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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)DescriptionActionsGraphical viewLength
Topological domaini156 – 703ExtracellularSequence analysisAdd BLAST548
Transmembranei704 – 728HelicalSequence analysisAdd BLAST25
Topological domaini729 – 880CytoplasmicSequence analysisAdd BLAST152

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000000372529 – 155Sequence analysisAdd BLAST127
ChainiPRO_0000003726156 – 880EP-cadherinAdd BLAST725

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi61N-linked (GlcNAc...)Sequence analysis1
Glycosylationi343O-linked (GalNAc...)1 Publication1
Glycosylationi382O-linked (GalNAc...)1 Publication1
Glycosylationi400O-linked (GalNAc...)1 Publication1
Glycosylationi425N-linked (GlcNAc...)1 Publication1
Glycosylationi428O-linked (GalNAc...)1 Publication1
Glycosylationi469O-linked (GalNAc...)1 Publication1
Glycosylationi471O-linked (GalNAc...)1 Publication1
Glycosylationi473O-linked (GalNAc...)1 Publication1
Glycosylationi475O-linked (GalNAc...)1 Publication1
Glycosylationi558N-linked (GlcNAc...)1 Publication1
Glycosylationi562O-linked (GalNAc...)1 Publication1
Glycosylationi576O-linked (GalNAc...)1 Publication1
Glycosylationi578O-linked (GalNAc...)1 Publication1
Glycosylationi580O-linked (GalNAc...)1 Publication1
Disulfide bondi603 ↔ 687
Glycosylationi681N-linked (GlcNAc...)1 Publication1
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

1880
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi162 – 167Combined sources6
Beta strandi170 – 172Combined sources3
Beta strandi174 – 178Combined sources5
Helixi183 – 185Combined sources3
Beta strandi189 – 196Combined sources8
Turni197 – 199Combined sources3
Beta strandi200 – 202Combined sources3
Beta strandi205 – 208Combined sources4
Turni210 – 212Combined sources3
Beta strandi214 – 217Combined sources4
Turni223 – 225Combined sources3
Beta strandi228 – 240Combined sources13
Beta strandi247 – 254Combined sources8
Beta strandi262 – 266Combined sources5
Beta strandi268 – 273Combined sources6
Beta strandi278 – 284Combined sources7
Beta strandi294 – 297Combined sources4
Beta strandi303 – 310Combined sources8
Beta strandi317 – 320Combined sources4
Turni322 – 324Combined sources3
Beta strandi326 – 329Combined sources4
Turni336 – 338Combined sources3
Beta strandi341 – 349Combined sources9
Helixi350 – 353Combined sources4
Beta strandi357 – 359Combined sources3
Beta strandi362 – 367Combined sources6
Beta strandi379 – 389Combined sources11
Beta strandi393 – 397Combined sources5
Beta strandi424 – 428Combined sources5
Turni430 – 432Combined sources3
Beta strandi435 – 441Combined sources7
Beta strandi451 – 455Combined sources5
Beta strandi458 – 461Combined sources4
Beta strandi472 – 479Combined sources8
Beta strandi486 – 489Combined sources4
Beta strandi502 – 508Combined sources7
Beta strandi522 – 526Combined sources5
Beta strandi535 – 537Combined sources3
Turni538 – 541Combined sources4
Beta strandi542 – 545Combined sources4
Beta strandi553 – 555Combined sources3
Beta strandi562 – 569Combined sources8
Beta strandi571 – 573Combined sources3
Beta strandi579 – 582Combined sources4
Beta strandi600 – 602Combined sources3
Beta strandi604 – 606Combined sources3
Beta strandi610 – 614Combined sources5
Turni620 – 623Combined sources4
Beta strandi634 – 637Combined sources4
Beta strandi646 – 652Combined sources7
Beta strandi665 – 667Combined sources3
Beta strandi670 – 672Combined sources3
Beta strandi676 – 679Combined sources4
Beta strandi682 – 684Combined sources3
Beta strandi688 – 690Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L3WX-ray3.08A156-695[»]
ProteinModelPortaliP33148.
SMRiP33148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33148.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini156 – 263Cadherin 1PROSITE-ProRule annotationAdd BLAST108
Domaini264 – 376Cadherin 2PROSITE-ProRule annotationAdd BLAST113
Domaini377 – 487Cadherin 3PROSITE-ProRule annotationAdd BLAST111
Domaini488 – 593Cadherin 4PROSITE-ProRule annotationAdd BLAST106
Domaini594 – 704Cadherin 5PROSITE-ProRule annotationAdd BLAST111

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi837 – 850Ser-richAdd BLAST14
Compositional biasi876 – 880Asp/Glu-rich (acidic)5

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3S → G in AAC16910 (Ref. 2) Curated1
Sequence conflicti112I → N in AAC16910 (Ref. 2) Curated1
Sequence conflicti163K → I AA sequence (PubMed:1879345).Curated1
Sequence conflicti169R → K AA sequence (PubMed:1879345).Curated1
Sequence conflicti176L → I AA sequence (PubMed:1879345).Curated1
Sequence conflicti573S → P in AAC16910 (Ref. 2) Curated1
Sequence conflicti864S → P in AAC16910 (Ref. 2) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L3WX-ray3.08A156-695[»]
ProteinModelPortaliP33148.
SMRiP33148.
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...

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: November 2, 2016
This is version 108 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.