FAT4_MOUSE
ID FAT4_MOUSE Reviewed; 4981 AA.
AC Q2PZL6; E9QMR9; Q68FE0; Q8BM82; Q8CD68;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protocadherin Fat 4;
DE AltName: Full=FAT tumor suppressor homolog 4;
DE AltName: Full=Fat-like cadherin protein FAT-J;
DE Flags: Precursor;
GN Name=Fat4; Synonyms=Fatj;
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 [MRNA] (ISOFORM 1).
RA Qi C., Zhu Y.T., Hu L., Zhang Z., Rao S.M., Zhu Y.-J.;
RT "Identification of Fat4 as the candidate tumor suppressor gene in breast
RT cancers through random chromosome deletion.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 1329-4981 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4473-4981 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
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 2963-4981 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4878, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=16059920; DOI=10.1002/dvdy.20515;
RA Rock R., Schrauth S., Gessler M.;
RT "Expression of mouse dchs1, fjx1, and fat-j suggests conservation of the
RT planar cell polarity pathway identified in Drosophila.";
RL Dev. Dyn. 234:747-755(2005).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18604206; DOI=10.1038/ng.179;
RA Saburi S., Hester I., Fischer E., Pontoglio M., Eremina V., Gessler M.,
RA Quaggin S.E., Harrison R., Mount R., McNeill H.;
RT "Loss of Fat4 disrupts PCP signaling and oriented cell division and leads
RT to cystic kidney disease.";
RL Nat. Genet. 40:1010-1015(2008).
RN [8]
RP HETEROPHILIC INTERACTION WITH DCHS1, AND INTERACTION WITH MPDZ.
RX PubMed=19506035; DOI=10.1083/jcb.200811030;
RA Ishiuchi T., Misaki K., Yonemura S., Takeichi M., Tanoue T.;
RT "Mammalian Fat and Dachsous cadherins regulate apical membrane organization
RT in the embryonic cerebral cortex.";
RL J. Cell Biol. 185:959-967(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=21303848; DOI=10.1242/dev.057166;
RA Mao Y., Mulvaney J., Zakaria S., Yu T., Morgan K.M., Allen S., Basson M.A.,
RA Francis-West P., Irvine K.D.;
RT "Characterization of a Dchs1 mutant mouse reveals requirements for Dchs1-
RT Fat4 signaling during mammalian development.";
RL Development 138:947-957(2011).
RN [11]
RP DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=24056717; DOI=10.1038/ng.2765;
RA Cappello S., Gray M.J., Badouel C., Lange S., Einsiedler M., Srour M.,
RA Chitayat D., Hamdan F.F., Jenkins Z.A., Morgan T., Preitner N., Uster T.,
RA Thomas J., Shannon P., Morrison V., Di Donato N., Van Maldergem L.,
RA Neuhann T., Newbury-Ecob R., Swinkells M., Terhal P., Wilson L.C.,
RA Zwijnenburg P.J., Sutherland-Smith A.J., Black M.A., Markie D.,
RA Michaud J.L., Simpson M.A., Mansour S., McNeill H., Goetz M.,
RA Robertson S.P.;
RT "Mutations in genes encoding the cadherin receptor-ligand pair DCHS1 and
RT FAT4 disrupt cerebral cortical development.";
RL Nat. Genet. 45:1300-1308(2013).
CC -!- FUNCTION: Cadherins are cell-cell interaction molecules. FAT4 plays a
CC role in the maintenance of planar cell polarity as well as in
CC inhibition of YAP1-mediated neuroprogenitor cell proliferation and
CC differentiation. {ECO:0000269|PubMed:18604206,
CC ECO:0000269|PubMed:24056717}.
CC -!- SUBUNIT: Heterophilic interaction with DCHS1; this interaction affects
CC their respective protein levels. Interacts (via cytoplasmic domain)
CC with MPDZ. Forms a complex with PALS1 and MPDZ.
CC {ECO:0000269|PubMed:19506035}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=In the kidney, localizes to
CC primary cilia. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2PZL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2PZL6-2; Sequence=VSP_032339, VSP_032340;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16059920}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all layers of the developing brain,
CC with expression being most prominent at the ventricular margin.
CC {ECO:0000269|PubMed:24056717}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit postnatal lethality,
CC growth retardation, small lungs, abnormal cochlea morphology, abnormal
CC kidney morphology, cardiovascular abnormalities and skeletal
CC abnormalities. DCHS1 and FAT4 single mutants and DCHS1/FAT4 double
CC mutants have similar phenotypes. {ECO:0000269|PubMed:18604206,
CC ECO:0000269|PubMed:21303848, ECO:0000269|PubMed:24056717}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27359.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC28751.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ286572; ABB88946.1; -; mRNA.
DR EMBL; AC122841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK031348; BAC27359.1; ALT_INIT; mRNA.
DR EMBL; AK034552; BAC28751.1; ALT_INIT; mRNA.
DR EMBL; BC079887; AAH79887.1; -; mRNA.
DR CCDS; CCDS17325.1; -. [Q2PZL6-1]
DR RefSeq; NP_899044.3; NM_183221.3. [Q2PZL6-1]
DR RefSeq; XP_006535547.1; XM_006535484.3. [Q2PZL6-1]
DR SMR; Q2PZL6; -.
DR IntAct; Q2PZL6; 1.
DR STRING; 10090.ENSMUSP00000061836; -.
DR GlyConnect; 2656; 1 N-Linked glycan (1 site).
DR GlyGen; Q2PZL6; 38 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q2PZL6; -.
DR PhosphoSitePlus; Q2PZL6; -.
DR MaxQB; Q2PZL6; -.
DR PaxDb; Q2PZL6; -.
DR PeptideAtlas; Q2PZL6; -.
DR PRIDE; Q2PZL6; -.
DR ProteomicsDB; 275590; -. [Q2PZL6-1]
DR ProteomicsDB; 275591; -. [Q2PZL6-2]
DR Antibodypedia; 62649; 119 antibodies from 17 providers.
DR Ensembl; ENSMUST00000061260; ENSMUSP00000061836; ENSMUSG00000046743. [Q2PZL6-1]
DR GeneID; 329628; -.
DR KEGG; mmu:329628; -.
DR UCSC; uc008pbe.1; mouse. [Q2PZL6-2]
DR UCSC; uc008pbf.1; mouse. [Q2PZL6-1]
DR CTD; 79633; -.
DR MGI; MGI:3045256; Fat4.
DR VEuPathDB; HostDB:ENSMUSG00000046743; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000155719; -.
DR HOGENOM; CLU_000042_1_0_1; -.
DR InParanoid; Q2PZL6; -.
DR OMA; YREAGGM; -.
DR OrthoDB; 34489at2759; -.
DR PhylomeDB; Q2PZL6; -.
DR TreeFam; TF331335; -.
DR BioGRID-ORCS; 329628; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Fat4; mouse.
DR PRO; PR:Q2PZL6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q2PZL6; protein.
DR Bgee; ENSMUSG00000046743; Expressed in manus and 186 other tissues.
DR Genevisible; Q2PZL6; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IMP:UniProtKB.
DR GO; GO:0072137; P:condensed mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:0048565; P:digestive tract development; IMP:MGI.
DR GO; GO:0001736; P:establishment of planar polarity; IC:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR GO; GO:0035329; P:hippo signaling; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0072006; P:nephron development; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
DR GO; GO:0043931; P:ossification involved in bone maturation; IMP:MGI.
DR GO; GO:0007009; P:plasma membrane organization; IMP:MGI.
DR GO; GO:0072307; P:regulation of metanephric nephron tubule epithelial cell differentiation; IMP:MGI.
DR CDD; cd00110; LamG; 2.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 33.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 34.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; SSF49313; 34.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00232; CADHERIN_1; 22.
DR PROSITE; PS50268; CADHERIN_2; 34.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..4981
FT /note="Protocadherin Fat 4"
FT /id="PRO_0000324638"
FT TOPO_DOM 43..4505
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4506..4526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4527..4981
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..135
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 136..250
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 251..353
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 359..475
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 476..582
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 584..689
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 690..793
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 794..893
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 894..996
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 997..1100
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1101..1210
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1211..1315
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1316..1420
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1421..1529
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1529..1629
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1630..1740
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1741..1841
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1842..1944
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1945..2051
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2051..2154
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2155..2259
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2260..2364
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2365..2468
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2469..2569
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2570..2671
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2672..2775
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2775..2874
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2875..2985
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2986..3091
FT /note="Cadherin 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3092..3196
FT /note="Cadherin 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3197..3300
FT /note="Cadherin 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3301..3406
FT /note="Cadherin 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3407..3512
FT /note="Cadherin 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3511..3622
FT /note="Cadherin 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3804..3862
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3864..3900
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3902..3938
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3940..3976
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3977..4161
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 4164..4200
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4219..4399
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 4427..4464
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4535..4585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4677..4713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4708..4797
FT /note="Necessary and sufficient for interaction with MPDZ"
FT /evidence="ECO:0000269|PubMed:19506035"
FT REGION 4753..4773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4796..4911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4957..4981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4535..4556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4677..4705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4813..4827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4849..4865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4875..4891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1085
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3038
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3808..3819
FT /evidence="ECO:0000250"
FT DISULFID 3813..3850
FT /evidence="ECO:0000250"
FT DISULFID 3852..3861
FT /evidence="ECO:0000250"
FT DISULFID 3868..3879
FT /evidence="ECO:0000250"
FT DISULFID 3873..3888
FT /evidence="ECO:0000250"
FT DISULFID 3890..3899
FT /evidence="ECO:0000250"
FT DISULFID 3906..3917
FT /evidence="ECO:0000250"
FT DISULFID 3911..3926
FT /evidence="ECO:0000250"
FT DISULFID 3928..3937
FT /evidence="ECO:0000250"
FT DISULFID 3944..3955
FT /evidence="ECO:0000250"
FT DISULFID 3949..3964
FT /evidence="ECO:0000250"
FT DISULFID 3966..3975
FT /evidence="ECO:0000250"
FT DISULFID 4135..4161
FT /evidence="ECO:0000250"
FT DISULFID 4168..4179
FT /evidence="ECO:0000250"
FT DISULFID 4173..4188
FT /evidence="ECO:0000250"
FT DISULFID 4190..4199
FT /evidence="ECO:0000250"
FT DISULFID 4366..4399
FT /evidence="ECO:0000250"
FT DISULFID 4431..4442
FT /evidence="ECO:0000250"
FT DISULFID 4436..4452
FT /evidence="ECO:0000250"
FT DISULFID 4454..4463
FT /evidence="ECO:0000250"
FT VAR_SEQ 1975..1978
FT /note="VNSQ -> MSFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032339"
FT VAR_SEQ 1979..4981
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032340"
FT CONFLICT 1481
FT /note="S -> N (in Ref. 1; ABB88946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4981 AA; 540316 MW; D0436BAC3162CFD2 CRC64;
MNLAANRAPG RRRLPLPSPS LCQLLRVWGL LSLLPGSARV QAAEQRQVFQ VMEEQPPGTL
VGTIPTRPGF TYRLSESHAL FAINSSTGAL YTTATIDRES LPSDVVNLVV LSSSPTYPTE
VRVLVRDLND NAPVFPDPSI VVTFKEDSGS GRQVILDTAT DSDIGSNGVD HHSYRIVSGN
EAGRFRLDIT LNPSGEGAFL HLVSKGGLDR EVTPQYQLLV EVEDKGEPKR RGYLQVNVTV
QDINDNPPVF GSSHYQAGVP EDAVVGSSVL QVAAADADEG TNADIRYRLQ DEGTPFQMDP
ETGLITVREP LDFEARRQYS LTVQATDRGV PSLTGRAEAF IQLLDVNDND PVVKFRYFPA
TSRYASVDEN AQVGTVVALL TVTDADSPAA NGNISVQILG GNEQRHFEVQ RSKVPNLSLI
KVASALDRER IPSYNLTVSV SDNSGAPPTA EVQARSSVAS LVIFVNDIND HPPVFEQQVY
RVNLSEEVPP GSYVSGVSAT DGDSGLNANL RYSIVSGNGL GWFHISEHSG LVTTSAAGGL
DRELASQIVL NISARDQGVH PKVSYAQLVV TVLDVNDEKP VFSQPEGYEV SVVENAPTGT
ELLVLGATDR DLGDNGTVRF SLQEAENDQR LFRLDPVSGR LSTASSLDRE EQAFYCLSIL
ATDLGSPPQS STAQVNVSLL DINDNSPVFY PVQYFAHIQE NEPGGSYVTT VSATDPDMGP
NGTVKYSISA GDRSRFQIHA KSGVISTKMA LDREEKTAYQ LQVVATDGGN LQSPNQAIVT
VTVLDTQDNP PVFSQAAYSF VVFENVALGY HVGSVSATTM DLNANISYLI TTGDQRGMFA
MNPVTGQLTT ASVIDREEQS FYQLKIVASG GAVTGDTVVN ITVKDLNDNA PHFLQAVESI
NAVENWQAGH SIFQAKAVDP DEGVNGRVLY SLKQNPKNLF TINEQNGNIS LLGALDVHAG
SYQVEIVASD MGVPQLSSSI LLTVYVHDVN DNPPVFDQIS YEVTLSESEP VNSRFFKVQA
SDKDSGANGE IAYTITDGNN GDAFGIFPDG QLYIKSELDR ELQDRYVLLV VASDRAVEPL
SATVNVTVLL EDVNDNRPLF NSTNYTFYFE EEQRAGSFVG KVSAVDKDFG PNGEVRYAFE
VTQPNFELHA VTGEITSTHK FDRESLMRRR GTAVFSFTVT AMDRGLPQPL KDQATVHVYM
KDINDNAPKF LKDFYQATVS ETATNLTQVL RVSASDVDEG SNGLIHYSIL KGNEERQFAI
DSFSGQVTLV GKLDYEATSA YSLLIQAVDS GAIPLNSTCT LSIDILDEND NTPSFPKSTL
FVDVLENMRI GELVSSVTAT DSDSGVNADL HYTITGSNNH GTFSISPNTG SIFLAKKLDF
ETQSLYKLNI TAKDQGRPPR SSTMSVVIQV RDFNDNPPSF PPGDIFKSIV ENIPLGTSVI
SVTAHDPDAD INGQLSYAII QQMPRGNHFS IDEVKGTIYT SAEIDREFAN LFELTVKAND
QAVPIETRRY ALKNVTILVT DLNDNVPMFI SQNALAADPS AMIGSVLTTI MAADPDEGAN
GEVEYEILNG DTDTFTVDRY SGDLRVASAL VPSQLIYNLI VSATDLGPER RKSTTELTVI
LQGLDGPVFT QTKYITILKE GEPIGTNVIS IEAASPRGSE APVEYYIVSV RCEEKTVGRL
FTIGRQTGVI QTAAILDREQ GACLYLVDVY AIEKSSAFPR TQRAEVEITL QDINDNPPVF
PTDTLDLTVE ENIGDGSKIM QLTAMDADEG ANALVTYALI SGADDSFRID PESGDLIATK
RLDREHRSKY SLLVRADDGL QSSDMRINIT ISDVNDHTPR FSRPVYSFDI PEDTTPGSLV
AAILATDDDS GVNGEISYVV EEDDGDGVFF LNLVTGVFNL TRALDYETQQ YYILTVRAED
GGGQSTTIRA YFNILDVNDN PPVFSMSSYS TSLMENLPLG STVLVFNVTD ADDGVNSQLS
YSIASGDSLG QFAVDKHGVL KTLKALDRES QSFYNLVIQV HDLPQPPTSR FTSTAQVSII
LLDVNDNPPM FLSPKLTYIP ENTPIDTVVF KAQATDPDSG PNSYIEYTLL NPSGNKFSIG
TIDGEVHLTG ELDREEVSNY SLTVVATDKG QPPLSSSTEV VVMVLDINDN NPVFAQAMYR
VQIKENILTG TDIIQVSAAD NDEGTNGQVR YGIVGGNTHQ EFRIDSVTGA ITVAKSLDRE
TTPAYTLTVQ ATDRGSSPRT DSCTVAITLL DMNDFVPVFE LSPYSVNVPE NLGTLPRAIL
QVVARDDDQG PNSQLSYVLL GGNEDNAFVL TASGELRVTQ SLDREARDHF VLVVTAADAG
SPALTGTGTI NIIVDDINDN VPTFANNMYL TSIAEDARTG TDVLLVNASD ADAAANAVIS
YSIIGGNSQF TINPSTGQII TSALLDRETK DNYTLVVVAS DAGSPESLSS STSVLVTITD
VNDNPPRFQH HPYVTHIPSP TPPGSFVFAV TVTDADIGSN SELHYSLSGR NSEKFHIDPL
RGAIMAAGPL SGASEVTFSV HVKDGGSFPK TDSTTVTVRF ANKADFPKVR AKEQTFMFPE
NQPVGTLVTT ITGSSLRGET LSYYIASGNL GDTFQIDPLT GQVSISQPLD FEKIQKYVVW
IEARDGGFPP FSSYEKLDIT VLDINDNAPT FEEDPFVSEI LENLSPRKIL TVSATDKDSG
PNGQLDYEIV NGNQESSFTI NHATGEIRSI RPLDREKISH YELTVKSSDK GSPSQSTSVK
VIISILDEND NAPRFSQIFS AYVSENSPLG YTVTRVTTSD EDIGINAISR YSIVDTSLPF
TINPNTGDIV ISRPLNREDT DRYRIRVSAH DSGWTVSTDV TIFVTDINDN TPRFSRPSYY
LDCPELPELG SRVTQVSATD PDEGSNGQVF YFIKSQSEYF RINATTGEIF NKQVLKYQNV
SGFSNVNINR HSFIVTASDR GNPSLLSETT VTINTVDSND NPPQFLQNKY FTPVTKNVKV
GTKLIKVTAV DDKDFGLNSE VEYFVSDGNH LGKFKLDNDT GWISIASSLV SDLNQNFLIR
VTAKDKGNPP LSSQAVVHIT VTEENYHTPE FSQNHISATI PESHSIGSVV RTVSARDRDT
AMNGLISYNI ISGNEEGIFA INSSTGVVTL AKALDYEMSS KHEMTISATD GGWVARTGYC
SLTVSVIDVN DNSPVFVPDE FFPTVMENAP SGTTVIHLNA TDADSGANAV IAYTVQSSDS
DLFVIDPNMG VITTQGFLDF ETKQSYHLTV KAFNVPDEEK CSFATVDIQL KGTNEYVPRF
VSKLYYFEVS EAASRGTAVG EVFASDRDMG ADGEVHYLIF GNSRKKGFQI NKMTGQIYVS
GLLDREKEER VSLKVLAKNF GNIRGADIDE VTVNITVLDA NDPPVFSLST YRVQISEGVP
IGTHVTFVSA FDSDSIPSWS RFSYFIGSGN ENGAFSINPQ TGQITVTSGL DRESLPVYNL
TVLAVDSGTP SATGSASLVV TLEDINDNGP VLTVSEGEVL ENKRPGTLVM TLQSTDPDLP
PNQGPFNYYL LSTGPATNYF SLSTAGVLST TREIDREQIA DFYLSVVTRD SGAPQMSSTG
TVHITVLDQN DNPSQSRTVE IFVNYYGNLF PGGTLGSVKP QDPDVLDSFH CSLTSGVTSL
FSIPAGSCDL SSQPRSTDGT FDLTVVSSDG VHSTVTNNIR VFFAGFSNAT IDNSILLRVG
VPTVKDFLTN HYLHFLRIAS SQLTGLGTAV QLYAAYEENN RTFLLAAVKR NNNQYVNPSG
VATFFESIKE ILLRQSGVKV ESVDHDPCIH GPCQNGGSCL RRLAVGSALK IQESLPVIIV
ANEPLQPSQC KCVPGYAGSW CEVDIDECLP APCHNGGTCH NLVGGFSCSC PEGFTGRACE
RDINECLPSP CKHGAVCQNF PGGFNCVCKT GYTGKMCESS VNYCECNPCF NGGSCQSGVE
SYYCHCPFGV FGKHCELNSY GFEELSYMEF PSLDPNNNYI YVKFATIKSH ALLLYNYDNQ
TGERAEFLAL EIAEERLRFS YNLGSGTYKL TTMKKVSDGQ FHTVIARRAG MAASLTVDSC
SENQEPGYCT VSNVAVSDDW TLDVQPNRVT VGGIRSLEPI LQRRGHVESH DFVGCVMEFA
VNGRPLEPSQ ALAAQGILDQ CPRLEGTCAR NPCQHGGTCV DFWSWQQCQC MEGLTGKYCE
KSVTPDTALS LEGKGRLDYH MSQSEKREYL LTQSIRDTTL EPFGVNSLEV KFRTRSENGI
LIHIQESSNY TTVKIKNGKV HFTSDAGVAG KVERIIPEAY IADGHWHTFR ISKNGSITVL
SVDRIHNRDI VHPTQDFGGI EVLSMSLGGI PPNQAHRDTQ TGFNGCIASV LYGGESLPFS
GKHSLASISK TDPSVKIGCR GPNICASNPC WGDLLCINQW YAYKCVPPGD CASHPCQNGG
SCEPGLLSGY TCSCPESHTG RTCETVVACL GVLCPQGKVC KAGSPGGHVC VQSQGPDEIS
LPLWAVPAIV GSCATALALL VLSLILCNQC RGKMPKNPKE EKKPKEKKKK GSENVAFDDP
DNIPPYGDDL AVRKQPEGNP KPDIIERENP YLIFDETDIP HNSETIPSAP LASPEQEIEH
YDIDNASSIA PSDADIIQHY KQFRSHTPKF SIQRHSPLGF ARQSPMPLGA SSLTYQPSSY
GQGLRTSSLS HSACPTPNPL SRHSPAPFSK PSAFYRNSPA RELHLPLRDG GTLEMHGDPC
QPGMFNYATR LGRRSKSPQA MASHGSRPGS RLKQPIAQIP LESSPPVGLS IEEVERLNTP
RPRNPSICSA DHGRSSSEED CRRPLSRTRN PADGIPAPES SSDSDSHDSF TCSEMEYDRE
KPVVYTSRMP KLSQVNESDA DDEDNYGARL KPRRYHGRRA EGGPVGTPAA ASGAADSTLK
LGQQAGNFNW DNLLNWGPGF GHYVDVFKDL ASLPEKAAGN EEGKSGAAKP AAKDGEAEQY
V
