Annexin A7 (ANXA7)
The protein contains 488 amino acids for an estimated molecular weight of 52739 Da.
Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- 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.
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- 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.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
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.
This protein is annotated as membranous in Gene Ontology.
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| Variant | Description |
|---|---|
| dbSNP:rs3750575 |
Biological Process
Autophagy
Cell population proliferation
Cellular calcium ion homeostasis
Cellular water homeostasis
Epithelial cell differentiation
Hemostasis
Membrane fusion
Negative regulation of gene expression
Regulation of cell shape
Response to calcium ion
Response to organic cyclic compound
Response to salt stress
Social behavior
The reference OMIM entry for this protein is 186360
Annexin a7; anxa7
Annexin vii; anx7
Synexin; snx
DESCRIPTION
Synexin is a calcium-dependent membrane-binding protein that not only fuses membranes but also acts as a voltage-dependent calcium channel.CLONING
Burns et al. (1989) isolated and sequenced a set of overlapping cDNA clones for human synexin. Its derived amino acid sequence shows strong homology in the C-terminal domain with a previously identified class of calcium-dependent membrane-binding proteins, including endonexin II (131230), lipocortin I (151690), calpactin I heavy chain (114085), and others. Magendzo et al. (1991) cloned 3 variants of synexin cDNA from a human fibroblast cDNA library. Sequence analysis indicated that the variants were formed by alternative splicing and use of alternate polyadenylation signals. Northern blot analysis of fibroblasts revealed transcripts of 2.0 and 2.4 kb. Using primers designed to differentiate between these 2 forms by PCR, Magendzo et al. (1991) found the larger transcript, containing a 66-bp exon, in human and monkey brain, heart, and skeletal muscle. They found the variant lacking this exon in liver, lung, kidney, spleen, fibroblasts, and placenta. Western blot analysis indicated the presence of the larger protein in human skeletal muscle and the smaller protein in lung.GENE FUNCTION
The ANX7 gene is located on chromosome 10q21, a site long hypothesized to harbor a tumor suppressor gene or genes associated with prostate and other cancers. To test this hypothesis, Srivastava et al. (2001) analyzed the action of the ANX7 gene on colony formation by human tumor cell lines. They also examined the expression of the ANX7 protein in a large number of prostate cancers using tumor tissue microarray technology. Finally, they tested a panel of primary and metastatic prostate cancers for evidence of loss of heterozygosity (LOH). They found that human tumor cell proliferation and colony formation were markedly reduced when the wildtype ANX7 gene was transfected into 2 prostate tumor cell lines. Consistently, analysis of ANX7 protein expression in human prostate tumor microarrays revealed a significantly higher rate of loss of ANX7 expression in metastatic and local recurrences of hormone refractory prostate cancer as compared with primary tumors (P = 0.0001). Using 4 microsatellite markers at or near the ANX7 locus and laser capture microdissected tumor cells, 35% of 20 primary prostate tumors showed LOH. The microsatellite marker closest to the ANX7 locus showed the highest rate of LOH, including 1 homozygous deletion. Srivastava et al. (2001) concluded that the ANX7 gene exhibits many biologic and genetic properties expected of a tumor suppressor gene and may play a role in prostate cancer progression. Caohuy et al. (1996) present experimental evidence, based on studies of recombinant human ANXA7 and isolated bovine chromaffin cells, that ANXA7 is a Ca(2+)-dependent GTP binding protein. ANXA7 was active in a chromaffin granule aggregation assays in the presence of Ca(2+) and GTP, and was deactivated upon GTP hydrolysis.GENE STRUCTURE
Shirvan et al. (1994) determined that the synexin gene contains 14 exons, including an alternatively spliced cassette exon, and spans approximately 34 kb of DNA. Only 5 of the 14 spliced exons are conserved compared to other annexins; the differences are particularly pronounced in the exons that encode the C-terminal third and fourth conserved repeats in the gene product. Shirvan et al. (1994) concluded that the ANXA ... More on the omim web site
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 186360 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed