Focadhesin (FOCAD)
The protein contains 1801 amino acids for an estimated molecular weight of 200072 Da.
Potential tumor suppressor in gliomas. (updated: Jan. 7, 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.
- 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.
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.
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Biological Process
Molecular Function
The reference OMIM entry for this protein is 614606
Focadhesin; focad
Kiaa1797
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA library, Nagase et al. (2001) cloned FOCAD, which they designated KIAA1797. The deduced protein contains 1,281 amino acids. RT-PCR analysis revealed low to moderate FOCAD expression in all adult and fetal tissues examined except spleen, which showed little to no expression. Expression was highest in adult brain, liver, kidney, ovary, and spinal cord and in fetal brain and liver. Low to moderate expression was detected in all specific adult brain regions examined, with highest levels in amygdala, cerebellum, caudate nucleus, and hippocampus. Using real-time RT-PCR, Brockschmidt et al. (2012) detected variable KIAA1797 expression in all adult and fetal tissues examined. In adult tissues, expression was highest in brain, followed by testis, muscle, pancreas, heart, ovary, small intestine, placenta, prostate, thymus, kidney, colon, liver, lung, spleen, and leukocytes. In fetal tissues, expression was highest in brain, followed by muscle, kidney, heart, thymus, lung, liver, and spleen. Kiaa1797 was expressed in granule cell layer and hilus of mouse dentate gyrus. Immunofluorescence analysis of human astrocytes revealed colocalization of KIAA1797 with vinculin (VCL; 193065) at focal adhesions at the ends of actin stress fibers. Western blot analysis revealed KIAA1797 protein at an apparent molecular mass of about 200 kD in human white matter, cortex, and astrocytes.GENE STRUCTURE
Brockschmidt et al. (2012) determined that the FOCAD gene contains 46 exons and spans 337.6 kb.MAPPING
Melton et al. (2010) stated that the FOCAD gene maps to chromosome 9p21.3.GENE FUNCTION
Using real-time RT-PCR, Brockschmidt et al. (2012) found that expression of KIAA1797 was reduced in nearly all primary glioblastomas and in all glioblastoma primary cultures and cell lines examined. Reexpression of KIAA1797 in the LN18 and U87MG glioblastoma cell lines, which have homozygous KIAA1797 deletions, led to reduced colony formation and invasion capacity in vitro and reduced tumor lesions following implantation in nude mice. Immunoprecipitation analysis of transfected LN18 cells revealed direct interaction between KIAA1797 and vinculin.CYTOGENETICS
Using FISH, Brockschmidt et al. (2012) found that the KIAA1797 gene was disrupted by a t(7;9) translocation and deletion in a human glioblastoma primary culture. The 5-prime UTR of KIAA1797 was translocated to the derivative chromosome 7, but the remainder of KIAA1797 was deleted and absent from the derivative chromosome 9. Array-based comparative genomic hybridization revealed that 6 of 13 primary glioblastomas had complete or partial deletions of KIAA1797, and microdeletions involving KIAA1797 were present in 5 of 10 glioblastoma primary cultures and gliobastoma cell lines. No glioblastomas or gliobastoma cell lines or primary cultures analyzed showed hypermethylation of the KIAA1797 gene. ... 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 614606 was added.