LRC4B_MOUSE
ID LRC4B_MOUSE Reviewed; 709 AA.
AC P0C192;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-709.
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH DLG4.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Interacts with DLG4.
CC {ECO:0000250, ECO:0000269|PubMed:16980967}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC Presynaptic cell membrane {ECO:0000250}.
CC -!- DOMAIN: The extreme C-terminus binds to the first 2 PDZ domains of
CC DLG4.
CC -!- PTM: N-glycosylated. O-glycosylated; contains sialic acid.
CC {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC060263; AAH60263.1; -; mRNA.
DR EMBL; AK140418; BAE24378.1; -; mRNA.
DR CCDS; CCDS21206.1; -.
DR RefSeq; NP_937893.1; NM_198250.1.
DR PDB; 3ZYN; X-ray; 3.20 A; A/B=57-365.
DR PDB; 3ZYO; X-ray; 3.10 A; A=57-455.
DR PDBsum; 3ZYN; -.
DR PDBsum; 3ZYO; -.
DR AlphaFoldDB; P0C192; -.
DR SMR; P0C192; -.
DR BioGRID; 234868; 1.
DR IntAct; P0C192; 2.
DR MINT; P0C192; -.
DR STRING; 10090.ENSMUSP00000053123; -.
DR GlyGen; P0C192; 9 sites.
DR iPTMnet; P0C192; -.
DR PhosphoSitePlus; P0C192; -.
DR MaxQB; P0C192; -.
DR PaxDb; P0C192; -.
DR PeptideAtlas; P0C192; -.
DR PRIDE; P0C192; -.
DR ProteomicsDB; 290157; -.
DR Antibodypedia; 53687; 80 antibodies from 18 providers.
DR DNASU; 272381; -.
DR Ensembl; ENSMUST00000058667; ENSMUSP00000053123; ENSMUSG00000047085.
DR GeneID; 272381; -.
DR KEGG; mmu:272381; -.
DR UCSC; uc009gpj.1; mouse.
DR CTD; 94030; -.
DR MGI; MGI:3027390; Lrrc4b.
DR VEuPathDB; HostDB:ENSMUSG00000047085; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160261; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; P0C192; -.
DR OMA; TSCPEAC; -.
DR OrthoDB; 282791at2759; -.
DR PhylomeDB; P0C192; -.
DR TreeFam; TF324303; -.
DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR BioGRID-ORCS; 272381; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Lrrc4b; mouse.
DR EvolutionaryTrace; P0C192; -.
DR PRO; PR:P0C192; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P0C192; protein.
DR Bgee; ENSMUSG00000047085; Expressed in embryonic brain and 99 other tissues.
DR ExpressionAtlas; P0C192; baseline and differential.
DR Genevisible; P0C192; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044300; C:cerebellar mossy fiber; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
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; IPI:BHF-UCL.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:BHF-UCL.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; ISO:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:MGI.
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 3D-structure; 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_0000232387"
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:0007744|PubMed:21183079"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
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 CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 387..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 574
FT /note="K -> R (in Ref. 2; BAE24378)"
FT /evidence="ECO:0000305"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3ZYO"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:3ZYN"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:3ZYO"
FT TURN 105..110
FT /evidence="ECO:0007829|PDB:3ZYN"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3ZYO"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:3ZYO"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3ZYO"
FT TURN 177..182
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3ZYO"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3ZYO"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3ZYO"
FT TURN 272..277
FT /evidence="ECO:0007829|PDB:3ZYN"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3ZYO"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:3ZYO"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:3ZYO"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:3ZYO"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:3ZYO"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 388..399
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:3ZYO"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:3ZYO"
FT STRAND 446..453
FT /evidence="ECO:0007829|PDB:3ZYO"
SQ SEQUENCE 709 AA; 76156 MW; 0C39148F9A8E3586 CRC64;
MAQAHIRGSP CPLLPPGRMS WPHGALLLLW 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
