LRIG2_HUMAN
ID LRIG2_HUMAN Reviewed; 1065 AA.
AC O94898; Q9NSN2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Leucine-rich repeats and immunoglobulin-like domains protein 2;
DE Short=LIG-2;
DE Flags: Precursor;
GN Name=LRIG2; Synonyms=KIAA0806, LIG2;
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 MRNA].
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-133.
RC TISSUE=Brain;
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).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15145052; DOI=10.1016/j.gene.2004.02.002;
RA Holmlund C., Nilsson J., Guo D., Starefeldt A., Golovleva I.,
RA Henriksson R., Hedman H.;
RT "Characterization and tissue-specific expression of human LRIG2.";
RL Gene 332:35-43(2004).
RN [4]
RP INVOLVEMENT IN UFS2.
RX PubMed=23313374; DOI=10.1016/j.ajhg.2012.12.002;
RA Stuart H.M., Roberts N.A., Burgu B., Daly S.B., Urquhart J.E., Bhaskar S.,
RA Dickerson J.E., Mermerkaya M., Silay M.S., Lewis M.A., Olondriz M.B.,
RA Gener B., Beetz C., Varga R.E., Guelpinar O., Sueer E., Soyguer T.,
RA Ozcakar Z.B., Yalcinkaya F., Kavaz A., Bulum B., Guecuek A., Yue W.W.,
RA Erdogan F., Berry A., Hanley N.A., McKenzie E.A., Hilton E.N., Woolf A.S.,
RA Newman W.G.;
RT "LRIG2 mutations cause urofacial syndrome.";
RL Am. J. Hum. Genet. 92:259-264(2013).
CC -!- INTERACTION:
CC O94898; P00533: EGFR; NbExp=4; IntAct=EBI-2830372, EBI-297353;
CC O94898; P09619: PDGFRB; NbExp=3; IntAct=EBI-2830372, EBI-641237;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15145052};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15145052}.
CC Cytoplasm {ECO:0000269|PubMed:15145052}.
CC -!- TISSUE SPECIFICITY: Detected in all tissues analyzed.
CC {ECO:0000269|PubMed:15145052}.
CC -!- DISEASE: Urofacial syndrome 2 (UFS2) [MIM:615112]: A rare autosomal
CC recessive disorder characterized by facial grimacing when attempting to
CC smile and failure of the urinary bladder to void completely despite a
CC lack of anatomical bladder outflow obstruction or overt neurological
CC damage. Affected individuals often have reflux of infected urine from
CC the bladder to the upper renal tract, with a risk of kidney damage and
CC renal failure. {ECO:0000269|PubMed:23313374}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34526.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018349; BAA34526.2; ALT_INIT; mRNA.
DR EMBL; AL161998; CAB82328.2; -; mRNA.
DR CCDS; CCDS30808.1; -.
DR PIR; T47152; T47152.
DR RefSeq; NP_001299615.1; NM_001312686.1.
DR RefSeq; NP_055628.1; NM_014813.2.
DR AlphaFoldDB; O94898; -.
DR SMR; O94898; -.
DR BioGRID; 115194; 97.
DR IntAct; O94898; 6.
DR STRING; 9606.ENSP00000355396; -.
DR GlyGen; O94898; 12 sites.
DR iPTMnet; O94898; -.
DR PhosphoSitePlus; O94898; -.
DR BioMuta; LRIG2; -.
DR EPD; O94898; -.
DR jPOST; O94898; -.
DR MassIVE; O94898; -.
DR MaxQB; O94898; -.
DR PaxDb; O94898; -.
DR PeptideAtlas; O94898; -.
DR PRIDE; O94898; -.
DR ProteomicsDB; 50530; -.
DR Antibodypedia; 2748; 143 antibodies from 19 providers.
DR DNASU; 9860; -.
DR Ensembl; ENST00000361127.6; ENSP00000355396.4; ENSG00000198799.12.
DR GeneID; 9860; -.
DR KEGG; hsa:9860; -.
DR MANE-Select; ENST00000361127.6; ENSP00000355396.4; NM_014813.3; NP_055628.1.
DR UCSC; uc001edf.2; human.
DR CTD; 9860; -.
DR DisGeNET; 9860; -.
DR GeneCards; LRIG2; -.
DR GeneReviews; LRIG2; -.
DR HGNC; HGNC:20889; LRIG2.
DR HPA; ENSG00000198799; Low tissue specificity.
DR MalaCards; LRIG2; -.
DR MIM; 608869; gene.
DR MIM; 615112; phenotype.
DR neXtProt; NX_O94898; -.
DR OpenTargets; ENSG00000198799; -.
DR Orphanet; 2704; Ochoa syndrome.
DR PharmGKB; PA134905053; -.
DR VEuPathDB; HostDB:ENSG00000198799; -.
DR eggNOG; KOG4194; Eukaryota.
DR GeneTree; ENSGT00940000158791; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; O94898; -.
DR OMA; MSCHRLQ; -.
DR OrthoDB; 161719at2759; -.
DR PhylomeDB; O94898; -.
DR TreeFam; TF325380; -.
DR PathwayCommons; O94898; -.
DR SignaLink; O94898; -.
DR BioGRID-ORCS; 9860; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; LRIG2; human.
DR GenomeRNAi; 9860; -.
DR Pharos; O94898; Tbio.
DR PRO; PR:O94898; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O94898; protein.
DR Bgee; ENSG00000198799; Expressed in tendon of biceps brachii and 186 other tissues.
DR Genevisible; O94898; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097708; C:intracellular vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0060384; P:innervation; IEA:Ensembl.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IEA:Ensembl.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR GO; GO:2001222; P:regulation of neuron migration; IEA:Ensembl.
DR GO; GO:0010640; P:regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.80.10.10; -; 2.
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 Pfam; PF07679; I-set; 2.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01463; LRRCT; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS51450; LRR; 14.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..1065
FT /note="Leucine-rich repeats and immunoglobulin-like domains
FT protein 2"
FT /id="PRO_0000014829"
FT TOPO_DOM 41..807
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 808..828
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 829..1065
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..75
FT /note="LRRNT"
FT REPEAT 76..97
FT /note="LRR 1"
FT REPEAT 98..119
FT /note="LRR 2"
FT REPEAT 121..142
FT /note="LRR 3"
FT REPEAT 145..166
FT /note="LRR 4"
FT REPEAT 168..189
FT /note="LRR 5"
FT REPEAT 193..214
FT /note="LRR 6"
FT REPEAT 216..237
FT /note="LRR 7"
FT REPEAT 240..261
FT /note="LRR 8"
FT REPEAT 264..285
FT /note="LRR 9"
FT REPEAT 288..309
FT /note="LRR 10"
FT REPEAT 312..333
FT /note="LRR 11"
FT REPEAT 336..357
FT /note="LRR 12"
FT REPEAT 360..382
FT /note="LRR 13"
FT REPEAT 387..408
FT /note="LRR 14"
FT REPEAT 411..432
FT /note="LRR 15"
FT DOMAIN 443..494
FT /note="LRRCT"
FT DOMAIN 498..597
FT /note="Ig-like C2-type 1"
FT DOMAIN 602..691
FT /note="Ig-like C2-type 2"
FT DOMAIN 696..785
FT /note="Ig-like C2-type 3"
FT REGION 962..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 906
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q52KR2"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 519..580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 623..675
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 717..766
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1065 AA; 118965 MW; CD2903A861DC4887 CRC64;
MAPAPLGVPE EQLLGCRSRV LSRLLFIAQT ALLLLPAAGA GLCPAPCSCR IPLLDCSRRK
LPAPSWRALS GLLPPDTAIL DFSHNRLSNW NISLESQTLQ EVKMNYNELT EIPYFGEPTS
NITLLSLVHN IIPEINAQAL QFYPALESLD LSSNIISEIK TSSFPRMQLK YLNLSNNRIT
TLEAGCFDNL SSSLLVVKLN RNRMSMIPPK IFKLPHLQFL ELKRNRIKIV EGLTFQGLDS
LRSLKMQRNG ISKLKDGAFF GLNNMEELEL EHNNLTRVNK GWLYGLRMLQ QLYVSQNAIE
RISPDAWEFC QRLSELDLSY NQLTRLDESA FVGLSLLERL NLGDNRVTHI ADGVFRFLSN
LQTLDLRNNE ISWAIEDASE AFAGLTSLTK LILQGNQIKS ITKKAFIGLE SLEHLDLNNN
AIMSIQENAF SQTHLKELIL NTSSLLCDCH LKWLLQWLVD NNFQHSVNVS CAHPEWLAGQ
SILNVDLKDF VCDDFLKPQI RTHPETIIAL RGMNVTLTCT AVSSSDSPMS TVWRKDSEIL
YDVDTENFVR YWQQAGEALE YTSILHLFNV NFTDEGKYQC IVTNHFGSNY SQKAKLTVNE
MPSFLKTPMD LTIRTGAMAR LECAAEGHPA PQISWQKDGG TDFPAARERR MHVMPEDDVF
FIANVKIEDM GIYSCMAQNT AGGLSANASL TVLETPSFIR PLEDKTVTRG ETAVLQCIAG
GSPAPRLNWT KDDGPLLVTE RHFFAAANQL LIIVDAGLED AGKYTCIMSN TLGTERGHIY
LNVISSPNCD SSQSSIGHED DGWTTVGIVI IVVVCCVVGT SLIWVIVIYH MRRKNEDYSI
TNTEELNLPA DIPSYLSSQG TLSEPQEGYS NSEAGSHQQL MPPANGYIHK GTDGGTGTRV
ICSDCYDNAN IYSRTREYCP YTYIAEEDVL DQTLSSLMVQ MPKETYLVHP PQDTTALESL
IPSANREPSA FPTNHERISE KKLPSTQMSG ETLQRPVWNI NRELGLPHPP FSQQPVHESP
QLHQNEGLAG REPDCSASSM SCHRLQDHAF DFSRTRNIQD GSEGT
