Gamma-glutamylaminecyclotransferase (GGACT)
The protein contains 153 amino acids for an estimated molecular weight of 17329 Da.
Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L-proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
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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No binding partner found
The reference OMIM entry for this protein is 613378
Aig2-like domain-containing protein 1; a2ld1
Gamma-glutamylamine cyclotransferase; ggact
DESCRIPTION
Proteolytic degradation of crosslinked fibrin (see FGA; 134820) results in the formation of the isodipeptide L-gamma-glutamyl-L-epsilon-lysine. Breakdown of this molecule is catalyzed by the gamma-glutamylamine cyclotransferase A2LD1, which cyclizes the gamma-glutamyl moiety to produce 5-oxo-L-proline and free alkylamine (Oakley et al., 2010).CLONING
By searching an EST database for genes encoding proteins with a GGCT (137170)-like fold, Oakley et al. (2010) identified A2LD1. The deduced 153-amino acid protein has a calculated molecular mass of 17.3 kD.GENE FUNCTION
Oakley et al. (2010) showed that recombinant human GGACT hydrolyzed L-gamma-glutamyl-L-epsilon-lysine, but it was inactive against L-gamma-glutamyl-alpha amino acids. Oakley et al. (2010) noted that this substrate specificity is opposite that found for GGCT. Mutation of glu82 rendered GGACT inactive.BIOCHEMICAL FEATURES
Oakley et al. (2010) found that the crystal structure of recombinant human GGACT was similar to that of GGCT, with a 5-stranded beta barrel decorated with helices and connecting loops, including characteristic crossover strands. Crystallization of GGACT in the presence of the product 5-oxo-L-proline unambiguously identified the active-site cavity on the side of the barrel adjacent to strands beta-1 and beta-5. Mutation of glu82 rendered GGACT inactive, but it did not alter the GGACT structure. Oakley et al. (2010) noted that GGACT and GGCT share less than 10% amino acid identity, suggesting that the similarity in their 3-dimensional structure is an example of convergent evolution in the catalytic mechanism.GENE STRUCTURE
Oakley et al. (2010) determined that the A2LD1 gene contains 2 exons and spans 2.2 kb. Only the second exon is protein coding.MAPPING
By genomic sequence analysis, Oakley et al. (2010) mapped the A2LD1 gene to chromosome 13q32.3. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 613378 was added.
Feb. 23, 2019: Protein entry updated
Automatic update: comparative model was added.
Feb. 23, 2019: Protein entry updated
Automatic update: model status changed
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).