Ester hydrolase C11orf54 (C11orf54)
The protein contains 315 amino acids for an estimated molecular weight of 35117 Da.
Exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- 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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Biological Process
The reference OMIM entry for this protein is 615810
Chromosome 11 open reading frame 54; c11orf54
Ptd012
CLONING
Manjasetty et al. (2006) reported that the C11ORF54 gene, which they called PTD012, generates 6 splice variants. One of the longer isoforms, which contains 315 amino acids, has orthologs in mouse, fish, fly, fungus, and nematode.GENE FUNCTION
Manjasetty et al. (2006) found that the recombinant 315-amino acid isoform of human PTD012 showed ester hydrolase activity against p-nitrophenyl acetate, forming nitrophenolate and acetate, when expressed in E. coli. PTD012 did not show carbonic anhydrase or carboxypeptidase activity.BIOCHEMICAL FEATURES
By examining the crystal structure of recombinant human PTD012, Manjasetty et al. (2006) concluded that the protein exists as a monomer in solution. PTD012 assumed a roughly globular shape, composed of 20 beta strands and 4 alpha helices, with a diameter of approximately 45 angstroms. Nine antiparallel beta strands formed a beta-screw region structurally similar to the cAMP-binding domain of the regulatory subunit of protein kinase A (PRKAR1A; 188830). This region of PTD012 and PRKAR1A also has an HxH motif that is predicted to coordinate zinc. The zinc-binding site of PTD012 bound an acetate molecule taken from the crystallization buffer. Manjasetty et al. (2006) noted that acetate is a product of hydrolysis of p-nitrophenyl acetate by PTD012, suggesting that acetate bound to zinc may represent an enzyme-product complex.MAPPING
Hartz (2014) mapped the C11ORF54 gene to chromosome 11q21 based on an alignment of the C11ORF54 sequence (GenBank GENBANK AF092133) with the genomic sequence (GRCh37). ... More on the omim web site
Nov. 17, 2018: Protein entry updated
Automatic update: OMIM entry 615810 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).