ERBIN_MOUSE
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 03-AUG-2022, entry version 176.
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},
GN Kiaa1225 {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, Pancreas,
RC 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};
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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; 11.
DR IntAct; Q80TH2; 5.
DR MINT; Q80TH2; -.
DR STRING; 10090.ENSMUSP00000140536; -.
DR iPTMnet; Q80TH2; -.
DR PhosphoSitePlus; Q80TH2; -.
DR SwissPalm; Q80TH2; -.
DR jPOST; Q80TH2; -.
DR MaxQB; Q80TH2; -.
DR PaxDb; Q80TH2; -.
DR PRIDE; Q80TH2; -.
DR ProteomicsDB; 275465; -. [Q80TH2-3]
DR ProteomicsDB; 275466; -. [Q80TH2-1]
DR ProteomicsDB; 275467; -. [Q80TH2-2]
DR Antibodypedia; 23812; 201 antibodies from 32 providers.
DR DNASU; 59079; -.
DR Ensembl; ENSMUST00000022222; ENSMUSP00000022222; ENSMUSG00000021709. [Q80TH2-1]
DR Ensembl; ENSMUST00000053927; ENSMUSP00000057956; ENSMUSG00000021709. [Q80TH2-1]
DR Ensembl; ENSMUST00000091269; ENSMUSP00000088813; ENSMUSG00000021709. [Q80TH2-3]
DR Ensembl; ENSMUST00000191275; ENSMUSP00000140536; ENSMUSG00000021709. [Q80TH2-2]
DR GeneID; 59079; -.
DR KEGG; mmu:59079; -.
DR UCSC; uc007rsk.3; mouse. [Q80TH2-3]
DR UCSC; uc056yux.1; mouse. [Q80TH2-1]
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 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 71 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 256 other tissues.
DR ExpressionAtlas; Q80TH2; baseline and differential.
DR Genevisible; Q80TH2; MM.
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:0005176; F:ErbB-2 class receptor binding; IEA:InterPro.
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:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IBA:GO_Central.
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 Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR032927; Erbin.
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:SF46; PTHR23119:SF46; 2.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51450; LRR; 13.
DR PROSITE; PS50106; PDZ; 1.
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
