Type-1 angiotensin II receptor-associated protein (AGTRAP)
The protein contains 159 amino acids for an estimated molecular weight of 17419 Da.
Appears to be a negative regulator of type-1 angiotensin II receptor-mediated signaling by regulating receptor internalisation as well as mechanism of receptor desensitization such as phosphorylation. Induces also a decrease in cell proliferation and angiotensin II-stimulated transcriptional activity. (updated: April 1, 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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs17875960 |
The reference OMIM entry for this protein is 608729
Angiotensin ii receptor-associated protein; agtrap
Atrap
CLONING
Using the C-terminal domain of murine At2r1a (106165) as bait in a yeast 2-hybrid screen, Daviet et al. (1999) cloned mouse Agtrap from a kidney cDNA library. The deduced 161-amino acid protein has a calculated molecular mass of 17.8 kD. It contains several extensive N-terminal hydrophobic domains, as well as potential sites for phosphorylation and N-glycosylation. Northern blot analysis detected transcripts of 1.2 and 0.8 kb in all mouse tissues examined, with relatively high levels in kidney, testis, and heart. PCR also detected Agtrap expression in mouse aortic tissue and vascular smooth muscle cells (VSMCs). By sequencing clones obtained from a fetal brain cDNA library, followed by EST database analysis, Wang et al. (2002) cloned human AGTRAP. The deduced 159-amino acid protein has a calculated molecular mass of 17.3 kD. AGTRAP has a 21-amino acid N-terminal transmembrane region that is followed by a conserved cysteine, which is potentially palmitoylated. Mouse and human AGTRAP share 74% amino acid homology. Northern blot analysis detected a 1.2-kb transcript in almost all tissues examined, with highest abundance in kidney, heart, pancreas, and thyroid.GENE FUNCTION
By affinity chromatography and coimmunoprecipitation experiments, Daviet et al. (1999) confirmed association between mouse Agtrap and At2r1a. Agtrap interacted specifically with the C-terminal domain of At2r1a, but not with the C-terminal domains of several other hormone receptors, including AT2R2 (300034), CHRM3 (118494), BDKRB2 (113503), EDNRB (131244), and ADRB2 (109690). Overexpression of Agtrap in COS-7 cells inhibited At2r1a activation of phospholipase C (see 607120). It did not affect Chrm3 activation. Cui et al. (2000) determined that transfection of mouse Agtrap into adult rat VSMCs potentiated At2r1 internalization upon angiotensin II (see 106150) stimulation. Receptor-induced DNA synthesis was inhibited in Agtrap-transfected VSMCs, and this was associated with inhibition of Stat3 (102582) and Akt (see 164730) phosphorylation. Cui et al. (2000) concluded that AGTRAP is a negative regulator of AT2R1-mediated cell proliferation in VSMCs. Using several assays of protein interaction, Wang et al. (2002) showed that AGTRAP interacted with RACK1 (176981). They suggested that the AGTRAP-RACK1 interaction may help recruit the signaling complex to AT2R1 and affect receptor signaling. Using a yeast 2-hybrid assay, Guo et al. (2005) demonstrated that mouse Caml (CAMLG; 601118) interacted with Atrap. The N-terminal hydrophilic domain of Caml mediated the interaction, and the proteins colocalized in the endoplasmic reticulum. Atrap knockdown increased NFAT (see NFATC2; 600490) activity, and overexpression of Atrap decreased angiotensin II- or Caml-induced NFAT transcriptional activation. Overexpression of the N-terminal ATRAP-interacting domain of Caml increased angiotensin II-induced NFAT promoter activity, whereas overexpression of the C-terminal end of Caml disrupted the effect of angiotensin II on NFAT signaling.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the AGTRAP gene to chromosome 1 (TMAP SHGC-32094). ... More on the omim web site
May 13, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 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
Oct. 27, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 608729 was added.
Feb. 25, 2016: Protein entry updated
Automatic update: model status changed
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed