ID   LHPL4_BOVIN             Reviewed;         247 AA.
AC   Q17R16;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=LHFPL tetraspan subfamily member 4 protein {ECO:0000250|UniProtKB:Q7Z7J7};
DE   AltName: Full=Lipoma HMGIC fusion partner-like 4 protein {ECO:0000250|UniProtKB:Q7Z7J7};
GN   Name=LHFPL4 {ECO:0000250|UniProtKB:Q7Z7J7};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the regulation of inhibitory synapse
CC       formation and function by being involved in maintening gamma-
CC       aminobutyric acid receptors (GABAARs) clustering and their associated
CC       scaffold proteins at inhibitory synaptic sites. Acts in concert with
CC       NLGN2 to recruit or stabilize GABAARs. {ECO:0000250|UniProtKB:Q5U4E0}.
CC   -!- SUBUNIT: Interacts with GABA(A) receptor subunits (By similarity).
CC       Interacts with GABRB3 (By similarity). Interacts with GABRA2 (By
CC       similarity). Interacts with GABRG2 (By similarity). Identified in a
CC       complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2
CC       and GABRB3 (By similarity). Interacts with GABRA1 (By similarity).
CC       Interacts with NLGN2; leading to mutual regulation of protein level and
CC       synaptic clustering (By similarity). {ECO:0000250|UniProtKB:Q5U4E0,
CC       ECO:0000250|UniProtKB:Q7TSY2, ECO:0000250|UniProtKB:Q7Z7J7}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q7TSY2}. Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q5U4E0}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Specifically localizes to inhibitory postsynaptic
CC       sites (By similarity). Colocalizes with GPHN, GABRG2 and NLGN2 at
CC       inhibitory postsynaptic sites (By similarity).
CC       {ECO:0000250|UniProtKB:Q5U4E0, ECO:0000250|UniProtKB:Q7TSY2}.
CC   -!- SIMILARITY: Belongs to the LHFP family. {ECO:0000305}.
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DR   EMBL; BC118076; AAI18077.1; -; mRNA.
DR   RefSeq; NP_001069694.1; NM_001076226.1.
DR   AlphaFoldDB; Q17R16; -.
DR   SMR; Q17R16; -.
DR   STRING; 9913.ENSBTAP00000044599; -.
DR   PaxDb; Q17R16; -.
DR   Ensembl; ENSBTAT00000047389; ENSBTAP00000044599; ENSBTAG00000010916.
DR   GeneID; 540541; -.
DR   KEGG; bta:540541; -.
DR   CTD; 375323; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010916; -.
DR   VGNC; VGNC:30867; LHFPL4.
DR   eggNOG; KOG4026; Eukaryota.
DR   GeneTree; ENSGT00990000203541; -.
DR   HOGENOM; CLU_084868_1_2_1; -.
DR   InParanoid; Q17R16; -.
DR   OMA; SHMYATN; -.
DR   OrthoDB; 1219117at2759; -.
DR   TreeFam; TF321143; -.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000010916; Expressed in Ammon's horn and 43 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0060077; C:inhibitory synapse; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR   GO; GO:0050811; F:GABA receptor binding; ISS:UniProtKB.
DR   GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; ISS:UniProtKB.
DR   GO; GO:1905702; P:regulation of inhibitory synapse assembly; ISS:UniProtKB.
DR   GO; GO:0007605; P:sensory perception of sound; IBA:GO_Central.
DR   InterPro; IPR019372; LHFPL.
DR   PANTHER; PTHR12489; PTHR12489; 1.
DR   Pfam; PF10242; L_HMGIC_fpl; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Membrane; Postsynaptic cell membrane;
KW   Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN           1..247
FT                   /note="LHFPL tetraspan subfamily member 4 protein"
FT                   /id="PRO_0000285960"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   247 AA;  27006 MW;  12DEB3F840B6D93D CRC64;
     MLPSQEASKL YHEHYMRNSR AIGVLWAIFT ICFAIINVVV FIQPYWVGDS VSTPKPGYFG
     LFHYCVGSGL AGRELTCRGS FTDFSTIPSG AFKAAAFFVL LSMVLILGCI TCFALFFFCN
     TATVYKICAW MQLLAALCLV LGCMIFPDGW DAETIRDMCG AKTGKYSLGD CSVRWAYILA
     IIGILNALIL SFLAFVLGNR QTDLLQEELK QENKDFVGST VSSVLRPGGD VSGWGVLPCP
     VAHTQGP