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Reviewed, UniProtKB/Swiss-Prot O88792 (JAM1_MOUSE)

Last modified October 13, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Junctional adhesion molecule A
      Short name=JAM-A
Alternative name(s):
    Junctional adhesion molecule 1
      Short name=JAM-1
    CD_antigen=CD321
Gene names
Name: F11r
Synonyms: Jam1, Jcam, Jcam1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Seems to plays a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Involved in platelet activation. In case of orthoreovirus infection, serves as receptor for the virus By similarity.

Subunit structure

Interacts with the ninth PDZ domain of MPDZ. Interacts with the first PDZ domain of PARD3. The association between PARD3 and PARD6B probably disrupts this interaction. Interacts with the orthoreovirus sigma-1 capsid protein By similarity.

Subcellular location

Cell junctiontight junction. Cell membrane; Single-pass type I membrane protein. Note: Localized at tight junctions of both epithelial and endothelial cells. Ref.2

Sequence similarities

Belongs to the immunoglobulin superfamily.

Contains 2 Ig-like V-type (immunoglobulin-like) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 300274Junctional adhesion molecule A
PRO_0000015067

Regions

Topological domain27 – 238212Extracellular Potential
Transmembrane239 – 25921 Potential
Topological domain260 – 29940Cytoplasmic Potential
Domain28 – 12295Ig-like V-type 1
Domain134 – 23097Ig-like V-type 2

Amino acid modifications

Modified residue2731Phosphothreonine By similarity
Modified residue2811Phosphotyrosine By similarity
Modified residue2821Phosphoserine By similarity
Modified residue2851Phosphoserine Ref.5
Modified residue2881Phosphoserine Ref.5
Glycosylation421N-linked (GlcNAc...) Ref.6
Glycosylation1851N-linked (GlcNAc...) Ref.6
Disulfide bond49 ↔ 108
Disulfide bond152 ↔ 212

Secondary structure

................................................... 300
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O88792-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 391F3E48FF3B97EC

FASTA30032,369
        10         20         30         40         50         60 
MGTEGKAGRK LLFLFTSMIL GSLVQGKGSV YTAQSDVQVP ENESIKLTCT YSGFSSPRVE 

        70         80         90        100        110        120 
WKFVQGSTTA LVCYNSQITA PYADRVTFSS SGITFSSVTR KDNGEYTCMV SEEGGQNYGE 

       130        140        150        160        170        180 
VSIHLTVLVP PSKPTISVPS SVTIGNRAVL TCSEHDGSPP SEYSWFKDGI SMLTADAKKT 

       190        200        210        220        230        240 
RAFMNSSFTI DPKSGDLIFD PVTAFDSGEY YCQAQNGYGT AMRSEAAHMD AVELNVGGIV 

       250        260        270        280        290        300 
AAVLVTLILL GLLIFGVWFA YSRGYFETTK KGTAPGKKVI YSQPSTRSEG EFKQTSSFLV 

« Hide

References

« Hide 'large scale' references
[1]"Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration."
Martin-Padura I., Lostaglio S., Schneemann M., Williams L., Romano M., Fruscella P., Panzeri C., Stoppacciaro A., Ruco L., Villa A., Simmons D., Dejana E.
J. Cell Biol. 142:117-127(1998) [PubMed: 9660867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of JAM-2 and JAM-3: an emerging junctional adhesion molecular family?"
Aurrand-Lions M.A., Duncan L., Du Pasquier L., Imhof B.A.
Curr. Top. Microbiol. Immunol. 251:91-98(2000) [PubMed: 11036763] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[3]"The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)."
Ebnet K., Suzuki A., Horikoshi Y., Hirose T., Meyer zu Brickwedde M.-K., Ohno S., Vestweber D.
EMBO J. 20:3738-3748(2001) [PubMed: 11447115] [Abstract]
Cited for: INTERACTION WITH PARD3.
[4]"Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response."
Muller W.A.
Trends Immunol. 24:327-334(2003) [PubMed: 12810109] [Abstract]
Cited for: REVIEW, NOMENCLATURE.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-288, MASS SPECTROMETRY.
Tissue: Liver.
[6]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-42 AND ASN-185, MASS SPECTROMETRY.
[7]"X-ray structure of junctional adhesion molecule: structural basis for homophilic adhesion via a novel dimerization motif."
Kostrewa D., Brockhaus M., D'Arcy A., Dale G.E., Nelboeck P., Schmid G., Mueller F., Bazzoni G., Dejana E., Bartfai T., Winkler F.K., Hennig M.
EMBO J. 20:4391-4398(2001) [PubMed: 11500366] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-238.
+Additional computationally mapped references.

Cross-references

Sequence databases

U89915 mRNA. Translation: AAC32982.1.
IPIIPI00316159.
UniGeneMm.294882

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1F97X-ray2.50A27-238[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGO88792.

PTM databases

PhosphoSiteO88792.

Genome annotation databases

EnsemblENSMUST00000043839; ENSMUSP00000041907; ENSMUSG00000038235; Mus musculus. [Genome view]

Organism-specific databases

MGIMGI:1321398. F11r.

Phylogenomic databases

HOGENOMO88792.
HOVERGENO88792.

Gene expression databases

ArrayExpressO88792.
BgeeO88792.
CleanExMM_F11R.
GenevestigatorO88792.
GermOnlineENSMUSG00000038235. Mus musculus.

Family and domain databases

InterProIPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_sub.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 2 hits.
PfamPF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00408. IGc2. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameJAM1_MOUSE
AccessionPrimary (citable) accession number: O88792
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: October 13, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents