ID   NLGNX_MACMU             Reviewed;         213 AA.
AC   Q8WMG7;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Neuroligin-4, X-linked;
DE   Flags: Fragment;
GN   Name=NLGN4X; Synonyms=NLGN4;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hypothalamus;
RA   Mungenast A.E., Ojeda S.R.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative neuronal cell surface protein involved in cell-cell-
CC       interactions. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AF462606; AAL66382.1; -; mRNA.
DR   AlphaFoldDB; Q8WMG7; -.
DR   SMR; Q8WMG7; -.
DR   STRING; 9544.ENSMMUP00000014838; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   HOGENOM; CLU_006586_5_1_1; -.
DR   InParanoid; Q8WMG7; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042043; F:neurexin family protein binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0050808; P:synapse organization; IEA:InterPro.
DR   InterPro; IPR030025; NLGN4.
DR   PANTHER; PTHR43903:SF5; PTHR43903:SF5; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Reference proteome; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..213
FT                   /note="Neuroligin-4, X-linked"
FT                   /id="PRO_0000070299"
FT   TOPO_DOM        <1..73
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62889"
FT   NON_TER         1
SQ   SEQUENCE   213 AA;  24096 MW;  0AF21610035C660B CRC64;
     FQYVSTTTKV PPPDMTSFPY GTRRSPAKIW PTTKRPAITP ANNPKHSKDP HKTGPEDTTV
     LIETKRDYST ELSVTIAVGA SLLFLNILAF AALYYKKDKR RHETHRRPSP QRNTTNDIAH
     IQNEEIMSLQ MKQLEHDHEC ESLQAHDTLR LTCPPDYTLT LRRSPDDIPL MTPNTITMIP
     NTLTGMQPLH TFNTFSGGQN STNLPHGHST TRV