Junctional adhesion molecule A (F11R)

The protein contains 299 amino acids for an estimated molecular weight of 32583 Da.

 

Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3 (PubMed:11489913). The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity). Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (By similarity). Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration (PubMed:11812992). Involved in platelet activation (PubMed:10753840).', '(Microbial infection) Acts as a receptor for Mammalian reovirus sigma-1.', '(Microbial infection) Acts as a receptor for Human Rotavirus strain Wa. (updated: Oct. 25, 2017)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  7. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.


Interpro domains
Total structural coverage: 72%
Model score: 0

(right-click above to access to more options from the contextual menu)

The reference OMIM entry for this protein is 605721

Junction adhesion molecule 1; jam1
Junction adhesion molecule, mouse, homolog of; jam
Jam-a

DESCRIPTION

JAM1 is an immunoglobulin-like molecule that colocalizes with tight junctions in endothelium and epithelium and is also found on blood leukocytes and platelets (summary by Arrate et al., 2001).

CLONING

By searching databases for sequences similar to mouse Jam, followed by PCR of human umbilical vein endothelial cell cDNA library, Williams et al. (1999) cloned JAM1. The deduced 299-amino acid type I transmembrane protein contains an N-terminal signal peptide, followed by a 210-amino acid extracellular region, a putative membrane-spanning domain, and a 38-amino acid cytoplasmic tail. The extracellular domain contains 2 immunoglobulin (Ig)-like V-subset domains. Northern blot analysis detected a dominant transcript of about 4.4 kb and minor transcripts of about 2.0 to 2.4 kb. Strongest expression was detected in liver, kidney, lung, placenta, pancreas, and peripheral blood leukocytes. Weaker expression was detected in spleen and heart, and very weak expression was detected in skeletal muscle. No expression was detected in brain. Western blot analysis detected widespread surface expression of JAM in leukemia cell lines. By FACS, expression of JAM was detected in all normal circulating monocytes and neutrophils and in the majority of platelets. About half of circulating T and B lymphocytes expressed JAM1. Expression of JAM1 was not increased in neutrophils or T lymphocytes by any activation protocol examined. Epithelial cells form a highly selective barrier and line many organs. The epithelial barrier is maintained by closely apposed cell-cell contacts containing tight junctions. Liu et al. (2000) reported the cloning and tissue localization of an Ig superfamily member that likely represents the human homolog of murine Jam. Analysis of the primary structure of human JAM, which was cloned from T84 epithelial cells, predicts a 299-amino acid transmembrane protein with an N-terminal signal peptide, 2 potential N-glycosylation sites, and an extracellular domain that contains 2 IgV loops. The mature mouse and human JAM proteins are 70% identical. Monoclonal antibodies generated against the putative extracellular domain were reactive with a 35- to 39-kD protein from both T84 epithelial cells and human neutrophils. By immunofluorescence, JAM monoclonal antibodies labeled epithelial cells from intestine, lung, and kidney, prominently in the region of tight junctions (colocalization with occludin (OCLN; 602876)) and also along lateral cell membranes below the tight junctions. Flow cytometric studies confirmed predominant JAM expression in epithelial cells but also revealed expression on endothelial and hematopoietic cells of all lineages. Cera et al. (2004) showed that JAM1 is expressed in mouse and human dendritic cells.

GENE STRUCTURE

Wenzel et al. (2003) determined that the JAM1 gene contains 10 exons and spans approximately 23 kb. Intron 1 is about 20 kb.

MAPPING

Wenzel et al. (2003) reported that the JAM1 gene maps to chromosome 1q23.3.

GENE FUNCTION

Functional studies by Liu et al. (2000) demonstrated that JAM-specific monoclonal antibodies markedly inhibited transepithelial resistance recovery of T84 monolayers after disruption of intercellular junctions, including tight junctions, by transient calcium depletion. Morphologic analysis revealed that after disassembly of cell-cell junctions, anti-JAM inhibition of barrier function recovery correlated with a loss of both occludin a ... More on the omim web site

Subscribe to this protein entry history

May 12, 2019: Protein entry updated
Automatic update: model status changed

Nov. 17, 2018: Protein entry updated
Automatic update: model status changed

Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

Oct. 27, 2017: Protein entry updated
Automatic update: model status changed

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605721 was added.

Feb. 24, 2016: Protein entry updated
Automatic update: model status changed