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Protein

Epithelial cell adhesion molecule

Gene

Epcam

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

Functioni

May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E (By similarity).By similarity

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: RGD

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-RNO-202733 Cell surface interactions at the vascular wall

Names & Taxonomyi

Protein namesi
Recommended name:
Epithelial cell adhesion molecule
Short name:
Ep-CAM
Alternative name(s):
Epithelial glycoprotein 314
Short name:
EGP314
Protein D5.7A
Tumor-associated calcium signal transducer 1
CD_antigen: CD326
Gene namesi
Name:Epcam
Synonyms:Tacstd1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi621365 Epcam

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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 266ExtracellularSequence analysisAdd BLAST243
Transmembranei267 – 289HelicalSequence analysisAdd BLAST23
Topological domaini290 – 315CytoplasmicSequence analysisAdd BLAST26

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000038018524 – 315Epithelial cell adhesion moleculeAdd BLAST292

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 46PROSITE-ProRule annotation
Disulfide bondi29 ↔ 59PROSITE-ProRule annotation
Disulfide bondi38 ↔ 48PROSITE-ProRule annotation
Disulfide bondi66 ↔ 99PROSITE-ProRule annotation
Disulfide bondi110 ↔ 116PROSITE-ProRule annotation
Glycosylationi111N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi118 ↔ 135PROSITE-ProRule annotation
Glycosylationi198N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Glycosylation at Asn-198 is crucial for protein stability.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO55159
PRIDEiO55159

PTM databases

iPTMnetiO55159
PhosphoSitePlusiO55159

Expressioni

Gene expression databases

BgeeiENSRNOG00000015667
GenevisibleiO55159 RN

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with phosphorylated CLDN7.By similarity

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021135

Structurei

3D structure databases

ProteinModelPortaliO55159
SMRiO55159
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 135Thyroglobulin type-1PROSITE-ProRule annotationAdd BLAST73

Sequence similaritiesi

Belongs to the EPCAM family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFI6 Eukaryota
ENOG4111M3B LUCA
GeneTreeiENSGT00390000018245
HOGENOMiHOG000074086
InParanoidiO55159
KOiK06737
OMAiREKPYDV
OrthoDBiEOG091G0G1E
PhylomeDBiO55159
TreeFamiTF332767

Family and domain databases

CDDicd00191 TY, 1 hit
Gene3Di4.10.800.10, 1 hit
InterProiView protein in InterPro
IPR000716 Thyroglobulin_1
IPR036857 Thyroglobulin_1_sf
PfamiView protein in Pfam
PF00086 Thyroglobulin_1, 1 hit
SMARTiView protein in SMART
SM00211 TY, 1 hit
SUPFAMiSSF57610 SSF57610, 1 hit
PROSITEiView protein in PROSITE
PS00484 THYROGLOBULIN_1_1, 1 hit
PS51162 THYROGLOBULIN_1_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

O55159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPPKALAFG LLLAVVTATL AAAQKDCVCN NYKLTSRCYE NENGECQCTS
60 70 80 90 100
YGTQNTVICS KLASKCLVMK AEMTHSKSGR RMKPEGAIQN NDGLYDPECD
110 120 130 140 150
EQGLFKAKQC NGTATCWCVN TAGVRRTDKD TEITCSERVR TYWIIIELKH
160 170 180 190 200
KERAQPYNFE SLHTALQDTF ASRYMLNPKF IKSIMYENNV ITIDLMQNSS
210 220 230 240 250
QKTQDDVDIA DVAYYFEKDV KGESLFHSSK SMDLRVNGEL LDLDPGQTLI
260 270 280 290 300
YYVDEKAPEF SMQGLTAGII AVIVVVVLAV IAGIVVLVIS TRKRSAKYEK
310
AEIKEMGEIH RELNA
Length:315
Mass (Da):35,207
Last modified:June 1, 1998 - v1
Checksum:i024F796B18F85BC4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001044 mRNA Translation: CAA04498.1
CH473947 Genomic DNA Translation: EDM02636.1
BC072691 mRNA Translation: AAH72691.1
RefSeqiNP_612550.1, NM_138541.1
XP_017449516.1, XM_017594027.1
UniGeneiRn.106481

Genome annotation databases

EnsembliENSRNOT00000021135; ENSRNOP00000021135; ENSRNOG00000015667
GeneIDi171577
KEGGirno:171577
UCSCiRGD:621365 rat

Similar proteinsi

Entry informationi

Entry nameiEPCAM_RAT
AccessioniPrimary (citable) accession number: O55159
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 1, 1998
Last modified: April 25, 2018
This is version 114 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health