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Entry version 194 (17 Jun 2020)
Sequence version 2 (01 Jun 2000)
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Protein

DE-cadherin

Gene

shg

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cadherins are calcium-dependent cell adhesion proteins (PubMed:7958432). In connecting cells they preferentially interact with themselves in a homophilic manner; cadherins may thus contribute to the sorting of heterogeneous cell types (PubMed:7958432). During oogenesis, integral component of the guidance mechanisms that regulate the directional persistent collective migration of the border cell (BC) cluster through the nurse cells to the oocyte (PubMed:24855950, PubMed:30763317). Functions downstream of the two chemoattractant receptors, Pvr and Egfr, to promote BC adhesion between the leader cells of the migrating cluster and the surrounding nurse cells (PubMed:24855950). This adhesion increases Rac1 signaling in the leading cells, which in turn stabilizes DE-cadherin/DE-cadherin adhesions through the formation of forward-directed protrusions which attach/detach to the surrounding nurse cells in order to pull the cluster through the egg chamber to the oocyte (PubMed:24855950). Within the BC cluster, also promotes adhesion between BCs, and between BCs and polar cells which enables the lead BC to communicate direction to the other cells in the cluster, providing polarity to each individual cell and ensuring collective behavior (PubMed:24855950, PubMed:30763317). May function in cell intercalation in the lateral epidermis during germband extension (PubMed:24681004). Contributes to the determination of body left-right asymmetry by enhancing Myo31DF activity and inhibiting Myo61F activity (PubMed:22491943).5 Publications

Miscellaneous

Overexpression in segment A8 of the male genital disk has no effect on the normal dextral rotation of the genital plate.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion
LigandCalcium, Metal-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DE-cadherin
Alternative name(s):
Protein shotgun
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:shgImported
Synonyms:E-cadherinImported
ORF Names:CG3722Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2R

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0003391 shg

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini262 – 1328ExtracellularSequence analysisAdd BLAST1067
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1329 – 1349HelicalSequence analysisAdd BLAST21
Topological domaini1350 – 1507CytoplasmicSequence analysisAdd BLAST158

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

RNAi-mediated knockdown in segment A8 of the male genital disk causes loss of the normal dextral rotation of the genital plate and results in a phenotype with no rotation (PubMed:22491943). During oocyte border cell migration, RNAi-mediated knockdown in either the border cells (BC) or in the surrounding nurse cells results in various BC migration defects such as BC deviating from their migration path or failing to sustain the directed, posterior movement (PubMed:30763317, PubMed:24855950). RNAi-mediated knockdown in the outer migratory BC disrupts distribution of Rac1 in the BC cluster but does not affect motility and cells remain clustered (PubMed:24855950). RNAi-mediated knockdown in oocyte polar cells (PCs) results in BC cluster dissociation in 80 percent of egg chambers (PubMed:30763317).3 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 69Sequence analysisAdd BLAST69
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000387970 – 261Sequence analysisAdd BLAST192
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000003880262 – 1507DE-cadherinAdd BLAST1246

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi317N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi466N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi552N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi766N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi949N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi983N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi999N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1073N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi1098 ↔ 1112PROSITE-ProRule annotation
Disulfide bondi1114 ↔ 1123PROSITE-ProRule annotation
Glycosylationi1145N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1274N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1287 ↔ 1313PROSITE-ProRule annotation
Glycosylationi1290N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1493Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylation is important for biosynthesis and function.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q24298

PRoteomics IDEntifications database

More...
PRIDEi
Q24298

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q24298

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

In early stage 9 and stage 10 oocytes, expressed in border cells, strongly expressed in polar cells and very weakly expressed in the nurse cells (at protein level) (PubMed:24855950). In the embryo, expressed in the leading edge cells of the dorsal epidermis (at protein level) (PubMed:16831834, PubMed:30763317). Stage 10 embryos exhibit intense expression in epithelial cells (PubMed:7958432). Stage 14 embryos show expression in the hindgut (at the apical poles of cell-cell boundaries), at the apical junctions of tracheal cells and in the dorsal longitudinal trunk (PubMed:7958432). In stage 16 embryos the glial midline cells of the central nervous system show strong expression (PubMed:7958432).4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0003391 Expressed in imaginal disc and 107 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q24298 DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts (via cytoplasmic region) with Inx2 (via cytoplasmic loop) (PubMed:15047872).

Interacts with Hakai (PubMed:19682089).

Interacts with Myo31DF (PubMed:22491943).

3 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
63025, 87 interactors

Database of interacting proteins

More...
DIPi
DIP-22198N

Protein interaction database and analysis system

More...
IntActi
Q24298, 4 interactors

STRING: functional protein association networks

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STRINGi
7227.FBpp0071475

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q24298

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini97 – 195Cadherin 1PROSITE-ProRule annotationAdd BLAST99
Domaini204 – 301Cadherin 2PROSITE-ProRule annotationAdd BLAST98
Domaini311 – 412Cadherin 3PROSITE-ProRule annotationAdd BLAST102
Domaini420 – 522Cadherin 4PROSITE-ProRule annotationAdd BLAST103
Domaini532 – 633Cadherin 5PROSITE-ProRule annotationAdd BLAST102
Domaini631 – 733Cadherin 6PROSITE-ProRule annotationAdd BLAST103
Domaini741 – 835Cadherin 7PROSITE-ProRule annotationAdd BLAST95
Domaini1084 – 1123EGF-likePROSITE-ProRule annotationAdd BLAST40
Domaini1125 – 1313Laminin G-likePROSITE-ProRule annotationAdd BLAST189

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1350 – 1507Interaction with Inx2Add BLAST158

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.By similarity

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1219 Eukaryota
ENOG410XPEI LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000172755

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_247555_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q24298

Identification of Orthologs from Complete Genome Data

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OMAi
DFYNVKV

Database of Orthologous Groups

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OrthoDBi
6237at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q24298

Family and domain databases

Database of protein disorder

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DisProti
DP00269

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
4.10.900.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002126 Cadherin-like_dom
IPR015919 Cadherin-like_sf
IPR020894 Cadherin_CS
IPR000233 Cadherin_cytoplasmic-dom
IPR027397 Catenin_binding_dom_sf
IPR013320 ConA-like_dom_sf
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR001791 Laminin_G

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00028 Cadherin, 5 hits
PF01049 Cadherin_C, 1 hit
PF02210 Laminin_G_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00205 CADHERIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00112 CA, 7 hits
SM00282 LamG, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49313 SSF49313, 8 hits
SSF49899 SSF49899, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00232 CADHERIN_1, 5 hits
PS50268 CADHERIN_2, 7 hits
PS00022 EGF_1, 1 hit
PS01186 EGF_2, 1 hit
PS50026 EGF_3, 1 hit
PS50025 LAM_G_DOMAIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q24298-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTSVQRMSR SYHCINMSAT PQAGHLNPAQ QQTHQQHKRK CRDLGRRLIP
60 70 80 90 100
ARLLLGVIVA ISLLSPALAL HSPPDKNFSG DNRKPAFKNC AGYAPKVKEE
110 120 130 140 150
QPENTYVLTV EAVDPDPDQV IRYSIVQSPF ERPKFFINPS TGVIFTTHTF
160 170 180 190 200
DRDEPIHEKF VFVTVQATDN GLPPLDDVCT FNVTIEDIND NAPAFNKARY
210 220 230 240 250
DESMSENAQP DAVVMTISAS DFDDGNNSLV EYEILRERDF QYFKIDKESG
260 270 280 290 300
IIYLKRPIDK RPGQSYAIIV RAYNVVPDPP QDAQIEVRIR VVESSIKPPS
310 320 330 340 350
FVNPIDTPIY LKENLKNFTH PIATLRAVSN MPDKPEVIFE LNTGRTEQTN
360 370 380 390 400
SKNTFVFNQI GNEVTISLGK TLDYEAITDY TLTMIVRNTH ELGTEHQIKI
410 420 430 440 450
QVEDVNDNIP YYTEVKSGTI LENEPPGTPV MQVRAFDMDG TSANNIVSFE
460 470 480 490 500
LADNREYFTI DPNTGNITAL TTFDREERDF YNVKVIASDN SPSSLFDNGE
510 520 530 540 550
PNRGHQVFRI SIGDKNDHKP HFQQDKYLAE RLLEDANTNT EVIEVKAEDE
560 570 580 590 600
DNASQILYSI ESGNVGDAFK IGLKTGKITV NQKLDYETIT EYELKVRAFD
610 620 630 640 650
GIYDDYTTVV IKIEDVNDNP PVFKQDYSVT ILEETTYDDC ILTVEAYDPD
660 670 680 690 700
IKDRNADQHI VYSIHQNDGN RWTIDNSGCL RLVKTLDRDP PNGHKNWQVL
710 720 730 740 750
IKANDEDGVG TTVSTVKEVT VTLKDINDNA PFLINEMPVY WQENRNPGHV
760 770 780 790 800
VQLQANDYDD TPGAGNFTFG IDSEATPDIK TKFSMDGDYL HANVQFDREA
810 820 830 840 850
QKEYFIPIRI SDSGVPRQSA VSILHLVIGD VNDNAMSEGS SRIFIYNYKG
860 870 880 890 900
EAPETDIGRV FVDDLDDWDL EDKYFEWKDL PHDQFRLNPS TGMITMLVHT
910 920 930 940 950
AEGEYDLSFV VTEDSMFVPR HSVDAYVTVV VRELPEEAVD KSGSIRFINV
960 970 980 990 1000
TKEEFISVPR DFQSPDALSL KDRLQLSLAK LFNTSVSNVD VFTVLQNENH
1010 1020 1030 1040 1050
TLDVRFSAHG SPYYAPEKLN GIVAQNQQRL ENELDLQMLM VNIDECLIEK
1060 1070 1080 1090 1100
FKCEESCTNE LHKSSVPYMI YSNTTSFVGV NAFVQAQCVC EAPLMRRCLN
1110 1120 1130 1140 1150
GGSPRYGEND VCDCIDGFTG PHCELVSVAF YGSGYAFYEP IAACNNTKIS
1160 1170 1180 1190 1200
LEITPQIDQG LIMYLGPLNF NPLLAISDFL ALELDNGYPV LTVDYGSGAI
1210 1220 1230 1240 1250
RIRHQHIKMV ADRTYQLDII LQRTSIEMTV DNCRLSTCQT LGAPIGPNEF
1260 1270 1280 1290 1300
LNVNAPLQLG GTPVDLEQLG RQLNWTHVPN QKGFFGCIRN LTINEQTYNL
1310 1320 1330 1340 1350
GMPSVFRNID SGCQQSVAVA FSFGIDRNFI IAIIVCLALL LIILLAVVVQ
1360 1370 1380 1390 1400
KKQKNGWHEK DIDDIRETII NYEDEGGGER DTDYDLNVLR TQPFYEEKLY
1410 1420 1430 1440 1450
KDPHALQGNM RDPNDIPDIA DFLGDKKENC DRDVGATTVD DVRHYAYEGD
1460 1470 1480 1490 1500
GNSDGSLSSL ASCTDDGDLN FDYLSNFGPR FRKLADMYGE EPSDTDSNVD

DDQGWRI
Length:1,507
Mass (Da):169,821
Last modified:June 1, 2000 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDF2B5CAAA29D8EE5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti974L → F in BAA05942 (PubMed:7958432).Curated1

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
D28749 mRNA Translation: BAA05942.1
AE013599 Genomic DNA Translation: AAF46659.1

NCBI Reference Sequences

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RefSeqi
NP_476722.1, NM_057374.3

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
FBtr0071546; FBpp0071475; FBgn0003391

Database of genes from NCBI RefSeq genomes

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GeneIDi
37386

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dme:Dmel_CG3722

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28749 mRNA Translation: BAA05942.1
AE013599 Genomic DNA Translation: AAF46659.1
RefSeqiNP_476722.1, NM_057374.3

3D structure databases

SMRiQ24298
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi63025, 87 interactors
DIPiDIP-22198N
IntActiQ24298, 4 interactors
STRINGi7227.FBpp0071475

PTM databases

iPTMnetiQ24298

Proteomic databases

PaxDbiQ24298
PRIDEiQ24298

Genome annotation databases

EnsemblMetazoaiFBtr0071546; FBpp0071475; FBgn0003391
GeneIDi37386
KEGGidme:Dmel_CG3722

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
37386
FlyBaseiFBgn0003391 shg

Phylogenomic databases

eggNOGiKOG1219 Eukaryota
ENOG410XPEI LUCA
GeneTreeiENSGT00940000172755
HOGENOMiCLU_247555_0_0_1
InParanoidiQ24298
OMAiDFYNVKV
OrthoDBi6237at2759
PhylomeDBiQ24298

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
37386 0 hits in 1 CRISPR screen

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
37386

Protein Ontology

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PROi
PR:Q24298

Gene expression databases

BgeeiFBgn0003391 Expressed in imaginal disc and 107 other tissues
GenevisibleiQ24298 DM

Family and domain databases

DisProtiDP00269
Gene3Di4.10.900.10, 1 hit
InterProiView protein in InterPro
IPR002126 Cadherin-like_dom
IPR015919 Cadherin-like_sf
IPR020894 Cadherin_CS
IPR000233 Cadherin_cytoplasmic-dom
IPR027397 Catenin_binding_dom_sf
IPR013320 ConA-like_dom_sf
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR001791 Laminin_G
PfamiView protein in Pfam
PF00028 Cadherin, 5 hits
PF01049 Cadherin_C, 1 hit
PF02210 Laminin_G_2, 1 hit
PRINTSiPR00205 CADHERIN
SMARTiView protein in SMART
SM00112 CA, 7 hits
SM00282 LamG, 1 hit
SUPFAMiSSF49313 SSF49313, 8 hits
SSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00232 CADHERIN_1, 5 hits
PS50268 CADHERIN_2, 7 hits
PS00022 EGF_1, 1 hit
PS01186 EGF_2, 1 hit
PS50026 EGF_3, 1 hit
PS50025 LAM_G_DOMAIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCADE_DROME
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q24298
Secondary accession number(s): Q9W2N1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 2000
Last modified: June 17, 2020
This is version 194 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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