S100A10

Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.

S100A10 Related Areas

Signal Transduction>>Calcium Signaling>>Calcium Binding Protein>>S100 Protein>>S100A10

S100A10 Alternative Names

S100A10, 42C, ANX2L, ANX2LG, CAL1L, CLP11, Ca[1], GP11, MGC111133, P11, p10 [Homo sapiens]

S100a10, 42C, AA409961, AL024248, CAL12, CLP11, Cal1l, p10, p11 [Mus musculus]

Summaries for S100A10

Entrez Gene summary for S100A10:

The protein encoded by this S100A10 gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. S100A10 may function in exocytosis and endocytosis. [provided by RefSeq, Jul 2008]

OMIM - description for S100A10:

The response to elevation of cytoplasmic Ca(2+) levels following extra- or intracellular stimuli is mediated by proteins that are capable of binding divalent calcium ions. A particular class of these proteins is characterized by the so-called EF-hand, a helix-loop-helix motif involved in coordinating the Ca(2+) ion. Within the EF-hand superfamily, a distinct set of proteins is grouped in the so-called S-100 protein family (see S100A1; 176940 and S100B; 176990), whose members share a high degree of sequence similarity with S-100A and S-100B, Ca(2+)-binding proteins originally isolated from cerebrospinal fluid. Protein p11 (calpactin I, light chain) is a member of the S-100 family but has several unique features. It has suffered crucial deletions and amino acid substitutions which are thought to render both Ca(2+)-binding sites inactive. In all tissues and cells studied, p11 is found in a heterotetrameric complex with another Ca(2+)-binding protein, annexin II (ANX2, LIP2; 151740). Some of the biochemical properties of annexin II are modulated by p11-induced complex formation, which involves the binding of one p11 dimer to 2 annexin II monomers. The p11 calpactin I light chain is an intracellular polypeptide of 97 amino acid residues that associates with the calpactin I heavy chain, p36, to form a calcium-binding complex (Saris et al., 1987). S100A10 subunit is a protein kinase substrate and likely plays a role in the regulation of p36 phosphorylation/activity.

Wikipedia summary for S100A10:

S100A10, also known as p11, is a protein that is encoded by the S100A10 gene in humans and the S100a10 gene in other species. S100A10 is a member of the S100 family of proteins containing two EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells. They regulate a number of cellular processes such as cell cycle progression and differentiation. The S100 protein is implicated in exocytosis and endocytosis by reorganization of F-actin.
S100A10 is linked with the transport of neurotransmitters. S100A10 is found in the brain of humans and other mammals, it has been implicated in the regulation of mood. In addition, due to its interaction with serotonin-signaling proteins and its correlation with symptoms of mood disorders, p11 is a new potential target for drug therapy.

Human S100A10 Protein General Information

 

• Protein names: Protein S100-A10
• Sequence length: 97 AA.
• Sequence similarities: S100A10 belongs to the S-100 family.
• Subunit structure: Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36. Interacts with SCN10A
• Miscellaneous: S100A10 does not appear to bind calcium. S100A10 contains 2 ancestral calcium site related to EF-hand domains that have lost their ability to bind calcium.

General information above from UniProt

Function for S100A10 Protein

UniProtKB:

Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.

Genatlas:

• S100A10 is involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation
• within the endothelial cell, S100A10 is required for Src kinase-mediated tyrosine phosphorylation of ANXA2, which signals translocation of both proteins to the cell surface
• S100A10 may play a role in the regulation of the proliferation or early maturation sequence of melanocytic lesions, and that it merits further study as a potential biomarker of activity
• S100A10 function as a regulator of the filamentous actin network
• direct involvement of S100A10 in macrophage recruitment in response to inflammatory stimuli
• S100A10 has a role in the antidepressant activity of neurotrophins
• S100A10 is a key cell surface receptor for plasminogen which regulates pericellular proteolysis and tumor cell invasion
• S100A10 plays a crucial role in the generation of plasmin leading to fibrinolysis, thus providing a link to the clinical hemorrhagic phenotype of Acute promyelocytic leukemia
• S100A10 is unable to bind calcium due to deletion and substitution of calcium-ligating residues