Calmodulin-like protein 5 (CALML5)

The protein contains 146 amino acids for an estimated molecular weight of 15893 Da.

 

Binds calcium. May be involved in terminal differentiation of keratinocytes. (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.

Interpro domains
Total structural coverage: 100%
Model score: 39

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VariantDescription
Confirmed at protein level
Confirmed at protein level

No binding partner found

The reference OMIM entry for this protein is 605183

Calmodulin-like 5; calml5
Calmodulin-like skin protein; clsp

CLONING

The stratum corneum, the uppermost layer of the human epidermis, provides the vital barrier between the organism and its environment. It is generated by keratinocytes that migrate from the basal layer to the surface of the epidermis undergoing terminal differentiation, a process that is calcium dependent. Low concentrations of calcium in the basal layer of the epidermis favor keratinocyte proliferation, and an increasing calcium gradient toward the surface controls part of the complex differentiation. Thus, calcium-binding proteins, which mediate calcium signals by interacting with and modulating specific target proteins, are important for epidermal differentiation. Using 2-dimensional gel electrophoresis, Mehul et al. (2000) separated an extract of total proteins from human stratum corneum. Peptide sequence analysis of 2 spots, followed by a homology search, revealed identification of a novel calcium-binding protein of the calmodulin (e.g., CALM1; 114180) family that the authors named 'calmodulin-like skin protein' (CLSP). By PCR using a degenerate oligonucleotide based on a CLSP peptide sequence, and 2 human keratinocyte cDNA libraries, one derived from proliferating cultured keratinocytes and the other from differentiated keratinocytes of reconstructed epidermis, Mehul et al. (2000) isolated a full-length CLSP cDNA. The predicted 146-amino acid CLSP protein contains 4 putative EF-hands, which are domains that bind to calcium, 2 potential sites for N-glycosylation, multiple potential sites for phosphorylation, and 1 potential site for myristoylation. CLSP shares 52% amino acid sequence homology with human calmodulin. RT-PCR of various human tissues and reconstructed epidermis detected abundant CLSP expression only in epidermis, with very low expression in lung. Evaluation of CLSP expression during keratinocyte differentiation revealed that CLSP was not detectably expressed in proliferating keratinocytes but was expressed in differentiating keratinocytes, beginning at an advanced stage of differentiation. Hwang and Morasso (2003) cloned mouse Scarf (skin calmodulin-related factor), the likely ortholog of human CLSP. The deduced 148-amino acid Scarf protein contains 4 EF-hand domains and shares 64.9% identity with human CLSP. Scarf has a slightly extended central helix compared with human CLSP. Northern and RNA dot blot analyses of adult mouse tissues detected Scarf only in thyroid and skeletal muscle. Northern blot analysis and RT-PCR showed strong Scarf expression in keratinocytes, with expression first detected at embryonic day 15. In situ hybridization localized Scarf within the spinous and granular layers in stratified epidermis, but not in the basal layer, of 16-day mouse embryos. In situ hybridization and immunohistochemical analysis of neonatal skin revealed Scarf only in anucleated differentiated layers of stratified epidermis. Hwang and Morasso (2003) noted that both Scarf and human CLSP are expressed predominantly in differentiated keratinocytes, but that Scarf is expressed earlier than CLSP during the differentiation process. In addition, Scarf and CLSP show slightly different distributions in other tissues.

GENE FUNCTION

Mehul et al. (2000) demonstrated that recombinant CLSP could bind calcium, and like calmodulin, thereafter exposed hydrophobic regions, which most likely interact with target proteins. Sequencing of an epidermal protein retained by a CLSP affinity column revealed 100% identity ... 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

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

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605183 was added.

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