Transportin-3 (TNPO3)
The protein contains 923 amino acids for an estimated molecular weight of 104203 Da.
Importin, which transports target proteins into the nucleus (PubMed:10366588, PubMed:10713112, PubMed:11517331, PubMed:12628928, PubMed:24449914). Specifically mediates the nuclear import of splicing factor serine/arginine (SR) proteins, such as RBM4, SFRS1 and SFRS2, by recognizing phosphorylated SR domains (PubMed:10366588, PubMed:10713112, PubMed:11517331, PubMed:12628928, PubMed:24449914). Also mediates the nuclear import of serine/arginine (SR) protein CPSF6, independently of CPSF6 phosphorylation (PubMed:30916345, PubMed:31465518). The nuclear import process is regulated by the small GTPase Ran that partitions between cytoplasm and nucleus in the predominantly GDP- and GTP-bound form, respectively (PubMed:23878195, PubMed:24449914). Importin associates with target cargo proteins in the cytoplasm, and the competitive binding of GTP-bound Ran induces the release of cargos in the nucleus (PubMed:23878195, PubMed:24449914).', '(Microbial infection) Involved in immunodeficiency virus (HIV-1) infection by importing the pre-integration complex (PIC) into the nucleus (PubMed:18722123, PubMed:21901095, PubMed:22398280, PubMed:29329553). Required for a nuclear maturation step of HIV-1 prior to integration (PubMed:21901095, PubMed:22398280). (updated: Nov. 13, 2019)
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.
- 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 |
|---|---|
| LGMDD2 |
The reference OMIM entry for this protein is 608423
Muscular dystrophy, limb-girdle, type 1f; lgmd1f
A number sign (#) is used with this entry because autosomal dominant limb-girdle muscular dystrophy type 1F (LGMD1F) is caused by heterozygous mutation in the TNPO3 gene (610032) on chromosome 7q32.
DESCRIPTION
Limb-girdle muscular dystrophy type 1F is an autosomal dominant myopathy characterized by proximal muscle weakness primarily affecting the lower limbs, but also affecting the upper limbs in most patients. Affected individuals also have distal muscle weakness of the hands and lower leg muscles. There is variability in presentation and progression. Some patients present in early childhood with mildly delayed walking and difficulty running and jumping, whereas others present as adults with mainly pelvic-girdle weakness. Patients with early onset tend to have a more severe disorder, and may develop contractures, loss of independent ambulation, and respiratory insufficiency. Muscle biopsy shows dystrophic changes with abnormal nuclei, rimmed vacuoles, and filamentous inclusions (summary by Melia et al., 2013). For a phenotypic description and a discussion of genetic heterogeneity of autosomal dominant limb-girdle muscular dystrophy, see LGMD1A (159000).CLINICAL FEATURES
Gamez et al. (2001) reported a large Spanish kindred in which 32 members spanning 5 generations were affected with autosomal dominant limb-girdle muscular dystrophy. Two forms were delineated based on age at onset: a juvenile form with onset before age 15 years (66%), and an adult-onset form starting around the third or fourth decade (28%). All affected patients showed characteristic pelvic and shoulder girdle proximal weakness. Pelvic girdle impairment was more severe and occurred earlier than shoulder girdle weakness, and distal weakness often occurred later. Respiratory muscles were clinically affected in 4 patients with juvenile onset. Muscle biopsies of 5 patients showed myopathic changes, including abnormal fiber size and variation, increased connective tissue, degenerative fibers, occasional central nuclei, and in 3 cases, rimmed vacuoles. There was no cardiac involvement, dysarthria, calf hypertrophy, or contractures. Melia et al. (2013) reported follow-up of the family reported by Gamez et al. (2001). There was variable distribution of affected muscles as well as variable severity and rate of progression. A predominant group of juvenile-onset patients showed mildly delayed walking followed by difficulty running and jumping. A small number of these patients also had joint contractures or rigid spine and developed respiratory insufficiency or lost independent ambulation in the third decade. A second group of patients had adult-onset of pelvic-girdle muscle weakness, followed by shoulder-girdle weakness in some. Other features of the disorder in all patients included thin legs and thenar muscle atrophy with hand weakness. Muscle biopsy showed dystrophic changes as well as abnormally enlarged nuclei with central pallor and filamentous or paracrystalline inclusions in muscle fibers. Torella et al. (2013) reported a patient with sporadic LGMD1F. He had young adult-onset of characteristic limb-girdle weakness. Muscle biopsy showed dystrophic features with mitochondrial alterations, sporadic ragged-red fibers, and cytochrome c oxidase-negative fibers.INHERITANCE
The transmission pattern in the family with LGMD1F reported by Gamez et al. (2001) was consistent with autosomal dominant inheritance.MAPPING
In the family with a ... More on the omim web site
Dec. 2, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 608423 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed