NLGNY_HUMAN
ID NLGNY_HUMAN Reviewed; 816 AA.
AC Q8NFZ3; F5H6W0; Q14D08; Q7Z3T5; Q8N5B6; Q9Y2F8;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Neuroligin-4, Y-linked;
DE Short=Neuroligin Y;
DE Flags: Precursor;
GN Name=NLGN4Y; Synonyms=KIAA0951;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12669065; DOI=10.1038/ng1136;
RA Jamain S., Quach H., Betancur C., Rastam M., Colineaux C., Gillberg I.C.,
RA Soderstrom H., Giros B., Leboyer M., Gillberg C., Bourgeron T., Nyden A.,
RA Philippe A., Cohen D., Chabane N., Mouren-Simeoni M.C., Brice A.,
RA Sponheim E., Spurkland I., Skjeldal O.H., Coleman M., Pearl P.L.,
RA Cohen I.L., Tsiouris J., Zappella M., Menchetti G., Pompella A.,
RA Aschauer H., Van Maldergem L.;
RT "Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are
RT associated with autism.";
RL Nat. Genet. 34:27-29(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=12815422; DOI=10.1038/nature01722;
RA Skaletsky H., Kuroda-Kawaguchi T., Minx P.J., Cordum H.S., Hillier L.W.,
RA Brown L.G., Repping S., Pyntikova T., Ali J., Bieri T., Chinwalla A.,
RA Delehaunty A., Delehaunty K., Du H., Fewell G., Fulton L., Fulton R.,
RA Graves T.A., Hou S.-F., Latrielle P., Leonard S., Mardis E., Maupin R.,
RA McPherson J., Miner T., Nash W., Nguyen C., Ozersky P., Pepin K., Rock S.,
RA Rohlfing T., Scott K., Schultz B., Strong C., Tin-Wollam A., Yang S.-P.,
RA Waterston R.H., Wilson R.K., Rozen S., Page D.C.;
RT "The male-specific region of the human Y chromosome is a mosaic of discrete
RT sequence classes.";
RL Nature 423:825-837(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Putative neuronal cell surface protein involved in cell-cell-
CC interactions.
CC -!- SUBUNIT: Homodimer. Interacts with NRXN1 in a calcium-dependent manner.
CC Interacts through its C-terminus with DLG4/PSD-95 third PDZ domain (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Postsynaptic density membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8NFZ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NFZ3-2; Sequence=VSP_007537;
CC Name=3;
CC IsoId=Q8NFZ3-3; Sequence=VSP_044852, VSP_044853, VSP_044854,
CC VSP_044855;
CC Name=4;
CC IsoId=Q8NFZ3-4; Sequence=VSP_044853, VSP_044854, VSP_044855;
CC -!- TISSUE SPECIFICITY: Expressed in fetal and adult brain, prostate and
CC testis. {ECO:0000269|PubMed:12815422}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76795.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF376804; AAM46113.1; -; mRNA.
DR EMBL; AB023168; BAA76795.2; ALT_INIT; mRNA.
DR EMBL; BX537428; CAD97670.1; -; mRNA.
DR EMBL; AC010726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032567; AAH32567.1; -; mRNA.
DR EMBL; BC113525; AAI13526.1; -; mRNA.
DR EMBL; BC113551; AAI13552.1; -; mRNA.
DR CCDS; CCDS14788.1; -. [Q8NFZ3-1]
DR CCDS; CCDS56619.1; -. [Q8NFZ3-2]
DR RefSeq; NP_001157710.1; NM_001164238.1. [Q8NFZ3-4]
DR RefSeq; NP_001193779.1; NM_001206850.1. [Q8NFZ3-2]
DR RefSeq; NP_055708.3; NM_014893.4. [Q8NFZ3-1]
DR RefSeq; XP_016885523.1; XM_017030034.1.
DR RefSeq; XP_016885524.1; XM_017030035.1.
DR RefSeq; XP_016885525.1; XM_017030036.1. [Q8NFZ3-1]
DR RefSeq; XP_016885526.1; XM_017030037.1.
DR RefSeq; XP_016885527.1; XM_017030038.1.
DR RefSeq; XP_016885529.1; XM_017030040.1. [Q8NFZ3-2]
DR RefSeq; XP_016885530.1; XM_017030041.1. [Q8NFZ3-4]
DR AlphaFoldDB; Q8NFZ3; -.
DR SMR; Q8NFZ3; -.
DR BioGRID; 116504; 5.
DR ESTHER; human-NLGN4Y; Neuroligin.
DR MEROPS; S09.989; -.
DR GlyGen; Q8NFZ3; 2 sites.
DR iPTMnet; Q8NFZ3; -.
DR PhosphoSitePlus; Q8NFZ3; -.
DR BioMuta; NLGN4Y; -.
DR DMDM; 31076823; -.
DR EPD; Q8NFZ3; -.
DR jPOST; Q8NFZ3; -.
DR MassIVE; Q8NFZ3; -.
DR PaxDb; Q8NFZ3; -.
DR PeptideAtlas; Q8NFZ3; -.
DR PRIDE; Q8NFZ3; -.
DR ProteomicsDB; 27307; -.
DR ProteomicsDB; 73395; -. [Q8NFZ3-1]
DR ProteomicsDB; 73396; -. [Q8NFZ3-2]
DR Antibodypedia; 21872; 151 antibodies from 27 providers.
DR DNASU; 22829; -.
DR Ensembl; ENST00000339174.9; ENSP00000342535.5; ENSG00000165246.15. [Q8NFZ3-1]
DR Ensembl; ENST00000355905.6; ENSP00000348169.2; ENSG00000165246.15. [Q8NFZ3-1]
DR Ensembl; ENST00000382872.5; ENSP00000372325.1; ENSG00000165246.15. [Q8NFZ3-2]
DR GeneID; 22829; -.
DR KEGG; hsa:22829; -.
DR UCSC; uc004fte.3; human. [Q8NFZ3-1]
DR CTD; 22829; -.
DR DisGeNET; 22829; -.
DR GeneCards; NLGN4Y; -.
DR HGNC; HGNC:15529; NLGN4Y.
DR HPA; ENSG00000165246; Tissue enhanced (brain).
DR MIM; 400028; gene.
DR neXtProt; NX_Q8NFZ3; -.
DR OpenTargets; ENSG00000165246; -.
DR PharmGKB; PA38386; -.
DR VEuPathDB; HostDB:ENSG00000165246; -.
DR GeneTree; ENSGT00940000156607; -.
DR HOGENOM; CLU_006586_5_1_1; -.
DR InParanoid; Q8NFZ3; -.
DR PhylomeDB; Q8NFZ3; -.
DR TreeFam; TF326187; -.
DR PathwayCommons; Q8NFZ3; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SIGNOR; Q8NFZ3; -.
DR BioGRID-ORCS; 22829; 6 hits in 635 CRISPR screens.
DR ChiTaRS; NLGN4Y; human.
DR GenomeRNAi; 22829; -.
DR Pharos; Q8NFZ3; Tbio.
DR PRO; PR:Q8NFZ3; -.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; Q8NFZ3; protein.
DR Bgee; ENSG00000165246; Expressed in prefrontal cortex and 119 other tissues.
DR ExpressionAtlas; Q8NFZ3; baseline and differential.
DR Genevisible; Q8NFZ3; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098985; C:asymmetric, glutamatergic, excitatory synapse; TAS:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0089717; C:spanning component of membrane; TAS:ARUK-UCL.
DR GO; GO:0098983; C:symmetric, GABA-ergic, inhibitory synapse; TAS:ARUK-UCL.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; TAS:BHF-UCL.
DR GO; GO:0042043; F:neurexin family protein binding; IBA:GO_Central.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007612; P:learning; IMP:BHF-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IBA:GO_Central.
DR GO; GO:0099054; P:presynapse assembly; TAS:ARUK-UCL.
DR GO; GO:0097105; P:presynaptic membrane assembly; IBA:GO_Central.
DR GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
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 InterPro; IPR000460; Nlgn.
DR InterPro; IPR030025; NLGN4.
DR PANTHER; PTHR43903:SF5; PTHR43903:SF5; 2.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR01090; NEUROLIGIN.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..816
FT /note="Neuroligin-4, Y-linked"
FT /id="PRO_0000008649"
FT TOPO_DOM 44..676
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..697
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..816
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 359..364
FT /note="Interaction with NRXN1"
FT /evidence="ECO:0000250"
FT REGION 636..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62889"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..146
FT /evidence="ECO:0000250"
FT DISULFID 306..317
FT /evidence="ECO:0000250"
FT DISULFID 476..510
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..168
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_007537"
FT VAR_SEQ 1..122
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044852"
FT VAR_SEQ 157
FT /note="D -> DGTNIKRNADDITSNDHGEDK (in isoform 3 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000305"
FT /id="VSP_044853"
FT VAR_SEQ 210..236
FT /note="FLSTGDQAAKGNYGLLDQIQALRWIEE -> MQEARLCGSSKMFNYFKSPFT
FT NLINFF (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000305"
FT /id="VSP_044854"
FT VAR_SEQ 237..816
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000305"
FT /id="VSP_044855"
FT CONFLICT 203
FT /note="Y -> C (in Ref. 3; CAD97670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 816 AA; 92021 MW; FB68910773B1BBF6 CRC64;
MLRPQGLLWL PLLFTSVCVM LNSNVLLWIT ALAIKFTLID SQAQYPVVNT NYGKIQGLRT
PLPSEILGPV EQYLGVPYAS PPTGERRFQP PESPSSWTGI RNATQFSAVC PQHLDERFLL
HDMLPIWFTT SLDTLMTYVQ DQNEDCLYLN IYVPMEDDIH EQNSKKPVMV YIHGGSYMEG
TGNMIDGSIL ASYGNVIVIT INYRLGILGF LSTGDQAAKG NYGLLDQIQA LRWIEENVGA
FGGDPKRVTI FGSGAGASCV SLLTLSHYSE GLFQKAIIQS GTALSSWAVN YQPAKYTRIL
ADKVGCNMLD TTDMVECLKN KNYKELIQQT ITPATYHIAF GPVIDGDVIP DDPQILMEQG
EFLNYDIMLG VNQGEGLKFV DGIVDNEDGV TPNDFDFSVS NFVDNLYGYP EGKDTLRETI
KFMYTDWADK ENPETRRKTL VALFTDHQWV APAVATADLH AQYGSPTYFY AFYHHCQSEM
KPSWADSAHG DEVPYVFGIP MIGPTELFSC NFSKNDVMLS AVVMTYWTNF AKTGDPNQPV
PQDTKFIHTK PNRFEEVAWS KYNPKDQLYL HIGLKPRVRD HYRATKVAFW LELVPHLHNL
NEIFQYVSTT TKVPPPDMTS FPYGTRRSPA KIWPTTKRPA ITPANNPKHS KDPHKTGPED
TTVLIETKRD YSTELSVTIA VGASLLFLNI LAFAALYYKK DKRRHETHRH PSPQRNTTND
ITHIQNEEIM SLQMKQLEHD HECESLQAHD TLRLTCPPDY TLTLRRSPDD IPFMTPNTIT
MIPNTLMGMQ PLHTFKTFSG GQNSTNLPHG HSTTRV
