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Protein

Epithelial cell adhesion molecule

Gene

Epcam

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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

GO - Biological processi

Complete GO annotation...

Protein family/group databases

MEROPSiI31.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Epithelial cell adhesion molecule
Short name:
Ep-CAM
Alternative name(s):
Epithelial glycoprotein 314
Short name:
EGP314
Short name:
mEGP314
Protein 289A
Tumor-associated calcium signal transducer 1
CD_antigen: CD326
Gene namesi
Name:Epcam
Synonyms:Tacstd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:106653. Epcam.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 266243ExtracellularSequence AnalysisAdd
BLAST
Transmembranei267 – 28923HelicalSequence AnalysisAdd
BLAST
Topological domaini290 – 31526CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • basolateral plasma membrane Source: MGI
  • bicellular tight junction Source: UniProtKB
  • cell surface Source: MGI
  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • lateral plasma membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 315292Epithelial cell adhesion moleculePRO_0000380183Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi118 ↔ 135PROSITE-ProRule annotation
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ99JW5.
PaxDbiQ99JW5.
PRIDEiQ99JW5.

Expressioni

Gene expression databases

BgeeiQ99JW5.
ExpressionAtlasiQ99JW5. baseline and differential.
GenevisibleiQ99JW5. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ99JW5. 3 interactions.
STRINGi10090.ENSMUSP00000061935.

Structurei

3D structure databases

ProteinModelPortaliQ99JW5.
SMRiQ99JW5. Positions 24-265.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 13573Thyroglobulin type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the EPCAM family.Curated
Contains 1 thyroglobulin type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46689.
GeneTreeiENSGT00390000018245.
HOGENOMiHOG000074086.
InParanoidiQ99JW5.
KOiK06737.
OMAiTTCWCVN.
OrthoDBiEOG7N0C5D.
PhylomeDBiQ99JW5.
TreeFamiTF332767.

Family and domain databases

Gene3Di4.10.800.10. 1 hit.
InterProiIPR000716. Thyroglobulin_1.
[Graphical view]
PfamiPF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
SMARTiSM00211. TY. 1 hit.
[Graphical view]
SUPFAMiSSF57610. SSF57610. 1 hit.
PROSITEiPS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q99JW5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGPQALAFG LLLAVVTATL AAAQRDCVCD NYKLATSCSL NEYGECQCTS
60 70 80 90 100
YGTQNTVICS KLASKCLAMK AEMTHSKSGR RIKPEGAIQN NDGLYDPDCD
110 120 130 140 150
EQGLFKAKQC NGTATCWCVN TAGVRRTDKD TEITCSERVR TYWIIIELKH
160 170 180 190 200
KERESPYDHQ SLQTALQEAF TSRYKLNQKF IKNIMYENNV ITIDLMQNSS
210 220 230 240 250
QKTQDDVDIA DVAYYFEKDV KGESLFHSSK SMDLRVNGEP LDLDPGQTLI
260 270 280 290 300
YYVDEKAPEF SMQGLTAGII AVIVVVSLAV IAGIVVLVIS TRKKSAKYEK
310
AEIKEMGEIH RELNA
Length:315
Mass (Da):35,019
Last modified:June 1, 2001 - v1
Checksum:iFDA853E165BA8906
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871Missing in AAA37543 (PubMed:1729376).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76124 mRNA. Translation: AAA37543.1.
AK145752 mRNA. Translation: BAE26627.1.
AK167182 mRNA. Translation: BAE39317.1.
BC005618 mRNA. Translation: AAH05618.1.
BC094465 mRNA. Translation: AAH94465.1.
CCDSiCCDS29018.1.
RefSeqiNP_032558.2. NM_008532.2.
UniGeneiMm.4259.

Genome annotation databases

EnsembliENSMUST00000053577; ENSMUSP00000061935; ENSMUSG00000045394.
GeneIDi17075.
KEGGimmu:17075.
UCSCiuc008duy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76124 mRNA. Translation: AAA37543.1.
AK145752 mRNA. Translation: BAE26627.1.
AK167182 mRNA. Translation: BAE39317.1.
BC005618 mRNA. Translation: AAH05618.1.
BC094465 mRNA. Translation: AAH94465.1.
CCDSiCCDS29018.1.
RefSeqiNP_032558.2. NM_008532.2.
UniGeneiMm.4259.

3D structure databases

ProteinModelPortaliQ99JW5.
SMRiQ99JW5. Positions 24-265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99JW5. 3 interactions.
STRINGi10090.ENSMUSP00000061935.

Protein family/group databases

MEROPSiI31.006.

Proteomic databases

MaxQBiQ99JW5.
PaxDbiQ99JW5.
PRIDEiQ99JW5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053577; ENSMUSP00000061935; ENSMUSG00000045394.
GeneIDi17075.
KEGGimmu:17075.
UCSCiuc008duy.1. mouse.

Organism-specific databases

CTDi4072.
MGIiMGI:106653. Epcam.

Phylogenomic databases

eggNOGiNOG46689.
GeneTreeiENSGT00390000018245.
HOGENOMiHOG000074086.
InParanoidiQ99JW5.
KOiK06737.
OMAiTTCWCVN.
OrthoDBiEOG7N0C5D.
PhylomeDBiQ99JW5.
TreeFamiTF332767.

Miscellaneous databases

NextBioi291194.
PROiQ99JW5.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JW5.
ExpressionAtlasiQ99JW5. baseline and differential.
GenevisibleiQ99JW5. MM.

Family and domain databases

Gene3Di4.10.800.10. 1 hit.
InterProiIPR000716. Thyroglobulin_1.
[Graphical view]
PfamiPF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
SMARTiSM00211. TY. 1 hit.
[Graphical view]
SUPFAMiSSF57610. SSF57610. 1 hit.
PROSITEiPS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A murine cDNA encodes a pan-epithelial glycoprotein that is also expressed on plasma cells."
    Bergsagel P.L., Victor-Kobrin C., Timblin C.R., Trepel J., Kuehl W.M.
    J. Immunol. 148:590-596(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiEPCAM_MOUSE
AccessioniPrimary (citable) accession number: Q99JW5
Secondary accession number(s): Q61512
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 100 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.