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   13-FEB-2019, entry version 153.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Bhaskar S., Dickerson J.E., Mermerkaya M., Silay M.S., Lewis M.A.,
RA   Olondriz M.B., Gener B., Beetz C., Varga R.E., Guelpinar O., Sueer E.,
RA   Soyguer T., Ozcakar Z.B., Yalcinkaya F., Kavaz A., Bulum B.,
RA   Guecuek A., Yue W.W., Erdogan F., Berry A., Hanley N.A.,
RA   McKenzie E.A., Hilton E.N., Woolf A.S., Newman W.G.;
RT   "LRIG2 mutations cause urofacial syndrome.";
RL   Am. J. Hum. Genet. 92:259-264(2013).
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
CC       autosomal recessive disorder characterized by facial grimacing
CC       when attempting to smile and failure of the urinary bladder to
CC       void completely despite a lack of anatomical bladder outflow
CC       obstruction or overt neurological damage. Affected individuals
CC       often have reflux of infected urine from the bladder to the upper
CC       renal tract, with a risk of kidney damage and renal failure.
CC       {ECO:0000269|PubMed:23313374}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA34526.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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   UniGene; Hs.448972; -.
DR   ProteinModelPortal; O94898; -.
DR   SMR; O94898; -.
DR   BioGrid; 115194; 8.
DR   IntAct; O94898; 2.
DR   STRING; 9606.ENSP00000355396; -.
DR   iPTMnet; O94898; -.
DR   PhosphoSitePlus; O94898; -.
DR   BioMuta; LRIG2; -.
DR   EPD; O94898; -.
DR   jPOST; O94898; -.
DR   MaxQB; O94898; -.
DR   PaxDb; O94898; -.
DR   PeptideAtlas; O94898; -.
DR   PRIDE; O94898; -.
DR   ProteomicsDB; 50530; -.
DR   Ensembl; ENST00000361127; ENSP00000355396; ENSG00000198799.
DR   GeneID; 9860; -.
DR   KEGG; hsa:9860; -.
DR   UCSC; uc001edf.2; human.
DR   CTD; 9860; -.
DR   DisGeNET; 9860; -.
DR   EuPathDB; HostDB:ENSG00000198799.11; -.
DR   GeneCards; LRIG2; -.
DR   GeneReviews; LRIG2; -.
DR   HGNC; HGNC:20889; LRIG2.
DR   HPA; HPA015538; -.
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   eggNOG; KOG4194; Eukaryota.
DR   eggNOG; COG4886; LUCA.
DR   GeneTree; ENSGT00940000158791; -.
DR   HOGENOM; HOG000113380; -.
DR   HOVERGEN; HBG052353; -.
DR   InParanoid; O94898; -.
DR   OMA; LVWVIVI; -.
DR   OrthoDB; 161719at2759; -.
DR   PhylomeDB; O94898; -.
DR   TreeFam; TF325380; -.
DR   ChiTaRS; LRIG2; human.
DR   GenomeRNAi; 9860; -.
DR   PRO; PR:O94898; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000198799; Expressed in 204 organ(s), highest expression level in forebrain.
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:0043025; C:neuronal cell body; 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: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: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   2: Evidence at transcript level;
KW   Cell membrane; Complete proteome; Cytoplasm; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     40       {ECO:0000255}.
FT   CHAIN        41   1065       Leucine-rich repeats and immunoglobulin-
FT                                like domains protein 2.
FT                                /FTId=PRO_0000014829.
FT   TOPO_DOM     41    807       Extracellular. {ECO:0000255}.
FT   TRANSMEM    808    828       Helical. {ECO:0000255}.
FT   TOPO_DOM    829   1065       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       41     75       LRRNT.
FT   REPEAT       76     97       LRR 1.
FT   REPEAT       98    119       LRR 2.
FT   REPEAT      121    142       LRR 3.
FT   REPEAT      145    166       LRR 4.
FT   REPEAT      168    189       LRR 5.
FT   REPEAT      193    214       LRR 6.
FT   REPEAT      216    237       LRR 7.
FT   REPEAT      240    261       LRR 8.
FT   REPEAT      264    285       LRR 9.
FT   REPEAT      288    309       LRR 10.
FT   REPEAT      312    333       LRR 11.
FT   REPEAT      336    357       LRR 12.
FT   REPEAT      360    382       LRR 13.
FT   REPEAT      387    408       LRR 14.
FT   REPEAT      411    432       LRR 15.
FT   DOMAIN      443    494       LRRCT.
FT   DOMAIN      498    597       Ig-like C2-type 1.
FT   DOMAIN      602    691       Ig-like C2-type 2.
FT   DOMAIN      696    785       Ig-like C2-type 3.
FT   MOD_RES     906    906       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q52KR2}.
FT   CARBOHYD     91     91       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    121    121       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    173    173       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    189    189       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    274    274       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    441    441       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    468    468       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    514    514       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    571    571       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    589    589       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    687    687       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    728    728       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    519    580       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    623    675       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    717    766       {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
//