CADE_DROME
ID CADE_DROME Reviewed; 1507 AA.
AC Q24298; Q9W2N1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=DE-cadherin;
DE AltName: Full=Protein shotgun;
DE Flags: Precursor;
GN Name=shg {ECO:0000312|FlyBase:FBgn0003391};
GN Synonyms=E-cadherin {ECO:0000312|FlyBase:FBgn0003391};
GN ORFNames=CG3722 {ECO:0000312|FlyBase:FBgn0003391};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=7958432; DOI=10.1006/dbio.1994.1287;
RA Oda H., Uemura T., Harada Y., Iwai Y., Takeichi M.;
RT "A Drosophila homolog of cadherin associated with armadillo and essential
RT for embryonic cell-cell adhesion.";
RL Dev. Biol. 165:716-726(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1493, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [5]
RP INTERACTION WITH INX2.
RX PubMed=15047872; DOI=10.1091/mbc.e04-01-0056;
RA Bauer R., Lehmann C., Martini J., Eckardt F., Hoch M.;
RT "Gap junction channel protein innexin 2 is essential for epithelial
RT morphogenesis in the Drosophila embryo.";
RL Mol. Biol. Cell 15:2992-3004(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=16831834; DOI=10.1242/dev.02467;
RA Murray M.J., Davidson C.M., Hayward N.M., Brand A.H.;
RT "The Fes/Fer non-receptor tyrosine kinase cooperates with Src42A to
RT regulate dorsal closure in Drosophila.";
RL Development 133:3063-3073(2006).
RN [7]
RP INTERACTION WITH HAKAI.
RX PubMed=19682089; DOI=10.1111/j.1365-2443.2009.01335.x;
RA Kaido M., Wada H., Shindo M., Hayashi S.;
RT "Essential requirement for RING finger E3 ubiquitin ligase Hakai in early
RT embryonic development of Drosophila.";
RL Genes Cells 14:1067-1077(2009).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP MYO31DF.
RX PubMed=22491943; DOI=10.1242/dev.047589;
RA Petzoldt A.G., Coutelis J.B., Geminard C., Speder P., Suzanne M.,
RA Cerezo D., Noselli S.;
RT "DE-Cadherin regulates unconventional Myosin ID and Myosin IC in Drosophila
RT left-right asymmetry establishment.";
RL Development 139:1874-1884(2012).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24855950; DOI=10.1016/j.cell.2014.03.045;
RA Cai D., Chen S.C., Prasad M., He L., Wang X., Choesmel-Cadamuro V.,
RA Sawyer J.K., Danuser G., Montell D.J.;
RT "Mechanical feedback through E-cadherin promotes direction sensing during
RT collective cell migration.";
RL Cell 157:1146-1159(2014).
RN [10]
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=24681004; DOI=10.1016/j.ydbio.2014.03.007;
RA Zhang Y., Kong D., Reichl L., Vogt N., Wolf F., Grosshans J.;
RT "The glucosyltransferase Xiantuan of the endoplasmic reticulum specifically
RT affects E-Cadherin expression and is required for gastrulation movements in
RT Drosophila.";
RL Dev. Biol. 390:208-220(2014).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30763317; DOI=10.1371/journal.pgen.1007720;
RA Raza Q., Choi J.Y., Li Y., O'Dowd R.M., Watkins S.C., Chikina M., Hong Y.,
RA Clark N.L., Kwiatkowski A.V.;
RT "Evolutionary rate covariation analysis of E-cadherin identifies Raskol as
RT a regulator of cell adhesion and actin dynamics in Drosophila.";
RL PLoS Genet. 15:E1007720-E1007720(2019).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins
CC (PubMed:7958432). In connecting cells they preferentially interact with
CC themselves in a homophilic manner; cadherins may thus contribute to the
CC sorting of heterogeneous cell types (PubMed:7958432). During oogenesis,
CC integral component of the guidance mechanisms that regulate the
CC directional persistent collective migration of the border cell (BC)
CC cluster through the nurse cells to the oocyte (PubMed:24855950,
CC PubMed:30763317). Functions downstream of the two chemoattractant
CC receptors, Pvr and Egfr, to promote BC adhesion between the leader
CC cells of the migrating cluster and the surrounding nurse cells
CC (PubMed:24855950). This adhesion increases Rac1 signaling in the
CC leading cells, which in turn stabilizes DE-cadherin/DE-cadherin
CC adhesions through the formation of forward-directed protrusions which
CC attach/detach to the surrounding nurse cells in order to pull the
CC cluster through the egg chamber to the oocyte (PubMed:24855950). Within
CC the BC cluster, also promotes adhesion between BCs, and between BCs and
CC polar cells which enables the lead BC to communicate direction to the
CC other cells in the cluster, providing polarity to each individual cell
CC and ensuring collective behavior (PubMed:24855950, PubMed:30763317).
CC May function in cell intercalation in the lateral epidermis during
CC germband extension (PubMed:24681004). Contributes to the determination
CC of body left-right asymmetry by enhancing Myo31DF activity and
CC inhibiting Myo61F activity (PubMed:22491943).
CC {ECO:0000269|PubMed:22491943, ECO:0000269|PubMed:24681004,
CC ECO:0000269|PubMed:24855950, ECO:0000269|PubMed:30763317,
CC ECO:0000269|PubMed:7958432}.
CC -!- SUBUNIT: Interacts (via cytoplasmic region) with Inx2 (via cytoplasmic
CC loop) (PubMed:15047872). Interacts with Hakai (PubMed:19682089).
CC Interacts with Myo31DF (PubMed:22491943). {ECO:0000269|PubMed:15047872,
CC ECO:0000269|PubMed:19682089, ECO:0000269|PubMed:22491943}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22491943};
CC Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane
CC {ECO:0000269|PubMed:30763317}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=In stage 8 embryos (before border cell (BC)
CC delimination), and during BC migration, colocalizes with raskol at the
CC cell membranes of BCs and polar cells (PCs), and is enriched at the PC
CC apical membrane. Also colocalizes with raskol in the aminoserosa cell
CC contacts and the dorsal most ectodermal cells at the zippering
CC interface. {ECO:0000269|PubMed:30763317}.
CC -!- TISSUE SPECIFICITY: In early stage 9 and stage 10 oocytes, expressed in
CC border cells, strongly expressed in polar cells and very weakly
CC expressed in the nurse cells (at protein level) (PubMed:24855950). In
CC the embryo, expressed in the leading edge cells of the dorsal epidermis
CC (at protein level) (PubMed:16831834, PubMed:30763317). Stage 10 embryos
CC exhibit intense expression in epithelial cells (PubMed:7958432). Stage
CC 14 embryos show expression in the hindgut (at the apical poles of cell-
CC cell boundaries), at the apical junctions of tracheal cells and in the
CC dorsal longitudinal trunk (PubMed:7958432). In stage 16 embryos the
CC glial midline cells of the central nervous system show strong
CC expression (PubMed:7958432). {ECO:0000269|PubMed:16831834,
CC ECO:0000269|PubMed:24855950, ECO:0000269|PubMed:30763317,
CC ECO:0000269|PubMed:7958432}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain.
CC {ECO:0000250|UniProtKB:P12830}.
CC -!- PTM: N-glycosylation is important for biosynthesis and function.
CC {ECO:0000269|PubMed:24681004}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in segment A8 of the male
CC genital disk causes loss of the normal dextral rotation of the genital
CC plate and results in a phenotype with no rotation (PubMed:22491943).
CC During oocyte border cell migration, RNAi-mediated knockdown in either
CC the border cells (BC) or in the surrounding nurse cells results in
CC various BC migration defects such as BC deviating from their migration
CC path or failing to sustain the directed, posterior movement
CC (PubMed:30763317, PubMed:24855950). RNAi-mediated knockdown in the
CC outer migratory BC disrupts distribution of Rac1 in the BC cluster but
CC does not affect motility and cells remain clustered (PubMed:24855950).
CC RNAi-mediated knockdown in oocyte polar cells (PCs) results in BC
CC cluster dissociation in 80 percent of egg chambers (PubMed:30763317).
CC {ECO:0000269|PubMed:22491943, ECO:0000269|PubMed:24855950,
CC ECO:0000269|PubMed:30763317}.
CC -!- MISCELLANEOUS: Overexpression in segment A8 of the male genital disk
CC has no effect on the normal dextral rotation of the genital plate.
CC {ECO:0000269|PubMed:22491943}.
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DR EMBL; D28749; BAA05942.1; -; mRNA.
DR EMBL; AE013599; AAF46659.1; -; Genomic_DNA.
DR RefSeq; NP_476722.1; NM_057374.3.
DR AlphaFoldDB; Q24298; -.
DR SMR; Q24298; -.
DR BioGRID; 63025; 89.
DR DIP; DIP-22198N; -.
DR IntAct; Q24298; 4.
DR STRING; 7227.FBpp0071475; -.
DR GlyGen; Q24298; 11 sites.
DR iPTMnet; Q24298; -.
DR PaxDb; Q24298; -.
DR PRIDE; Q24298; -.
DR EnsemblMetazoa; FBtr0071546; FBpp0071475; FBgn0003391.
DR GeneID; 37386; -.
DR KEGG; dme:Dmel_CG3722; -.
DR CTD; 37386; -.
DR FlyBase; FBgn0003391; shg.
DR VEuPathDB; VectorBase:FBgn0003391; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000172755; -.
DR HOGENOM; CLU_247555_0_0_1; -.
DR InParanoid; Q24298; -.
DR OMA; EQPENTY; -.
DR OrthoDB; 6237at2759; -.
DR PhylomeDB; Q24298; -.
DR SignaLink; Q24298; -.
DR BioGRID-ORCS; 37386; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37386; -.
DR PRO; PR:Q24298; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003391; Expressed in presumptive embryonic/larval digestive system (Drosophila) and 128 other tissues.
DR Genevisible; Q24298; DM.
DR GO; GO:0005912; C:adherens junction; IDA:FlyBase.
DR GO; GO:0043296; C:apical junction complex; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016342; C:catenin complex; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0030175; C:filopodium; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:FlyBase.
DR GO; GO:0005914; C:spot adherens junction; IDA:FlyBase.
DR GO; GO:0008013; F:beta-catenin binding; IPI:CAFA.
DR GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
DR GO; GO:0017022; F:myosin binding; IPI:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
DR GO; GO:0008356; P:asymmetric cell division; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0007420; P:brain development; IMP:FlyBase.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IMP:FlyBase.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
DR GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0030031; P:cell projection assembly; IMP:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:FlyBase.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IDA:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0050832; P:defense response to fungus; IMP:FlyBase.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IMP:FlyBase.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0010004; P:gastrulation involving germ band extension; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:FlyBase.
DR GO; GO:0007506; P:gonadal mesoderm development; IMP:FlyBase.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; IGI:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:FlyBase.
DR GO; GO:0001748; P:insect visual primordium development; IMP:FlyBase.
DR GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IMP:FlyBase.
DR GO; GO:0098730; P:male germline stem cell symmetric division; IMP:FlyBase.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
DR GO; GO:0030720; P:oocyte localization involved in germarium-derived egg chamber formation; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IGI:FlyBase.
DR GO; GO:0007379; P:segment specification; IMP:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
DR GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR GO; GO:0045186; P:zonula adherens assembly; IMP:FlyBase.
DR CDD; cd00110; LamG; 1.
DR DisProt; DP00269; -.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 7.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; SSF49313; 8.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 7.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..69
FT /evidence="ECO:0000255"
FT PROPEP 70..261
FT /evidence="ECO:0000255"
FT /id="PRO_0000003879"
FT CHAIN 262..1507
FT /note="DE-cadherin"
FT /id="PRO_0000003880"
FT TOPO_DOM 262..1328
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1329..1349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1350..1507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 97..195
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 204..301
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 311..412
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 420..522
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 532..633
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 631..733
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 741..835
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1084..1123
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1125..1313
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1350..1507
FT /note="Interaction with Inx2"
FT REGION 1488..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1493
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 983
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 999
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1073
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1098..1112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1114..1123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1287..1313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CONFLICT 974
FT /note="L -> F (in Ref. 1; BAA05942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1507 AA; 169821 MW; DF2B5CAAA29D8EE5 CRC64;
MSTSVQRMSR SYHCINMSAT PQAGHLNPAQ QQTHQQHKRK CRDLGRRLIP ARLLLGVIVA
ISLLSPALAL HSPPDKNFSG DNRKPAFKNC AGYAPKVKEE QPENTYVLTV EAVDPDPDQV
IRYSIVQSPF ERPKFFINPS TGVIFTTHTF DRDEPIHEKF VFVTVQATDN GLPPLDDVCT
FNVTIEDIND NAPAFNKARY DESMSENAQP DAVVMTISAS DFDDGNNSLV EYEILRERDF
QYFKIDKESG IIYLKRPIDK RPGQSYAIIV RAYNVVPDPP QDAQIEVRIR VVESSIKPPS
FVNPIDTPIY LKENLKNFTH PIATLRAVSN MPDKPEVIFE LNTGRTEQTN SKNTFVFNQI
GNEVTISLGK TLDYEAITDY TLTMIVRNTH ELGTEHQIKI QVEDVNDNIP YYTEVKSGTI
LENEPPGTPV MQVRAFDMDG TSANNIVSFE LADNREYFTI DPNTGNITAL TTFDREERDF
YNVKVIASDN SPSSLFDNGE PNRGHQVFRI SIGDKNDHKP HFQQDKYLAE RLLEDANTNT
EVIEVKAEDE DNASQILYSI ESGNVGDAFK IGLKTGKITV NQKLDYETIT EYELKVRAFD
GIYDDYTTVV IKIEDVNDNP PVFKQDYSVT ILEETTYDDC ILTVEAYDPD IKDRNADQHI
VYSIHQNDGN RWTIDNSGCL RLVKTLDRDP PNGHKNWQVL IKANDEDGVG TTVSTVKEVT
VTLKDINDNA PFLINEMPVY WQENRNPGHV VQLQANDYDD TPGAGNFTFG IDSEATPDIK
TKFSMDGDYL HANVQFDREA QKEYFIPIRI SDSGVPRQSA VSILHLVIGD VNDNAMSEGS
SRIFIYNYKG EAPETDIGRV FVDDLDDWDL EDKYFEWKDL PHDQFRLNPS TGMITMLVHT
AEGEYDLSFV VTEDSMFVPR HSVDAYVTVV VRELPEEAVD KSGSIRFINV TKEEFISVPR
DFQSPDALSL KDRLQLSLAK LFNTSVSNVD VFTVLQNENH TLDVRFSAHG SPYYAPEKLN
GIVAQNQQRL ENELDLQMLM VNIDECLIEK FKCEESCTNE LHKSSVPYMI YSNTTSFVGV
NAFVQAQCVC EAPLMRRCLN GGSPRYGEND VCDCIDGFTG PHCELVSVAF YGSGYAFYEP
IAACNNTKIS LEITPQIDQG LIMYLGPLNF NPLLAISDFL ALELDNGYPV LTVDYGSGAI
RIRHQHIKMV ADRTYQLDII LQRTSIEMTV DNCRLSTCQT LGAPIGPNEF LNVNAPLQLG
GTPVDLEQLG RQLNWTHVPN QKGFFGCIRN LTINEQTYNL GMPSVFRNID SGCQQSVAVA
FSFGIDRNFI IAIIVCLALL LIILLAVVVQ KKQKNGWHEK DIDDIRETII NYEDEGGGER
DTDYDLNVLR TQPFYEEKLY KDPHALQGNM RDPNDIPDIA DFLGDKKENC DRDVGATTVD
DVRHYAYEGD GNSDGSLSSL ASCTDDGDLN FDYLSNFGPR FRKLADMYGE EPSDTDSNVD
DDQGWRI
