LRC4C_MOUSE
ID LRC4C_MOUSE Reviewed; 640 AA.
AC Q8C031; Q505E5; Q8BGH8;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Leucine-rich repeat-containing protein 4C;
DE AltName: Full=Netrin-G1 ligand;
DE Short=NGL-1;
DE Flags: Precursor;
GN Name=Lrrc4c; Synonyms=Ngl1;
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=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=14595443; DOI=10.1038/nn1148;
RA Lin J.C., Ho W.-H., Gurney A.L., Rosenthal A.;
RT "The netrin-G1 ligand NGL-1 promotes the outgrowth of thalamocortical
RT axons.";
RL Nat. Neurosci. 6:1270-1276(2003).
RN [4]
RP INTERACTION WITH WHRN.
RX PubMed=15590698; DOI=10.1093/hmg/ddi036;
RA Delprat B., Michel V., Goodyear R., Yamasaki Y., Michalski N.,
RA El-Amraoui A., Perfettini I., Legrain P., Richardson G., Hardelin J.-P.,
RA Petit C.;
RT "Myosin XVa and whirlin, two deafness gene products required for hair
RT bundle growth, are located at the stereocilia tips and interact directly.";
RL Hum. Mol. Genet. 14:401-410(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: May promote neurite outgrowth of developing thalamic neurons.
CC {ECO:0000269|PubMed:14595443}.
CC -!- SUBUNIT: Interacts with NTNG1 and WHRN. {ECO:0000269|PubMed:15590698}.
CC -!- INTERACTION:
CC Q8C031; Q80VW5: Whrn; NbExp=4; IntAct=EBI-7417983, EBI-7417603;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Single-
CC pass type I membrane protein.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the developing cerebral cortex
CC and striatum at 14 dpc. {ECO:0000269|PubMed:14595443}.
CC -!- DOMAIN: The LRR region is both necessary and sufficient for the
CC interaction with NTNG1. {ECO:0000250}.
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DR EMBL; AK032467; BAC27884.1; -; mRNA.
DR EMBL; AK034276; BAC28656.1; -; mRNA.
DR EMBL; AK048322; BAC33302.1; -; mRNA.
DR EMBL; BC094588; AAH94588.1; -; mRNA.
DR CCDS; CCDS16460.1; -.
DR RefSeq; NP_001276671.1; NM_001289742.1.
DR RefSeq; NP_001276672.1; NM_001289743.1.
DR RefSeq; NP_001276673.1; NM_001289744.1.
DR RefSeq; NP_848840.3; NM_178725.6.
DR RefSeq; XP_006499542.1; XM_006499479.3.
DR RefSeq; XP_017173628.1; XM_017318139.1.
DR RefSeq; XP_017173629.1; XM_017318140.1.
DR AlphaFoldDB; Q8C031; -.
DR SMR; Q8C031; -.
DR BioGRID; 232325; 1.
DR DIP; DIP-42049N; -.
DR IntAct; Q8C031; 2.
DR MINT; Q8C031; -.
DR STRING; 10090.ENSMUSP00000131795; -.
DR GlyConnect; 2470; 1 N-Linked glycan (2 sites).
DR GlyGen; Q8C031; 2 sites, 1 N-linked glycan (2 sites).
DR iPTMnet; Q8C031; -.
DR PhosphoSitePlus; Q8C031; -.
DR MaxQB; Q8C031; -.
DR PaxDb; Q8C031; -.
DR PeptideAtlas; Q8C031; -.
DR PRIDE; Q8C031; -.
DR ProteomicsDB; 252671; -.
DR Antibodypedia; 26031; 209 antibodies from 26 providers.
DR DNASU; 241568; -.
DR Ensembl; ENSMUST00000059049; ENSMUSP00000131795; ENSMUSG00000050587.
DR Ensembl; ENSMUST00000135431; ENSMUSP00000130984; ENSMUSG00000050587.
DR Ensembl; ENSMUST00000162807; ENSMUSP00000125218; ENSMUSG00000050587.
DR GeneID; 241568; -.
DR KEGG; mmu:241568; -.
DR UCSC; uc008lhc.2; mouse.
DR CTD; 57689; -.
DR MGI; MGI:2442636; Lrrc4c.
DR VEuPathDB; HostDB:ENSMUSG00000050587; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157405; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q8C031; -.
DR OMA; TYKTAYN; -.
DR OrthoDB; 282791at2759; -.
DR PhylomeDB; Q8C031; -.
DR TreeFam; TF324303; -.
DR BioGRID-ORCS; 241568; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Lrrc4c; mouse.
DR PRO; PR:Q8C031; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C031; protein.
DR Bgee; ENSMUSG00000050587; Expressed in caudate-putamen and 135 other tissues.
DR ExpressionAtlas; Q8C031; baseline and differential.
DR Genevisible; Q8C031; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
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; 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; IPR013106; Ig_V-set.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR026878; LRRC4C.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR24369:SF8; PTHR24369:SF8; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00369; LRR_TYP; 8.
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; Immunoglobulin domain; Leucine-rich repeat;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
KW Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..640
FT /note="Leucine-rich repeat-containing protein 4C"
FT /id="PRO_0000015109"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 45..76
FT /note="LRRNT"
FT REPEAT 77..98
FT /note="LRR 1"
FT REPEAT 101..122
FT /note="LRR 2"
FT REPEAT 125..146
FT /note="LRR 3"
FT REPEAT 149..170
FT /note="LRR 4"
FT REPEAT 173..195
FT /note="LRR 5"
FT REPEAT 198..219
FT /note="LRR 6"
FT REPEAT 220..241
FT /note="LRR 7"
FT REPEAT 244..265
FT /note="LRR 8"
FT REPEAT 268..289
FT /note="LRR 9"
FT DOMAIN 301..353
FT /note="LRRCT"
FT DOMAIN 354..442
FT /note="Ig-like C2-type"
FT REGION 463..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 375..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 581
FT /note="M -> V (in Ref. 1; BAC27884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 71992 MW; 9810515A995CAB6B CRC64;
MLNKMTLHPQ QIMIGPRFNR ALFDPLLVVL LALQLLVVAG LVRAQTCPSV CSCSNQFSKV
ICVRKNLREV PDGISTNTRL LNLHENQIQI IKVNSFKHLR HLEILQLSRN HIRTIEIGAF
NGLANLNTLE LFDNRLTTIP NGAFVYLSKL KELWLRNNPI ESIPSYAFNR IPSLRRLDLG
ELKRLSYISE GAFEGLSNLR YLNLAMCNLR EIPNLTPLIK LDELDLSGNH LSAIRPGSFQ
GLMHLQKLWM IQSQIQVIER NAFDNLQSLV EINLAHNNLT LLPHDLFTPL HHLERIHLHH
NPWNCNCDIL WLSWWIRDMA PSNTACCARC NTPPNLKGRY IGELDQNYFT CYAPVIVEPP
ADLNVTEGMA AELKCRASTS LTSVSWITPN GTVMTHGAYK VRIAVLSDGT LNFTNVTVQD
TGMYTCMVSN SVGNTTASAT LNVTAATTTP FSYFSTVTVE TMEPSQDEAR TTDNNVGPTP
VIDWETTNVT TSLTPQSTRS TEKTFTIPVT DINSGIPGID EVMKTTKIII GCFVAITLMA
AVMLVIFYKM RKQHHRQNHH APTRTVEIIN VDDEITGDTP MESHLPMPAI EHEHLNHYNS
YKSPFNHTTT VNTINSIHSS VHEPLLIRMN SKDNVQETQI
