LRC4B_HUMAN
ID LRC4B_HUMAN Reviewed; 713 AA.
AC Q9NT99; Q3ZCQ4; Q58F20;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 161.
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 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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-713.
RC TISSUE=Brain;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 216-636.
RC TISSUE=Amygdala;
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTPRF. Interacts with DLG4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC Presynaptic cell membrane {ECO:0000250}.
CC -!- DOMAIN: The last 4 C-terminal residues bind to the first 2 PDZ domains
CC of DLG4. {ECO:0000250}.
CC -!- PTM: N-glycosylated. O-glycosylated; contains sialic acid.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19687.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC008743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019687; AAH19687.1; ALT_INIT; mRNA.
DR EMBL; BC056207; AAH56207.1; -; mRNA.
DR EMBL; AL137451; CAB70743.2; -; mRNA.
DR CCDS; CCDS42595.1; -.
DR PIR; T46266; T46266.
DR RefSeq; NP_001073926.1; NM_001080457.1.
DR RefSeq; NP_001335497.1; NM_001348568.1.
DR RefSeq; XP_005259486.1; XM_005259429.4.
DR RefSeq; XP_006723569.1; XM_006723506.3.
DR RefSeq; XP_011525822.1; XM_011527520.2.
DR AlphaFoldDB; Q9NT99; -.
DR SMR; Q9NT99; -.
DR BioGRID; 125098; 11.
DR IntAct; Q9NT99; 4.
DR STRING; 9606.ENSP00000471502; -.
DR TCDB; 8.A.43.1.24; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR GlyGen; Q9NT99; 10 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NT99; -.
DR PhosphoSitePlus; Q9NT99; -.
DR BioMuta; LRRC4B; -.
DR DMDM; 91207142; -.
DR EPD; Q9NT99; -.
DR MassIVE; Q9NT99; -.
DR MaxQB; Q9NT99; -.
DR PaxDb; Q9NT99; -.
DR PeptideAtlas; Q9NT99; -.
DR PRIDE; Q9NT99; -.
DR ProteomicsDB; 82604; -.
DR Antibodypedia; 53687; 80 antibodies from 18 providers.
DR DNASU; 94030; -.
DR Ensembl; ENST00000389201.7; ENSP00000373853.3; ENSG00000131409.13.
DR Ensembl; ENST00000599957.5; ENSP00000471502.1; ENSG00000131409.13.
DR Ensembl; ENST00000652263.1; ENSP00000498662.1; ENSG00000131409.13.
DR GeneID; 94030; -.
DR KEGG; hsa:94030; -.
DR MANE-Select; ENST00000652263.1; ENSP00000498662.1; NM_001080457.2; NP_001073926.1.
DR UCSC; uc002pss.4; human.
DR CTD; 94030; -.
DR GeneCards; LRRC4B; -.
DR HGNC; HGNC:25042; LRRC4B.
DR HPA; ENSG00000131409; Tissue enhanced (brain, cervix, pituitary gland).
DR neXtProt; NX_Q9NT99; -.
DR OpenTargets; ENSG00000131409; -.
DR PharmGKB; PA134890612; -.
DR VEuPathDB; HostDB:ENSG00000131409; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160261; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q9NT99; -.
DR OMA; TSCPEAC; -.
DR OrthoDB; 282791at2759; -.
DR PhylomeDB; Q9NT99; -.
DR TreeFam; TF324303; -.
DR PathwayCommons; Q9NT99; -.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR SignaLink; Q9NT99; -.
DR SIGNOR; Q9NT99; -.
DR BioGRID-ORCS; 94030; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; LRRC4B; human.
DR GenomeRNAi; 94030; -.
DR Pharos; Q9NT99; Tbio.
DR PRO; PR:Q9NT99; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NT99; protein.
DR Bgee; ENSG00000131409; Expressed in cortical plate and 103 other tissues.
DR ExpressionAtlas; Q9NT99; baseline and differential.
DR Genevisible; Q9NT99; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044300; C:cerebellar mossy fiber; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:BHF-UCL.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IBA:GO_Central.
DR GO; GO:1905606; P:regulation of presynapse assembly; IBA:GO_Central.
DR GO; GO:0099560; P:synaptic membrane adhesion; IBA:GO_Central.
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 2: Evidence at transcript 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..35
FT /evidence="ECO:0000255"
FT CHAIN 36..713
FT /note="Leucine-rich repeat-containing protein 4B"
FT /id="PRO_0000231654"
FT TOPO_DOM 36..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..86
FT /note="LRRNT"
FT REPEAT 87..108
FT /note="LRR 1"
FT REPEAT 111..132
FT /note="LRR 2"
FT REPEAT 135..156
FT /note="LRR 3"
FT REPEAT 159..180
FT /note="LRR 4"
FT REPEAT 183..205
FT /note="LRR 5"
FT REPEAT 208..229
FT /note="LRR 6"
FT REPEAT 230..251
FT /note="LRR 7"
FT REPEAT 254..275
FT /note="LRR 8"
FT REPEAT 278..299
FT /note="LRR 9"
FT DOMAIN 311..363
FT /note="LRRCT"
FT DOMAIN 364..452
FT /note="Ig-like C2-type"
FT REGION 497..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C192"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 385..436
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 637..638
FT /note="AV -> TA (in Ref. 2; AAH56207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 713 AA; 76434 MW; 085B5CACE28038D9 CRC64;
MARARGSPCP PLPPGRMSWP HGALLFLWLF SPPLGAGGGG VAVTSAAGGG SPPATSCPVA
CSCSNQASRV ICTRRDLAEV PASIPVNTRY LNLQENGIQV IRTDTFKHLR HLEILQLSKN
LVRKIEVGAF NGLPSLNTLE LFDNRLTTVP TQAFEYLSKL RELWLRNNPI ESIPSYAFNR
VPSLRRLDLG ELKRLEYISE AAFEGLVNLR YLNLGMCNLK DIPNLTALVR LEELELSGNR
LDLIRPGSFQ GLTSLRKLWL MHAQVATIER NAFDDLKSLE ELNLSHNNLM SLPHDLFTPL
HRLERVHLNH NPWHCNCDVL WLSWWLKETV PSNTTCCARC HAPAGLKGRY IGELDQSHFT
CYAPVIVEPP TDLNVTEGMA AELKCRTGTS MTSVNWLTPN GTLMTHGSYR VRISVLHDGT
LNFTNVTVQD TGQYTCMVTN SAGNTTASAT LNVSAVDPVA AGGTGSGGGG PGGSGGVGGG
SGGYTYFTTV TVETLETQPG EEALQPRGTE KEPPGPTTDG VWGGGRPGDA AGPASSSTTA
PAPRSSRPTE KAFTVPITDV TENALKDLDD VMKTTKIIIG CFVAITFMAA VMLVAFYKLR
KQHQLHKHHG PTRTVEIINV EDELPAASAV SVAAAAAVAS GGGVGGDSHL ALPALERDHL
NHHHYVAAAF KAHYSSNPSG GGCGGKGPPG LNSIHEPLLF KSGSKENVQE TQI