO:0051240; P:positive regulation of multicellular organismal process; IEA:UniProtKB-ARBA.
DR   GO; GO:0042391; P:regulation of membrane potential; IEA:UniProtKB-ARBA.
DR   GO; GO:0031644; P:regulation of nervous system process; IEA:UniProtKB-ARBA.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:UniProtKB-ARBA.
DR   GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR   GO; GO:0007416; P:synapse assembly; IEA:UniProtKB-ARBA.
DR   GO; GO:0071625; P:vocalization behavior; IEA:Ensembl.
DR   FunFam; 3.40.50.1820:FF:000001; Neuroligin 3 isoform; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR051093; Neuroligin/BSAL.
DR   InterPro; IPR000460; Nlgn.
DR   PANTHER; PTHR43903; NEUROLIGIN; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR01090; NEUROLIGIN.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A2AGI2,
KW   ECO:0007829|ProteomicsDB:A2AGI2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..845
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002641897"
FT   TRANSMEM        705..728
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          38..621
FT                   /note="Carboxylesterase type B"
FT                   /evidence="ECO:0000259|Pfam:PF00135"
FT   REGION          166..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..191
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  93487 MW;  422AB9C7C945DA77 CRC64;
     MWLQPSLSLS PTPTVGRSLC LTLGFLSLVL RASTQAPAPT VNTHFGKLRG ARVPLPSEIL
     GPVDQYLGVP YAAPPIGEKR FLPPEPPPSW SGIRNATHFP PVCPQNIHTA VPEVMLPVWF
     TANLDIVATY IQEPNEDCLY LNVYVPTEDV KRISKECARK PNKKICRKGG SGAKKQGEDL
     ADNDGDEDED IRDSGAKPVM VYIHGGSYME GTGNMIDGSV LASYGNVIVI TLNYRVGVLG
     FLSTGDQAAK GNYGLLDQIQ ALRWVSENIA FFGGDPRRIT VFGSGIGASC VSLLTLSHHS
     EGLFQRAIIQ SGSALSSWAV NYQPVKYTSL LADKVGCNVL DTVDMVDCLR QKSAKELVEQ
     DIQPARYHVA FGPVIDGDVI PDDPEILMEQ GEFLNYDIML GVNQGEGLKF VEGVVDPEDG
     VSGTDFDYSV SNFVDNLYGY PEGKDTLRET IKFMYTDWAD RDNPETRRKT LVALFTDHQW
     VEPSVVTADL HARYGSPTYF YAFYHHCQSL MKPAWSDAAH GDEVPYVFGV PMVGPTDLFP
     CNFSKNDVML SAVVMTYWTN FAKTGDPNKP VPQDTKFIHT KANRFEEVAW SKYNPRDQLY
     LHIGLKPRVR DHYRATKVAF WKHLVPHLYN LHDMFHYTST TTKVPPPDTT HSSHITRRPN
     GKTWSTKRPA ISPAYSNENA PGSWNGDQDA GPLLVENPRD YSTELSVTIA VGASLLFLNV
     LAFAALYYRK DKRRQEPLRQ PSPQRGTGAP ELGTAPEEEL AALQLGPTHH ECEAGPPHDT
     LRLTALPDYT LTLRRSPDDI PLMTPNTITM IPNSLVGLQT LHPYNTFAAG FNSTGLPHSH
     STTRV
//