Lymphocyte function-associated antigen 3 (CD58)

The protein contains 250 amino acids for an estimated molecular weight of 28147 Da.

 

Ligand of the T-lymphocyte CD2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells, antigen-independent and -dependent interactions of T-lymphocytes with target cells and antigen-presenting cells and the T-lymphocyte rosetting with erythrocytes. In addition, the LFA-3/CD2 interaction may prime response by both the CD2+ and LFA-3+ cells. (updated: March 4, 2015)

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. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

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: 68%
Model score: 60

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

VariantDescription
dbSNP:rs17426456

No binding partner found

The reference OMIM entry for this protein is 153420

Cd58 molecule; cd58
Lymphocyte function-associated antigen, type 3; lfa3

DESCRIPTION

The CD58 gene encodes a CD2 (186990) receptor. The presence of these 2 antigens on opposing cells optimizes immune recognition, facilitating contacts between helper T lymphocytes and antigen-presenting cells as well as between cytolytic effectors and target cells (Wang et al., 1999).

CLONING

The LFA3 gene has been cloned (Barbosa, 1987). Wallner et al. (1987) isolated the cDNA for CD58, which they called LFA3, the ligand of the T lymphocyte CD2 molecule. The deduced protein contains 222 amino acids and structurally resembles a typical membrane-anchored protein. An extracellular domain with six N-linked glycosylation sites is followed by a hydrophobic putative transmembrane region and a short cytoplasmic domain. Northern blot analysis detected a 1.3-kb LFA3 transcript that was widely distributed in human tissues and cell lines. Sewell et al. (1988) noted that the amino acid sequences of the extracellular domains of CD2 and CD58, which are predicted from their cDNA sequences, show significant similarities, and both are members of the immunoglobulin supergene family. They probably arose by duplication of a common evolutionary precursor.

MAPPING

Barbosa et al. (1985, 1986) mapped the LFA3 gene to chromosome 1 by study of mouse-human cell hybrids. There is some possibility that LFA3 is identical to the cell surface antigen identified by monoclonal antibodies and known as MSK2 (158040). MSK1 (158030) maps to the short arm of chromosome 1, and MSK2 to the long arm of chromosome 1. By a combination of Southern blot analysis of somatic cell hybrid DNA and in situ hybridization, Sewell et al. (1988) assigned the LFA3 gene to chromosome 1p13, which is the same location as CD2.

BIOCHEMICAL FEATURES

- Crystal Structure Wang et al. (1999) reported the crystal structure of the heterophilic adhesion complex between the N-terminal domains of human CD2 and CD58 at more than 3.2-angstrom resolution. A strikingly asymmetric, orthogonal, face-to-face interaction involving the major beta sheets of the respective immunoglobulin-like domains with poor shape complementarity was revealed. These features explained CD2-CD58 dynamic binding, offering insights into the interactions of related immunoglobulin superfamily receptors.

MOLECULAR GENETICS

For a discussion of a possible association between variation in the CD58 gene and protection against multiple sclerosis, see MS (126200). ... More on the omim web site

Subscribe to this protein entry history

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

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 153420 was added.

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