Protein S100-A7 (S100A7)

The protein contains 101 amino acids for an estimated molecular weight of 11471 Da.

 

No function (updated: Jan. 7, 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.

Interpro domains
Total structural coverage: 100%
Model score: 99

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VariantDescription
dbSNP:rs3014837

The reference OMIM entry for this protein is 600353

S100 calcium-binding protein a7; s100a7
Psoriasin; psor1

CLONING

Celis et al. (1990) established a computer-accessible 2D gel protein database of epidermal keratinocytes from normal and psoriatic skin. As a result of these studies, Celis et al. (1990) identified several low molecular mass proteins that were highly upregulated in psoriatic epidermis. Madsen et al. (1991) reported the molecular cloning and expression of one of these proteins, which they termed psoriasin. The sequence predicts a protein of molecular mass 11,457 Da. The predicted amino acid sequence includes a potential calcium-binding sequence of the EF-hand type. Schafer et al. (1995) isolated a YAC clone from 1q21 on which 9 different genes coding for S100 calcium-binding proteins could be localized. Clustered organization of these S100 genes allowed introduction of a new and logical nomenclature based on their physical arrangement; the 9 genes were symbolized S100A1 (176940), which is nearest the telomere, to S100A9 (123886), which is nearest the centromere. In this nomenclature, the gene encoding psoriasin was symbolized S100A7, rather than PSOR1.

GENE FUNCTION

Jinquan et al. (1996) reported that human psoriasin is a potent and selected chemotactic inflammatory protein for CD4+ T lymphocytes and neutrophils at a low concentration. Psoriasin is not structurally related to the alpha- or the beta-chemokine subfamilies or to lymphotactin (600250), a member of a unique class of chemokines. Glaser et al. (2005) analyzed skin extracts by affinity chromatography, HPLC, and mass spectrophotometry and found that the 11-kD psoriasin protein preferentially killed the gut bacterium Escherichia coli, but had little or no activity against Staphylococcus aureus or other bacteria. The activity could be inhibited by zinc, but not by other bivalent ions, suggesting that psoriasin kills E. coli by sequestration of zinc. Immunohistochemical analysis demonstrated intense expression of psoriasin in healthy skin, particularly in the face, scalp, and sebaceous glands. Real-time PCR and ELISA analysis of keratinocytes stimulated with E. coli culture supernatants induced transcription of psoriasin and its secretion. Stimulation with IL1B (147720) or, to a lesser extent, with TNF (191160) also induced psoriasin transcription and secretion. Glaser et al. (2005) concluded that psoriasin is key to the local innate defense against E. coli on body surfaces and kills the bacteria by sequestering essential transition metal ions.

GENE STRUCTURE

Semprini et al. (1999) determined the genomic structure and characterized the promoter of S100A7. The gene contains 3 exons spanning 2.7 kb.

MAPPING

Hardas et al. (1993) mapped the S100A7 gene to 1q21 by fluorescence in situ hybridization and YAC analysis. By Southern blot analysis of human/rodent somatic cell hybrids, Borglum et al. (1995) mapped the S100A7 gene to chromosome 1. By multipoint linkage analysis they assigned the locus to a site proximal to MUC1 (158340) and distal to AMY2B (104660).

MOLECULAR GENETICS

Mutation analysis by Semprini et al. (1999) using SSCP and direct sequencing of 15 unrelated psoriasis patients from 1q-linked pedigrees and 25 normal controls failed to identify any mutations, excluding S100A7 as a candidate gene for familial psoriasis susceptibility. ... 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

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600353 was added.

Jan. 28, 2016: Protein entry updated
Automatic update: model status changed

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