LRRC4_RAT
ID LRRC4_RAT Reviewed; 652 AA.
AC Q45R42;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Leucine-rich repeat-containing protein 4;
DE AltName: Full=Netrin-G2 ligand;
DE Short=NGL-2;
DE Flags: Precursor;
GN Name=Lrrc4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA He H., Wei X., Minghua W., Dan L., Xaiomin L., Guiyuan L.;
RT "Cloning and expression of LRRC4 in wistar rat.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=16980967; DOI=10.1038/nn1763;
RA Kim S., Burette A., Chung H.S., Kwon S.-K., Woo J., Lee H.W., Kim K.,
RA Kim H., Weinberg R.J., Kim E.;
RT "NGL family PSD-95-interacting adhesion molecules regulate excitatory
RT synapse formation.";
RL Nat. Neurosci. 9:1294-1301(2006).
CC -!- FUNCTION: Synaptic adhesion protein. Regulates the formation of
CC exitatory synapses through the recruitment of pre-and-postsynaptic
CC proteins. Organize the lamina/pathway-specific differentiation of
CC dendrites. Plays an important role for auditory synaptic responses.
CC Involved in the suppression of glioma.
CC -!- SUBUNIT: Interacts (via LRR repeats) with NTNG2. Interacts with DLG4.
CC Found in a complex with NMDA receptors. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16980967}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16980967}.
CC Postsynaptic cell membrane {ECO:0000269|PubMed:16980967}. Note=LRRC4
CC and DLG4 are interdependent for synaptic localization. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the brain. Expression is
CC concentrated in the olfactory bulb, cortex, hippocampus and cerebellum
CC in adult brain. Detected both embryonically and postnatally with
CC stronger expression in postnatal stages. {ECO:0000269|PubMed:16980967}.
CC -!- DOMAIN: The last 4 C-terminal residues binds to the first 2 PDZ domains
CC of DLG4. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16980967}.
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DR EMBL; DQ119102; AAZ23788.1; -; mRNA.
DR RefSeq; NP_001032413.1; NM_001037336.1.
DR AlphaFoldDB; Q45R42; -.
DR SMR; Q45R42; -.
DR BioGRID; 566016; 3.
DR STRING; 10116.ENSRNOP00000010673; -.
DR GlyGen; Q45R42; 2 sites.
DR iPTMnet; Q45R42; -.
DR PhosphoSitePlus; Q45R42; -.
DR PaxDb; Q45R42; -.
DR PRIDE; Q45R42; -.
DR Ensembl; ENSRNOT00000010673; ENSRNOP00000010673; ENSRNOG00000008098.
DR GeneID; 641521; -.
DR KEGG; rno:641521; -.
DR UCSC; RGD:1560026; rat.
DR CTD; 64101; -.
DR RGD; 1560026; Lrrc4.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000159260; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q45R42; -.
DR OMA; QVWILCV; -.
DR OrthoDB; 282791at2759; -.
DR PhylomeDB; Q45R42; -.
DR TreeFam; TF324303; -.
DR PRO; PR:Q45R42; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000008098; Expressed in frontal cortex and 10 other tissues.
DR Genevisible; Q45R42; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0060076; C:excitatory synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0044309; C:neuron spine; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:1904861; P:excitatory synapse assembly; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR026882; Lrrc4.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR24369:SF9; PTHR24369:SF9; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..652
FT /note="Leucine-rich repeat-containing protein 4"
FT /id="PRO_0000390393"
FT TOPO_DOM 1..526
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..74
FT /note="LRRNT"
FT REPEAT 75..96
FT /note="LRR 1"
FT REPEAT 99..120
FT /note="LRR 2"
FT REPEAT 123..144
FT /note="LRR 3"
FT REPEAT 147..168
FT /note="LRR 4"
FT REPEAT 171..193
FT /note="LRR 5"
FT REPEAT 196..217
FT /note="LRR 6"
FT REPEAT 218..239
FT /note="LRR 7"
FT REPEAT 242..263
FT /note="LRR 8"
FT REPEAT 266..287
FT /note="LRR 9"
FT DOMAIN 299..351
FT /note="LRRCT"
FT DOMAIN 352..441
FT /note="Ig-like C2-type"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 49..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 303..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 305..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 373..423
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 652 AA; 72609 MW; B604B6FCAD285AF7 CRC64;
MKLLWQVTVH HTWNAVLLPV VYLTAQVWIL CAAIAAAASA GPQNCPSVCS CSNQFSKVVC
TRRGLSEVPQ GIPSNTRYLN LMENNIQMIQ ADTFRHLHHL EVLQLGRNAI RQIEVGAFNG
LASLNTLELF DNWLTVIPSG AFEYLSKLRE LWLRNNPIES IPSYAFNRVP SLMRLDLGEL
KKLEYISEGA FEGLFNLKYL NLGMCNIKDM PNLTPLVGLE ELEMSGNHFP EIRPGSFHGL
SSLKKLWVMN SQVSLIERNA FDGLASLVEL NLAHNNLSSL PHDLFTPLRY LVELHLHHNP
WNCDCDILWL AWWLREYIPT NSTCCGRCHA PMHMRGRYLV EVDQASFQCS APFIMDAPRD
LNISEDRMAE LKCRTPPMSS VKWLLPNGTV LSHASRHPRI SVLNDGTLNF SRVLLIDTGV
YTCMVTNVAG NSNASAYLNV SSAELNTPNF SFFTTVTVET TEISPEDITR KYKPVPTTST
GYQPAYTTST TVLIQTTRVP KQVPVPSTDT TDKMQTSLDE VMKTTKIIIG CFVAVTLLAA
AMLIVFYKLR KRHQQRSTVT AARTVEIIQV DEDIPAAASA AATAAPSGVS GEGAVVLPTI
HDHINYNTYK PAHGAHWTEN SLGNSLHPTV TTISEPYIIQ THTKDKVQET QI
