LRC4B_RAT
ID LRC4B_RAT Reviewed; 709 AA.
AC P0CC10;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Leucine-rich repeat-containing protein 4B;
DE AltName: Full=Netrin-G3 ligand;
DE Short=NGL-3;
DE Flags: Precursor;
GN Name=Lrrc4b; Synonyms=Lrig4;
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 [LARGE SCALE MRNA] OF 1-189.
RG Amgen EST program;
RT "Amgen rat EST program.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY, 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).
RN [3]
RP FUNCTION, INTERACTION WITH PTPRF, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=19252495; DOI=10.1038/nn.2279;
RA Woo J., Kwon S.K., Choi S., Kim S., Lee J.-R., Dunah A.W., Sheng M.,
RA Kim E.;
RT "Trans-synaptic adhesion between NGL-3 and LAR regulates the formation of
RT excitatory synapses.";
RL Nat. Neurosci. 12:428-437(2009).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-402, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Synaptic adhesion protein. Regulates the formation of
CC excitatory synapses. The trans-synaptic adhesion between LRRC4B and
CC PTPRF regulates the formation of excitatory synapses in a bidirectional
CC manner. {ECO:0000269|PubMed:19252495}.
CC -!- SUBUNIT: Interacts with PTPRF. Interacts with DLG4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19252495}; Single-
CC pass membrane protein {ECO:0000269|PubMed:19252495}. Presynaptic cell
CC membrane {ECO:0000269|PubMed:19252495}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the brain. Widespread
CC distribution in various brain regions (at protein level). Detected both
CC embryonically and postnatally with stronger expression in postnatal
CC stages. {ECO:0000269|PubMed:16980967}.
CC -!- DOMAIN: The extreme C-terminus binds to the first 2 PDZ domains of
CC DLG4. {ECO:0000250}.
CC -!- PTM: N-glycosylated. O-glycosylated; contains sialic acid.
CC {ECO:0000269|PubMed:16980967, ECO:0000269|PubMed:19252495}.
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DR EMBL; CB608563; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001258010.1; NM_001271081.1.
DR RefSeq; XP_006229117.1; XM_006229055.2.
DR AlphaFoldDB; P0CC10; -.
DR SMR; P0CC10; -.
DR BioGRID; 259067; 1.
DR STRING; 10116.ENSRNOP00000026259; -.
DR GlyGen; P0CC10; 5 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P0CC10; -.
DR PaxDb; P0CC10; -.
DR PRIDE; P0CC10; -.
DR ABCD; P0CC10; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000026259; ENSRNOP00000026259; ENSRNOG00000019418.
DR GeneID; 308571; -.
DR KEGG; rno:308571; -.
DR UCSC; RGD:1307121; rat.
DR CTD; 94030; -.
DR RGD; 1307121; Lrrc4b.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160261; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; P0CC10; -.
DR OMA; TSCPEAC; -.
DR OrthoDB; 282791at2759; -.
DR PhylomeDB; P0CC10; -.
DR TreeFam; TF324303; -.
DR Reactome; R-RNO-388844; Receptor-type tyrosine-protein phosphatases.
DR PRO; PR:P0CC10; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019418; Expressed in frontal cortex and 12 other tissues.
DR Genevisible; P0CC10; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044300; C:cerebellar mossy fiber; 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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
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; IPR026883; LRRC4B.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR24369:SF102; PTHR24369:SF102; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13855; LRR_8; 4.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 8.
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; Cell projection; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..709
FT /note="Leucine-rich repeat-containing protein 4B"
FT /id="PRO_0000390416"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 50..88
FT /note="LRRNT"
FT REPEAT 89..110
FT /note="LRR 1"
FT REPEAT 113..134
FT /note="LRR 2"
FT REPEAT 137..158
FT /note="LRR 3"
FT REPEAT 161..182
FT /note="LRR 4"
FT REPEAT 185..207
FT /note="LRR 5"
FT REPEAT 210..231
FT /note="LRR 6"
FT REPEAT 232..253
FT /note="LRR 7"
FT REPEAT 256..277
FT /note="LRR 8"
FT REPEAT 280..301
FT /note="LRR 9"
FT DOMAIN 313..365
FT /note="LRRCT"
FT DOMAIN 366..454
FT /note="Ig-like C2-type"
FT REGION 496..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C192"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 387..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 709 AA; 76119 MW; BB59CD872BD409BD CRC64;
MAQAHIQGSP CPLLPPGRMS WPQGALLLLW LFSPPLRAGG GGVAVTSAAG GGSPPATSCP
AACSCSNQAS RVICTRRELA EVPASIPVNT RYLNLQENSI QVIRTDTFKH LRHLEILQLS
KNLVRKIEVG AFNGLPSLNT LELFDNRLTT VPTQAFEYLS KLRELWLRNN PIESIPSYAF
NRVPSLRRLD LGELKRLEYI SEAAFEGLVN LRYLNLGMCN LKDIPNLTAL VRLEELELSG
NRLDLIRPGS FQGLTSLRKL WLMHAQVATI ERNAFDDLKS LEELNLSHNN LMSLPHDLFT
PLHRLERVHL NHNPWHCNCD VLWLSWWLKE TVPSNTTCCA RCHAPAGLKG RYIGELDQSH
FTCYAPVIVE PPTDLNVTEG MAAELKCRTG TSMTSVNWLT PNGTLMTHGS YRVRISVLHD
GTLNFTNVTV QDTGQYTCMV TNSAGNTTAS ATLNVSAVDP VAAGGPGGGG PGGGGGAGGA
GGYTYFTTVT VETLETQPGE EAQQPRGTEK EPPGPTTDGA WGGGRPDAAA PASASTTAPA
PRSSRPTEKA FTVPITDVTE NALKDLDDVM KTTKIIIGCF VAITFMAAVM LVAFYKLRKQ
HQLHKHHGPT RTVEIINVED ELPAASAVSV AAAAAVAGGA GVGGDSHLAL PALERDHLNH
HHYVAAAFKA HYGGNPGGGC GAKGPGLNSI HEPLLFKSGS KENVQETQI
