Plastin-2 (LCP1)

The protein contains 627 amino acids for an estimated molecular weight of 70288 Da.

 

Actin-binding protein (PubMed:16636079, PubMed:17294403, PubMed:28493397). Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28 (PubMed:17294403). Modulates the cell surface expression of IL2RA/CD25 and CD69 (PubMed:17294403). (updated: Jan. 31, 2018)

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.


Interpro domains
Total structural coverage: 84%
Model score: 0

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VariantDescription
empty
dbSNP:rs4941543
dbSNP:rs17067725
Found in a patient with isolated coloboma; increases interaction with actin

The reference OMIM entry for this protein is 153430

Lymphocyte cytosolic protein 1; lcp1
Lymphocyte cytosol polypeptide, 64-kd; lc64p; cp64
L-plastin; lpl
Plastin 2; pls2

CLONING

Lin et al. (1988) isolated partial cDNAs encoding L-plastin and T-plastin (PLS3; 300131) from a transformed human fibroblast cDNA library. Northern blot analysis revealed that L-plastin is expressed as a 3.7-kb mRNA in leukocytes, transformed fibroblasts, and a diverse array of human tumor cell lines. Zu et al. (1990) reported that L-plastin is identical to p65, an interleukin-2 (IL2; 147680)-stimulated phosphoprotein found in human T cells. Zu et al. (1990) isolated p65 cDNAs from a human T-lymphocyte cDNA library. The predicted 627-amino acid p65 protein contains 2 EF-hand calcium-binding domains, a calmodulin-binding site, and 2 tandem repeats of an actin-binding domain.

GENE STRUCTURE

Lin et al. (1993) reported that both the L-plastin and T-plastin genes contain 16 exons and span approximately 90 kb. Lin et al. (1997) found that the human and murine L-plastin promoters are highly homologous and function equally well in either human or murine leukocytes.

MAPPING

Kondo et al. (1985) assigned the LCP1 gene to 13q14.1-q14.2 by the deletion/dosage method. They studied a patient with trisomy 13 who had 1.5 times the normal amount of protein, a patient with retinoblastoma and deletion of 13q12.3-q21.2 who had half the normal amount of protein, and a patient with retinoblastoma and deletion of 13q14.1-q31.2 who had lost the father's allele and had half the normal amount of protein (Kondo et al., 1985). Close linkage to ESD (133280) was indicated by a maximum lod score of 4.221 at zero recombination. As part of an undertaking to map by genetic linkage human lymphocyte proteins that are genetically polymorphic in isoelectric point, Goldman et al. (1991) mapped the LCP1 gene to a site near the ESD locus on chromosome 13 by studies in 9 families from the CEPH collection. The proteins in the immortalized lymphocyte cell lines were analyzed by 2-dimensional electrophoresis. Murayama et al. (1993) demonstrated that L-plastin and LCP1 are identical and mapped the gene to 13q14.3.

CYTOGENETICS

The LAZ3 gene (BCL6; 109565) on 3q27 is nonrandomly disrupted in B-cell non-Hodgkin lymphoma by chromosomal translocations. Galiegue-Zouitina et al. (1999) identified the L-plastin gene as a novel LAZ3 partner in chimeric transcripts resulting from a t(3;13)(q27;q14) translocation in 2 cases of B-cell lymphoma. As a consequence of the translocation, the 5-prime regulatory region of each gene was exchanged, creating both LCP1-LAZ3 and reciprocal LAZ3-LCP1 fusion transcripts in one case, and only an LCP1-LAZ3 fusion transcript in the other.

MOLECULAR GENETICS

Hamaguchi et al. (1982) described a genetic polymorphism of a major human LCP of molecular weight 64,000, detected in PHA-stimulated peripheral blood lymphocytes by high-resolution 2-dimensional electrophoresis (O'Farrell, 1975; Klose, 1975). Three different phenotypes determined by 2 common alleles at a single locus were found. In Japanese, the frequency of the 2 alleles was 0.936 and 0.064, respectively. The polypeptide was not detected in HeLa cells, fibroblasts, red cells, serum, or cerebrum. Traces were found in liver, kidney and skeletal muscle. (Hamaguchi et al. (1982) demonstrated polymorphism in 3 others of about 100 polypeptides. The 4 were all cytosolic and since they were separated by isoelectric focusing, they are all charge variants. The molecular weights of the 3 other polymorphic lymphocyte cytosol polypeptides were 40, 49, and 1 ... 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 153430 was added.

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed