Exportin-7 (XPO7)
The protein contains 1087 amino acids for an estimated molecular weight of 123907 Da.
Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. (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.
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| Variant | Description |
|---|---|
| dbSNP:rs17856894 | |
| dbSNP:rs17856895 |
The reference OMIM entry for this protein is 606140
Exportin 7; xpo7
Ran-binding protein 16; ranbp16
DESCRIPTION
The transport of protein and large RNAs through the nuclear pore complexes (NPC) is an energy-dependent and regulated process. The import of proteins with a nuclear localization signal (NLS) is accomplished by recognition of one or more clusters of basic amino acids by the importin-alpha/beta complex; see 600685 and 602738. The small GTPase RAN (601179) plays a key role in NLS-dependent protein import. RAN-binding protein-16 is a member of the importin-beta superfamily of nuclear transport receptors.CLONING
By screening human brain cDNAs for those encoding proteins larger than 50 kD, Nagase et al. (1998) identified KIAA0745, a cDNA encoding a deduced 909-amino acid RANBP16 protein. RT-PCR ELISA demonstrated very high expression of RANBP16 in brain, moderate expression in heart, lung, and ovary, and low expression in liver, skeletal muscle, pancreas, testis, and spleen. In the course of cloning genes at the breakpoint of t(5;14)(q33-q34;q11), a recurring translocation in acute lymphoblastic leukemia, Koch et al. (2000) isolated and characterized 2 novel members of the importin-beta superfamily of nuclear transport receptors: RANBP16 and RANBP17 (606141). They also cloned the mouse Ranbp16 and Ranbp17 homologs. The human RANBP16 and RANBP17 proteins share 66% sequence identity. Human and mouse RANBP16 cDNAs encode 1,087-amino acid proteins containing an importin-beta N-terminal domain which is important for the binding of Ran protein. Northern blot analysis demonstrated restricted expression of RANBP17, but ubiquitous expression RANBP16. A major, approximately 4.8-kb RANBP16 transcript was strongly expressed in testis, thyroid, and bone marrow, moderately expressed in many other tissues, and weakly expressed in lung, liver, and small intestine, but not expressed in thymus. Two other transcripts of approximately 3.5 and 2.5 kb were strongly expressed in bone marrow and the 3.5-kb transcript was also strongly expressed in testis. The mouse Ranbp16 gene was also ubiquitously expressed. Both RANBP16 and RANBP17 were found to be predominantly nuclear proteins. Kutay et al. (2000) independently cloned RANBP16 and RANBP17. They identified RANBP16 by use of affinity chromatography on immobilized RanGTP. Based on the RANBP16 sequence, they identified RANBP17 by database searches. Kutay et al. (2000) determined that RANBP16 binds RanGTP directly. It can interact directly with the nuclear pore complex and is able to enter the nucleus independent of energy and additional nuclear transport receptors.MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the RANBP16 gene to chromosome 8. ... More on the omim web site
Dec. 10, 2018: Protein entry updated
Automatic update: model status changed
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 606140 was added.