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Q9R0T4

- CADH1_RAT

UniProt

Q9R0T4 - CADH1_RAT

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Protein

Cadherin-1

Gene

Cdh1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity).By similarity
E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi261 – 2611Calcium 1By similarity
Metal bindingi261 – 2611Calcium 2By similarity
Metal bindingi292 – 2921Calcium 3By similarity
Sitei704 – 7052Cleavage; by a metalloproteinaseBy similarity
Sitei735 – 7362Cleavage; by gamma-secretase/PS1By similarity
Sitei754 – 7552Cleavage; by caspase-3By similarity

GO - Molecular functioni

  1. calcium ion binding Source: Ensembl

GO - Biological processi

  1. calcium-dependent cell-cell adhesion Source: Ensembl
  2. cellular response to amino acid stimulus Source: Ensembl
  3. cellular response to indole-3-methanol Source: Ensembl
  4. cellular response to lithium ion Source: Ensembl
  5. cochlea development Source: Ensembl
  6. epithelial cell morphogenesis Source: Ensembl
  7. establishment of protein localization to plasma membrane Source: Ensembl
  8. homophilic cell adhesion Source: InterPro
  9. intestinal epithelial cell development Source: Ensembl
  10. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  11. negative regulation of cell-cell adhesion Source: Ensembl
  12. negative regulation of epithelial cell proliferation Source: Ensembl
  13. neuron projection development Source: RGD
  14. pituitary gland development Source: RGD
  15. positive regulation of transcription, DNA-templated Source: Ensembl
  16. positive regulation of transcription factor import into nucleus Source: Ensembl
  17. protein homooligomerization Source: Ensembl
  18. protein metabolic process Source: Ensembl
  19. regulation of branching involved in salivary gland morphogenesis Source: Ensembl
  20. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  21. regulation of neuron migration Source: Ensembl
  22. regulation of protein localization to cell surface Source: Ensembl
  23. regulation of water loss via skin Source: Ensembl
  24. response to drug Source: RGD
  25. response to organic substance Source: RGD
  26. response to toxic substance Source: RGD
  27. salivary gland cavitation Source: Ensembl
  28. sensory perception of sound Source: Ensembl
  29. single organismal cell-cell adhesion Source: DFLAT
  30. synapse assembly Source: RGD
  31. tight junction assembly Source: Ensembl
  32. trophectodermal cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_199178. Degradation of the extracellular matrix.

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-1
Alternative name(s):
Epithelial cadherin
Short name:
E-cadherin
Uvomorulin
CD_antigen: CD324
Cleaved into the following 3 chains:
Gene namesi
Name:Cdh1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 19

Organism-specific databases

RGDi69279. Cdh1.

Subcellular locationi

Cell junction. Cell membrane; Single-pass type I membrane protein. Endosome By similarity. Golgi apparatustrans-Golgi network By similarity
Note: Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane (By similarity).By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. aggresome Source: Ensembl
  3. apical junction complex Source: Ensembl
  4. apical part of cell Source: Ensembl
  5. axon terminus Source: Ensembl
  6. basolateral plasma membrane Source: Ensembl
  7. catenin complex Source: Ensembl
  8. cell-cell adherens junction Source: Ensembl
  9. cell surface Source: Ensembl
  10. cytoplasm Source: RGD
  11. cytoplasmic side of plasma membrane Source: Ensembl
  12. endosome Source: UniProtKB-KW
  13. extracellular vesicular exosome Source: Ensembl
  14. focal adhesion Source: Ensembl
  15. integral component of membrane Source: UniProtKB-KW
  16. lateral loop Source: Ensembl
  17. lateral plasma membrane Source: Ensembl
  18. node of Ranvier Source: Ensembl
  19. perinuclear region of cytoplasm Source: Ensembl
  20. plasma membrane Source: RGD
  21. Schmidt-Lanterman incisure Source: Ensembl
  22. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endosome, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Propeptidei24 – 158135Sequence AnalysisPRO_0000003719Add
BLAST
Chaini159 – 886728Cadherin-1PRO_0000003720Add
BLAST
Chaini705 – 886182E-Cad/CTF1Sequence AnalysisPRO_0000236073Add
BLAST
Chaini736 – 886151E-Cad/CTF2Sequence AnalysisPRO_0000236074Add
BLAST
Chaini755 – 886132E-Cad/CTF3Sequence AnalysisPRO_0000236075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi562 – 5621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi641 – 6411N-linked (GlcNAc...)Sequence Analysis
Modified residuei757 – 7571Phosphotyrosine; by SRCBy similarity
Modified residuei758 – 7581Phosphotyrosine; by SRCBy similarity
Modified residuei759 – 7591Phosphotyrosine; by SRCBy similarity
Modified residuei842 – 8421PhosphoserineBy similarity
Modified residuei844 – 8441PhosphoserineBy similarity
Modified residuei850 – 8501PhosphoserineBy similarity

Post-translational modificationi

N-glycosylation at Asn-641 is essential for expression, folding and trafficking.By similarity
Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-758 (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiQ9R0T4.
PRIDEiQ9R0T4.

PTM databases

PhosphoSiteiQ9R0T4.

Miscellaneous databases

PMAP-CutDBQ9R0T4.

Expressioni

Gene expression databases

GenevestigatoriQ9R0T4.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and potentially alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs). Interacts with AJAP1, CTNND1 and DLGAP5 (By similarity). Interacts with TBC1D2. Interacts with LIMA1. Interacts with CAV1. Interacts with the TRPV4 and CTNNB1 complex (By similarity). Interacts with PIP5K1C. Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization (By similarity). Interacts with RAPGEF2 (By similarity). Interacts with RAB8B.By similarity1 Publication

Protein-protein interaction databases

BioGridi249721. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9R0T4.
SMRiQ9R0T4. Positions 159-376, 788-881.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 713690ExtracellularSequence AnalysisAdd
BLAST
Topological domaini735 – 886152CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei714 – 73421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 266108Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini267 – 379113Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini380 – 490111Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini491 – 597107Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini598 – 701104Cadherin 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni762 – 77312Required for binding CTNND1 and PSEN1By similarityAdd
BLAST
Regioni815 – 88672Required for binding alpha, beta andBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi842 – 85716Ser-richAdd
BLAST

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

Sequence similaritiesi

Contains 5 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG328838.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiQ9R0T4.
KOiK05689.
OMAiDFGVGQE.
OrthoDBiEOG7PS1DS.
PhylomeDBiQ9R0T4.
TreeFamiTF316817.

Family and domain databases

Gene3Di2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
[Graphical view]
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 6 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R0T4-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MGARCRSFSA LLLLLQVSSW LCQQPESESD SCRPGFSSEV YTFLVPERHL
60 70 80 90 100
ERGHILGRVK FEGCTGRPRT AFFSEDSRFK VSTDGVITVK RHLKLHKLET
110 120 130 140 150
SFLVHAWDSS YRKLSTKVTL KSLGHHHHRH HHRDPVSESN PELLTFPSFH
160 170 180 190 200
QGLRRQKRDW VIPPINCPEN QKGEFPQRLV QIKSNRDKET TVFYSITGPG
210 220 230 240 250
ADKPPVGVFI IERETGWLKV TQPLDREAID KYLLYSHAVS SNGEAVEDPM
260 270 280 290 300
EIVVTVTDQN DNRPEFIQEV FEGSVAEGAL PGTSVMQVSA TDADDDINTY
310 320 330 340 350
NAAIAYTILS QDPELPHKNM FTVNRDTGVI SVVTSGLDRE SYPTYTLVVQ
360 370 380 390 400
AADLQGEGLS TTAKAVITVK DINDNAPIFN PSTYQGQVLE NEVGARIATL
410 420 430 440 450
KVTDDDAPNT PAWNAVYTVV NDPDHQFTVI TDPKTNEGIL KTAKGLDFEA
460 470 480 490 500
KQQYILHVTV ENEEPFEGSL VPSTATVTVD VVDVNEAPIF VPAEKRVEVP
510 520 530 540 550
EDFGVGLEIA SYTAREPDTF MEQKITYRIW RDTANWLEIN PETGVISTRA
560 570 580 590 600
EMDREDSEHV KNSTYTALII ATDDGSPIAT GTGTLLLVLS DVNDNAPIPE
610 620 630 640 650
PRNMQFCQRN PKPHVITILD PDLPPNTSPF TAELTHGASV NWTIEYNDAE
660 670 680 690 700
QESLILQPRK DLEIGEYKIN LKLSDNQNKD QVTTLEVHVC DCEGTVNNCM
710 720 730 740 750
KAISLEAGLQ VPAILGILGG ILALLILILL LLLFLRRRTV VKEPLLPPDD
760 770 780 790 800
DTRDNVYYYD EEGGGEEDQD FDLSQLHRGL DARPEVIRND VAPTLMSMPQ
810 820 830 840 850
YRPRPANPDE IGNFIDENLK AADSDPTAPP YDSLLVFDYE GSGSEAASLS
860 870 880
SLNSSESDQD QDYDYLNEWG NRFKKLADMY GGGEED
Length:886
Mass (Da):98,715
Last modified:May 1, 2000 - v1
Checksum:iA9AEE28EB797A547
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB017696 mRNA. Translation: BAA84920.1.
AF177680 mRNA. Translation: AAF87055.1.
AJ000540 mRNA. Translation: CAA04173.1.
RefSeqiNP_112624.1. NM_031334.1.
UniGeneiRn.1303.

Genome annotation databases

EnsembliENSRNOT00000027346; ENSRNOP00000027346; ENSRNOG00000020151.
GeneIDi83502.
KEGGirno:83502.
UCSCiRGD:69279. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB017696 mRNA. Translation: BAA84920.1 .
AF177680 mRNA. Translation: AAF87055.1 .
AJ000540 mRNA. Translation: CAA04173.1 .
RefSeqi NP_112624.1. NM_031334.1.
UniGenei Rn.1303.

3D structure databases

ProteinModelPortali Q9R0T4.
SMRi Q9R0T4. Positions 159-376, 788-881.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249721. 3 interactions.

PTM databases

PhosphoSitei Q9R0T4.

Proteomic databases

PaxDbi Q9R0T4.
PRIDEi Q9R0T4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000027346 ; ENSRNOP00000027346 ; ENSRNOG00000020151 .
GeneIDi 83502.
KEGGi rno:83502.
UCSCi RGD:69279. rat.

Organism-specific databases

CTDi 999.
RGDi 69279. Cdh1.

Phylogenomic databases

eggNOGi NOG328838.
GeneTreei ENSGT00760000118906.
HOGENOMi HOG000231254.
HOVERGENi HBG106438.
InParanoidi Q9R0T4.
KOi K05689.
OMAi DFGVGQE.
OrthoDBi EOG7PS1DS.
PhylomeDBi Q9R0T4.
TreeFami TF316817.

Enzyme and pathway databases

Reactomei REACT_199178. Degradation of the extracellular matrix.

Miscellaneous databases

NextBioi 615920.
PMAP-CutDB Q9R0T4.
PROi Q9R0T4.

Gene expression databases

Genevestigatori Q9R0T4.

Family and domain databases

Gene3Di 2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProi IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
[Graphical view ]
Pfami PF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view ]
PRINTSi PR00205. CADHERIN.
SMARTi SM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view ]
SUPFAMi SSF49313. SSF49313. 6 hits.
PROSITEi PS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Asai K., Tada T., Yamamoto M., Obayashi M., Mizuno M., Toda A., Eimoto T., Kato T.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Jejunum.
  2. "Multiple cadherin superfamily members with unique expression profiles are produced in rat testis."
    Johnson K.J., Patel S.R., Boekelheide K.
    Endocrinology 141:675-683(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 769-872.
    Strain: Fischer 344.
    Tissue: Testis.
  3. Gibbons K.L.
    Thesis (1997), University of Technology / Sydney, Australia
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 779-846.
    Tissue: Mammary tumor.
  4. "Rab8B GTPase and junction dynamics in the testis."
    Lau A.S., Mruk D.D.
    Endocrinology 144:1549-1563(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB8B.

Entry informationi

Entry nameiCADH1_RAT
AccessioniPrimary (citable) accession number: Q9R0T4
Secondary accession number(s): O35794, Q9JIV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3