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Protein

EP-cadherin

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
EP-cadherin
Alternative name(s):
C-cadherin
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6254663. cdh3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini156 – 703548ExtracellularSequence analysisAdd
BLAST
Transmembranei704 – 72825HelicalSequence analysisAdd
BLAST
Topological domaini729 – 880152CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Propeptidei29 – 155127Sequence analysisPRO_0000003725Add
BLAST
Chaini156 – 880725EP-cadherinPRO_0000003726Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence analysis
Glycosylationi343 – 3431O-linked (GalNAc...)1 Publication
Glycosylationi382 – 3821O-linked (GalNAc...)1 Publication
Glycosylationi400 – 4001O-linked (GalNAc...)1 Publication
Glycosylationi425 – 4251N-linked (GlcNAc...)1 Publication
Glycosylationi428 – 4281O-linked (GalNAc...)1 Publication
Glycosylationi469 – 4691O-linked (GalNAc...)1 Publication
Glycosylationi471 – 4711O-linked (GalNAc...)1 Publication
Glycosylationi473 – 4731O-linked (GalNAc...)1 Publication
Glycosylationi475 – 4751O-linked (GalNAc...)1 Publication
Glycosylationi558 – 5581N-linked (GlcNAc...)1 Publication
Glycosylationi562 – 5621O-linked (GalNAc...)1 Publication
Glycosylationi576 – 5761O-linked (GalNAc...)1 Publication
Glycosylationi578 – 5781O-linked (GalNAc...)1 Publication
Glycosylationi580 – 5801O-linked (GalNAc...)1 Publication
Disulfide bondi603 ↔ 687
Glycosylationi681 – 6811N-linked (GlcNAc...)1 Publication
Disulfide bondi685 ↔ 694

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Expressioni

Developmental stagei

Unfertilized eggs and early Xenopus embryos.

Interactioni

Subunit structurei

Interacts with CTNNB1.1 Publication

Protein-protein interaction databases

DIPiDIP-59585N.

Structurei

Secondary structure

1
880
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi162 – 1676Combined sources
Beta strandi170 – 1723Combined sources
Beta strandi174 – 1785Combined sources
Helixi183 – 1853Combined sources
Beta strandi189 – 1968Combined sources
Turni197 – 1993Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi205 – 2084Combined sources
Turni210 – 2123Combined sources
Beta strandi214 – 2174Combined sources
Turni223 – 2253Combined sources
Beta strandi228 – 24013Combined sources
Beta strandi247 – 2548Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi268 – 2736Combined sources
Beta strandi278 – 2847Combined sources
Beta strandi294 – 2974Combined sources
Beta strandi303 – 3108Combined sources
Beta strandi317 – 3204Combined sources
Turni322 – 3243Combined sources
Beta strandi326 – 3294Combined sources
Turni336 – 3383Combined sources
Beta strandi341 – 3499Combined sources
Helixi350 – 3534Combined sources
Beta strandi357 – 3593Combined sources
Beta strandi362 – 3676Combined sources
Beta strandi379 – 38911Combined sources
Beta strandi393 – 3975Combined sources
Beta strandi424 – 4285Combined sources
Turni430 – 4323Combined sources
Beta strandi435 – 4417Combined sources
Beta strandi451 – 4555Combined sources
Beta strandi458 – 4614Combined sources
Beta strandi472 – 4798Combined sources
Beta strandi486 – 4894Combined sources
Beta strandi502 – 5087Combined sources
Beta strandi522 – 5265Combined sources
Beta strandi535 – 5373Combined sources
Turni538 – 5414Combined sources
Beta strandi542 – 5454Combined sources
Beta strandi553 – 5553Combined sources
Beta strandi562 – 5698Combined sources
Beta strandi571 – 5733Combined sources
Beta strandi579 – 5824Combined sources
Beta strandi600 – 6023Combined sources
Beta strandi604 – 6063Combined sources
Beta strandi610 – 6145Combined sources
Turni620 – 6234Combined sources
Beta strandi634 – 6374Combined sources
Beta strandi646 – 6527Combined sources
Beta strandi665 – 6673Combined sources
Beta strandi670 – 6723Combined sources
Beta strandi676 – 6794Combined sources
Beta strandi682 – 6843Combined sources
Beta strandi688 – 6903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L3WX-ray3.08A156-695[»]
ProteinModelPortaliP33148.
SMRiP33148. Positions 156-695, 779-873.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33148.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini156 – 263108Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini264 – 376113Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini377 – 487111Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini488 – 593106Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini594 – 704111Cadherin 5PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi837 – 85014Ser-richAdd
BLAST
Compositional biasi876 – 8805Asp/Glu-rich (acidic)

Domaini

Three calcium ions are usually bound at the interface of each cadherin domain.

Sequence similaritiesi

Contains 5 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG106438.
KOiK05689.

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. 4 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. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P33148-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSTRLRNAS VWLCGLLCLL QVVPSINADV SGCKPGFSSA EYIFSVNRRE
60 70 80 90 100
LERGRKLGKV NFSDCTTRKH GLYDVGDSRF RVLPDGTVLV KRHVKLHKDT
110 120 130 140 150
KFTISTWDAR GIKHSTNIAV ASKRHRSGEE AHSRSSKLPV LTFPETHTGL
160 170 180 190 200
KRKKRDWVIP PIKVSENERG PFPKRLVQIK SNKDRFNKVY YSITGQGADN
210 220 230 240 250
PPQGVFRIEW ETGWMLVTRP LDREEYDKYV LSSHAVSENG SPVEEPMEIT
260 270 280 290 300
INVIDQNDNR PKFTQDVFRG SVREGVQPGT QVMAVSATDE DDNIDSLNGV
310 320 330 340 350
LSYSILKQDP EEPIPNLFTI NRETGVISLI GTGLDREKFP EYTLTVQATD
360 370 380 390 400
LEGAGLSVEG KAIIQITDAN DNAPIFDPKT YTALVPENEI GFEVQRLSVT
410 420 430 440 450
DLDMPGTPAW QAVYKIRVNE GGFFNITTDP ESNQGILTTA KGLDFELRKQ
460 470 480 490 500
YVLQITVENA EPFSVPLPTS TATVTVTVED VNEAPFFVPA VSRVDVSEDL
510 520 530 540 550
SRGEKIISLV AQDPDKQQIQ KLSYFIGNDP ARWLTVNKDN GIVTGNGNLD
560 570 580 590 600
RESEYVKNNT YTVIMLVTDD GVSVGTGTGT LILHVLDVND NGPVPSPRVF
610 620 630 640 650
TMCDQNPEPQ VLTISDADIP PNTYPYKVSL SHGSDLTWKA ELDSKGTSML
660 670 680 690 700
LSPTQQLKKG DYSIYVLLSD AQNNPQLTVV NATVCSCEGK AIKCQEKLVG
710 720 730 740 750
GFDLPIILVI LGSVLALLIL FLLLLLFLKR KKVVKEPLLL PEDDTRDNIF
760 770 780 790 800
YYGEEGGGEE DQDYDLSQLH RGLDSRPDIM RNDVVPTLMP APHYRPRPSN
810 820 830 840 850
PDEIGNFIDE NLDAADNDPT APPYDSLLVF DYEGSGSEAA SLSSLNSSNS
860 870 880
NDEHDYNYLS DWGSRFRKLA DMYGGDDDEE
Length:880
Mass (Da):97,651
Last modified:April 27, 2001 - v2
Checksum:iC6CCD91566427D86
GO

Sequence cautioni

The sequence CAA45252.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31S → G in AAC16910 (Ref. 2) Curated
Sequence conflicti112 – 1121I → N in AAC16910 (Ref. 2) Curated
Sequence conflicti163 – 1631K → I AA sequence (PubMed:1879345).Curated
Sequence conflicti169 – 1691R → K AA sequence (PubMed:1879345).Curated
Sequence conflicti176 – 1761L → I AA sequence (PubMed:1879345).Curated
Sequence conflicti573 – 5731S → P in AAC16910 (Ref. 2) Curated
Sequence conflicti864 – 8641S → P in AAC16910 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63720 mRNA. Translation: CAA45252.1. Different initiation.
U04707 mRNA. Translation: AAC16910.1.
PIRiB43785. IJXLCP.
RefSeqiNP_001080946.1. NM_001087477.1.
UniGeneiXl.281.

Genome annotation databases

GeneIDi394290.
KEGGixla:394290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63720 mRNA. Translation: CAA45252.1. Different initiation.
U04707 mRNA. Translation: AAC16910.1.
PIRiB43785. IJXLCP.
RefSeqiNP_001080946.1. NM_001087477.1.
UniGeneiXl.281.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L3WX-ray3.08A156-695[»]
ProteinModelPortaliP33148.
SMRiP33148. Positions 156-695, 779-873.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59585N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi394290.
KEGGixla:394290.

Organism-specific databases

CTDi394290.
XenbaseiXB-GENE-6254663. cdh3.

Phylogenomic databases

HOVERGENiHBG106438.
KOiK05689.

Miscellaneous databases

EvolutionaryTraceiP33148.

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. 4 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. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Expression of a novel cadherin (EP-cadherin) in unfertilized eggs and early Xenopus embryos."
    Ginsberg D., Desimone D., Geiger B.
    Development 111:315-325(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Lee C.H.
    Thesis (1994), University of California San Francisco, United States
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Flament S.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 260.
  4. "Differential expression of two cadherins in Xenopus laevis."
    Angres B., Mueller A.H.J., Kellermann J., Hausen P.
    Development 111:829-844(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 156-176.
  5. "Crystal structure of a beta-catenin/BCL9/Tcf4 complex."
    Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.
    Mol. Cell 24:293-300(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTNNB1.
  6. "C-cadherin ectodomain structure and implications for cell adhesion mechanisms."
    Boggon T.J., Murray J., Chappuis-Flament S., Wong E., Gumbiner B.M., Shapiro L.
    Science 296:1308-1313(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 156-695, CALCIUM-BINDING SITES, GLYCOSYLATION AT THR-343; THR-382; THR-400; ASN-425; THR-428; THR-469; THR-471; THR-473; THR-475; ASN-558; THR-562; THR-576; THR-578; THR-580 AND ASN-681.
  7. "Untangling desmosomal knots with electron tomography."
    He W., Cowin P., Stokes D.L.
    Science 302:109-113(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 156-695.

Entry informationi

Entry nameiCADHF_XENLA
AccessioniPrimary (citable) accession number: P33148
Secondary accession number(s): Q91543
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 27, 2001
Last modified: October 14, 2015
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.