Junctional adhesion molecule A precursor

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O88792 (JAM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	300 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.3
Subcellular location	Cell junction › tight 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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cell junction Cell membrane Membrane Tight junction
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW tight junction Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

Potential

Chain

27 – 300

274

Junctional adhesion molecule A

PRO_0000015067

Regions

Topological domain

27 – 238

212

Extracellular Potential

Transmembrane

239 – 259

Helical; Potential

Topological domain

260 – 299

Cytoplasmic Potential

Domain

28 – 122

Ig-like V-type 1

Domain

134 – 230

Ig-like V-type 2

Amino acid modifications

Modified residue

273

Phosphothreonine By similarity

Modified residue

281

Phosphotyrosine By similarity

Modified residue

282

Phosphoserine By similarity

Modified residue

285

Phosphoserine Ref.5

Modified residue

288

Phosphoserine Ref.5

Modified residue

297

Phosphoserine By similarity

Glycosylation

N-linked (GlcNAc...) Ref.7

Glycosylation

185

N-linked (GlcNAc...) Ref.6 Ref.7

Disulfide bond

49 ↔ 108

Disulfide bond

152 ↔ 212

Secondary structure

300

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

O88792 [UniParc].

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

FASTA

300

32,369

        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' referencesShow '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]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed: 19656770] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185, MASS SPECTROMETRY. Tissue: Myoblast.
[7]	"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.
[8]	"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

EMBL
GenBank
DDBJ

U89915 mRNA. Translation: AAC32982.1.

IPI

IPI00316159.

UniGene

Mm.294882.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F97	X-ray	2.50	A	27-238	[»]

ProteinModelPortal

O88792.

SMR

O88792. Positions 27-238.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-247376.

STRING

O88792.

PTM databases

PhosphoSite

O88792.

Proteomic databases

PRIDE

O88792.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

MGI

MGI:1321398. F11r.

Phylogenomic databases

eggNOG

roNOG16058.

HOGENOM

HBG446408.

HOVERGEN

HBG000518.

InParanoid

O88792.

OrthoDB

EOG4VT5XV.

Gene expression databases

ArrayExpress

O88792.

Bgee

O88792.

CleanEx

MM_F11R.

Genevestigator

O88792.

GermOnline

ENSMUSG00000038235. Mus musculus.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR003596. Ig_V-set_subgr.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 2 hits.

Pfam

PF07679. I-set. 2 hits.
[Graphical view]

SMART

SM00408. IGc2. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

JAM1_MOUSE

Accession

Primary (citable) accession number: O88792

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	September 21, 2011
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents