ID   ERBIN_MOUSE             Reviewed;        1402 AA.
AC   Q80TH2; E9QND6; Q8BQ14; Q8CE41; Q8K171; Q99JU3; Q9JI47;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Erbin {ECO:0000303|PubMed:10878805};
DE   AltName: Full=Densin-180-like protein;
DE   AltName: Full=Erbb2-interacting protein {ECO:0000303|PubMed:10878805};
DE   AltName: Full=Protein LAP2;
GN   Name=Erbin {ECO:0000303|PubMed:10878805};
GN   Synonyms=Erbb2ip {ECO:0000312|MGI:MGI:1890169}, Kiaa1225
GN   {ECO:0000312|EMBL:BAC65755.1}, Lap2;
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] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 308-1376 (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Skin, and Spinal ganglion;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 721-1402 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1160-1402 (ISOFORM 1).
RC   TISSUE=Colon, and Mammary tumor;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 908-1402 (ISOFORM 3).
RX   PubMed=10878805; DOI=10.1038/35017038;
RA   Borg J.-P., Marchetto S., Le Bivic A., Ollendorff V., Jaulin-Bastard F.,
RA   Saito H., Fournier E., Adelaide J., Margolis B., Birnbaum D.;
RT   "ERBIN: a basolateral PDZ protein that interacts with the mammalian
RT   ERBB2/HER2 receptor.";
RL   Nat. Cell Biol. 2:407-414(2000).
RN   [6]
RP   FUNCTION, INTERACTION WITH NOD2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   PRO-315.
RX   PubMed=16203728; DOI=10.1074/jbc.m508538200;
RA   McDonald C., Chen F.F., Ollendorff V., Ogura Y., Marchetto S., Lecine P.,
RA   Borg J.P., Nunez G.;
RT   "A role for Erbin in the regulation of Nod2-dependent NF-kappaB
RT   signaling.";
RL   J. Biol. Chem. 280:40301-40309(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1097, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599 AND SER-600, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18802028; DOI=10.1161/circresaha.108.176024;
RA   Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S.,
RA   O'Connell T.D.;
RT   "Nuclear alpha1-adrenergic receptors signal activated ERK localization to
RT   caveolae in adult cardiac myocytes.";
RL   Circ. Res. 103:992-1000(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; SER-600; SER-712 AND
RP   SER-854, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; SER-444; TYR-483;
RP   SER-595; SER-599; SER-600; SER-712; SER-849; SER-869 AND SER-1150,
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231 AND SER-1234 (ISOFORM
RP   2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, and Spleen;
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: Acts as an adapter for the receptor ERBB2, in epithelia. By
CC       binding the unphosphorylated ERBB2 'Tyr-1248' receptor, it may
CC       contribute to stabilize this unphosphorylated state (By similarity).
CC       Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory
CC       cytokine secretion (PubMed:16203728). {ECO:0000250|UniProtKB:Q96RT1,
CC       ECO:0000269|PubMed:16203728}.
CC   -!- SUBUNIT: Interacts with ERBB2, BPAG1 and ITGB4. May favor the
CC       localization of ERBB2, by restricting its presence to the basolateral
CC       membrane of epithelial cells. Also found to interact with ARVCF and
CC       delta catenin. Interacts (via C-terminus) with DST (via N-terminus) (By
CC       similarity). Interacts with NOD2 (via CARD domain) (PubMed:16203728).
CC       {ECO:0000250|UniProtKB:Q96RT1, ECO:0000269|PubMed:16203728}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome
CC       {ECO:0000250|UniProtKB:Q96RT1}. Nucleus membrane
CC       {ECO:0000269|PubMed:18802028}. Basolateral cell membrane
CC       {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which are
CC       cell-substrate adhesion complexes in stratified epithelia. In
CC       transfected cells, either diffusely distributed over the cytoplasm or
CC       concentrated at the basolateral membrane (By similarity). Colocalizes
CC       with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear
CC       membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q96RT1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3;
CC         IsoId=Q80TH2-3; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q80TH2-1; Sequence=VSP_010809;
CC       Name=2;
CC         IsoId=Q80TH2-2; Sequence=VSP_010808;
CC   -!- PTM: Isoform 2 is phosphorylated on Ser-1231 and Ser-1234.
CC   -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65755.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AK122473; BAC65755.1; ALT_INIT; mRNA.
DR   EMBL; AC154310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT009728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK029054; BAC26267.1; -; mRNA.
DR   EMBL; AK051733; BAC34742.1; -; mRNA.
DR   EMBL; BC005691; AAH05691.3; -; mRNA.
DR   EMBL; BC028256; AAH28256.1; -; mRNA.
DR   EMBL; AF263743; AAF77047.1; -; mRNA.
DR   CCDS; CCDS26744.1; -. [Q80TH2-2]
DR   CCDS; CCDS79233.1; -. [Q80TH2-3]
DR   RefSeq; NP_001005868.1; NM_001005868.2. [Q80TH2-2]
DR   RefSeq; NP_001276402.1; NM_001289473.1. [Q80TH2-3]
DR   RefSeq; NP_001276403.1; NM_001289474.1.
DR   RefSeq; NP_001276404.1; NM_001289475.1.
DR   AlphaFoldDB; Q80TH2; -.
DR   BMRB; Q80TH2; -.
DR   SMR; Q80TH2; -.
DR   BioGRID; 208523; 25.
DR   IntAct; Q80TH2; 5.
DR   MINT; Q80TH2; -.
DR   STRING; 10090.ENSMUSP00000140536; -.
DR   GlyGen; Q80TH2; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q80TH2; -.
DR   PhosphoSitePlus; Q80TH2; -.
DR   SwissPalm; Q80TH2; -.
DR   jPOST; Q80TH2; -.
DR   MaxQB; Q80TH2; -.
DR   PaxDb; 10090-ENSMUSP00000140536; -.
DR   ProteomicsDB; 275465; -. [Q80TH2-3]
DR   ProteomicsDB; 275466; -. [Q80TH2-1]
DR   ProteomicsDB; 275467; -. [Q80TH2-2]
DR   Pumba; Q80TH2; -.
DR   Antibodypedia; 23812; 239 antibodies from 32 providers.
DR   DNASU; 59079; -.
DR   Ensembl; ENSMUST00000022222.12; ENSMUSP00000022222.6; ENSMUSG00000021709.15. [Q80TH2-1]
DR   Ensembl; ENSMUST00000053927.12; ENSMUSP00000057956.7; ENSMUSG00000021709.15. [Q80TH2-1]
DR   Ensembl; ENSMUST00000091269.11; ENSMUSP00000088813.5; ENSMUSG00000021709.15. [Q80TH2-3]
DR   Ensembl; ENSMUST00000191275.7; ENSMUSP00000140536.2; ENSMUSG00000021709.15. [Q80TH2-2]
DR   GeneID; 59079; -.
DR   KEGG; mmu:59079; -.
DR   UCSC; uc007rsk.3; mouse. [Q80TH2-3]
DR   UCSC; uc056yux.1; mouse. [Q80TH2-1]
DR   AGR; MGI:1890169; -.
DR   CTD; 55914; -.
DR   MGI; MGI:1890169; Erbin.
DR   VEuPathDB; HostDB:ENSMUSG00000021709; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000159526; -.
DR   InParanoid; Q80TH2; -.
DR   OMA; QLPETIX; -.
DR   OrthoDB; 2909504at2759; -.
DR   TreeFam; TF351429; -.
DR   Reactome; R-MMU-1227986; Signaling by ERBB2.
DR   Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
DR   Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR   Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR   Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR   Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR   Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR   Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR   Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR   Reactome; R-MMU-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR   BioGRID-ORCS; 59079; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Erbin; mouse.
DR   PRO; PR:Q80TH2; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q80TH2; Protein.
DR   Bgee; ENSMUSG00000021709; Expressed in parotid gland and 258 other cell types or tissues.
DR   ExpressionAtlas; Q80TH2; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030056; C:hemidesmosome; ISO:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0099572; C:postsynaptic specialization; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR   GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IMP:UniProtKB.
DR   GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
DR   GO; GO:0006605; P:protein targeting; IDA:MGI.
DR   GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR   GO; GO:0032495; P:response to muramyl dipeptide; ISO:MGI.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR23119; DISCS LARGE; 1.
DR   PANTHER; PTHR23119:SF46; ERBB2-INTERACTING PROTEIN; 1.
DR   Pfam; PF13855; LRR_8; 4.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00364; LRR_BAC; 9.
DR   SMART; SM00365; LRR_SD22; 8.
DR   SMART; SM00369; LRR_TYP; 12.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS51450; LRR; 13.
DR   PROSITE; PS50106; PDZ; 1.
DR   Genevisible; Q80TH2; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Leucine-rich repeat;
KW   Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1402
FT                   /note="Erbin"
FT                   /id="PRO_0000188302"
FT   REPEAT          23..44
FT                   /note="LRR 1"
FT   REPEAT          47..68
FT                   /note="LRR 2"
FT   REPEAT          70..91
FT                   /note="LRR 3"
FT   REPEAT          93..114
FT                   /note="LRR 4"
FT   REPEAT          116..137
FT                   /note="LRR 5"
FT   REPEAT          139..161
FT                   /note="LRR 6"
FT   REPEAT          162..183
FT                   /note="LRR 7"
FT   REPEAT          185..206
FT                   /note="LRR 8"
FT   REPEAT          208..229
FT                   /note="LRR 9"
FT   REPEAT          231..252
FT                   /note="LRR 10"
FT   REPEAT          254..275
FT                   /note="LRR 11"
FT   REPEAT          277..298
FT                   /note="LRR 12"
FT   REPEAT          300..321
FT                   /note="LRR 13"
FT   REPEAT          323..344
FT                   /note="LRR 14"
FT   REPEAT          346..367
FT                   /note="LRR 15"
FT   REPEAT          369..391
FT                   /note="LRR 16"
FT   REPEAT          392..413
FT                   /note="LRR 17"
FT   DOMAIN          1311..1400
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          465..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          990..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1070..1093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1198..1217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1222..1274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..688
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1070..1088
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1109..1169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1250..1269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         444
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         483
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         485
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RT1"
FT   MOD_RES         595
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         599
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         600
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         617
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RT1"
FT   MOD_RES         712
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         849
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         854
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         869
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         914
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RT1"
FT   MOD_RES         917
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RT1"
FT   MOD_RES         928
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RT1"
FT   MOD_RES         970
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RT1"
FT   MOD_RES         1097
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         1150
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1171
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RT1"
FT   MOD_RES         1276
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RT1"
FT   VAR_SEQ         1203
FT                   /note="K -> KSMLSRSFNSNLTAVSSSHYGSSRDLHGSQGSLALSVADGRGSGGHI
FT                   FR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010808"
FT   VAR_SEQ         1243..1268
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:12693553,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010809"
FT   MUTAGEN         315
FT                   /note="P->L: Decreases interaction with NOD2."
FT                   /evidence="ECO:0000269|PubMed:16203728"
FT   CONFLICT        255
FT                   /note="L -> P (in Ref. 1; BAC65755)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        721..723
FT                   /note="DKK -> HAS (in Ref. 4; AAH28256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        908..910
FT                   /note="VRS -> ASG (in Ref. 5; AAF77047)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q80TH2-2:1231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q80TH2-2:1234
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   1402 AA;  157248 MW;  DBAFF4BD1BC48019 CRC64;
     MTTKRSLFVR LVPCRCLRGE EETVTTLDYS HCSLEQVPKE IFTFEKTLEE LYLDANQIEE
     LPKQLFNCQS LHKLSLPDND LTTLPASIAN LINLRELDVS KNGIQEFPEN IKNCKVLTIV
     EASVNPISKL PDGFSQLLNL TQLYLNDAFL EFLPANFGRL TKLQILELRE NQLKMLPKTM
     NRLTQLERLD LGSNEFTEVP EVLEQLSGLR EFWMDGNRLT FIPGFIGSLR QLTYLDVSKN
     NIEMVEEGIS TCENLQDFLL SSNSLQQLPE TIGSLKNVTT LKIDENQLMY LPDSIGGLRS
     IEELDCSFNE IEALPSSIGQ LTNMRTFAAD HNYLQQLPPE IGNWKNITVL FLHCNKLETL
     PEEMGDMQKL KVINLSDNRL KNLPFSFTKL QQLTAMWLSD NQSKPLIPLQ KETDTETQKM
     VLTNYMFPQQ PRTEDVMFIS DNESFNPALW EEQRKQRAQV AFECDEDKDE REAPPREGNL
     KRYPTPYPDE LKNMVKTVQT IVHRLKDEET NEESGRDLKQ HEDQQVVNKD KCVKTSESTT
     TKSKLDEREK YMNSVQKMSE PEAETNGGNL PVTASMKLSG NLKHIVNHDD VFEESEELSS
     DEEMKMAEMR PPLIESSINQ PKVVALSNNK KDDAKDADSL SDEVTHNSNQ NNSNCSSPSR
     MSDSVSLNTD SSQDTSLCSP VKQTPVDSNS KVRQEDENFN SLLQNGVNLN NSPEEKFKIN
     DKKDFKLPEY DLNIEEQLVL IEKDIDSKAT SDDSRQLDHI NMNINKLVTN NIFQPEVMER
     SKMQDIVLGT GFLSIHPKNE AEHIENGAKF PNLESINKVN GLCEDTAPSP GRVEPQKASS
     SADVGISKST EDLSPQRSGP TGAVVKSHSI TNMETGGLKI YDILGDDGPQ PPSAAVKIAS
     AVDGKNIVRS KSATLLYDQP LQVFTAASSS SELLSGTKAV FKFDSNHNPE EPDIIRAATV
     SGPQSTPHLY GPPQYNVQYS GSATVKDTLW HPKQNPQIDP VSFPPQRLPR SESAENHSYA
     KHSANMNFSN HNNVRANTGY HLQQRLAPAR HGEMWAISPN DRLVPAVTRT TIQRQSSVSS
     TASVNLGDPT RRTEGDYLSY RELHSMGRTP VMSGSQRPLS ARAYSIDGPN TSRPQSARPS
     INEIPERTMS VSDFNYSRTS PSKRPNTRVG SEHSLLDPPG KSKVPHDWRE QVLRHIEAKK
     LEKHPQTSSP GECCQDDRFM SEEQNHPSGA LSHRGLPDSL MKMPLSNGQM GQPLRPQAHY
     SQTHHPPQAS VARHPSREQL IDYLMLKVAH QPPYTHPHCS PRQGHELAKQ EIRVRVEKDP
     ELGFSISGGV GGRGNPFRPD DDGIFVTRVQ PEGPASKLLQ PGDKIIQANG YSFINIEHGQ
     AVSLLKTFHN AVDLIIVREV SS
//