Alpha-1-acid glycoprotein 1 (ORM1)
The protein contains 201 amino acids for an estimated molecular weight of 23512 Da.
Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction. (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.
- 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
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 |
|---|---|
| allele ORM1*S | |
| dbSNP:rs3182034 | |
| allele ORM1*F2 |
Biological Process
Acute-phase response
Inflammatory response
Negative regulation of interleukin-6 production
Negative regulation of tumor necrosis factor production
Neutrophil degranulation
Platelet degranulation
Positive regulation of interleukin-1 beta production
Positive regulation of interleukin-1 beta secretion
Positive regulation of interleukin-1 production
Positive regulation of interleukin-1 secretion
Positive regulation of tumor necrosis factor production
Positive regulation of tumor necrosis factor secretion
Regulation of immune system process
Transport
Cellular Component
Blood microparticle
Collagen-containing extracellular matrix
Extracellular exosome
Extracellular matrix
Extracellular region
Extracellular space
Platelet alpha granule lumen
Specific granule lumen
Tertiary granule lumen
Molecular Function
The reference OMIM entry for this protein is 138600
Orosomucoid 1; orm1
Orm
Glycoprotein, alpha-1-acid, of serum
Alpha-1-acid glycoprotein
Alpha-1-agp; agp1
DESCRIPTION
Alpha-1-acid glycoprotein, or orosomucoid, is a relatively abundant plasma protein synthesized in the liver. It has a molecular weith of 40,000 Da and is a single polypeptide chain of about 180 amino acids. AGP is considered an acute phase reactant; its plasma levels increase several fold during acute infections (summary by Dente et al., 1985).CLONING
Board et al. (1986) isolated a cDNA clone for ORM and compared the derived amino acid sequence with preexisting data. Dente et al. (1988) studied the regulation of AGP-A by transfecting cell lines and preparing transgenic mice with constructs including the entire AGP gene. The AGP constructs were expressed with comparable efficiency in hepatoma and HeLa cells; however, these same constructs were expressed in transgenic mice in a tissue-specific manner. The mRNA was found solely in the liver. These authors found that a 6.6-kb segment consisting of the entire coding region plus 1.2 kb of 5-prime-flanking and 2 kb of 3-prime-flanking DNA contained sufficient information for tissue-specific, regulated expression of the gene. Tomei et al. (1989) generated families of transgenic mice carrying various orosomucoid genes and studied the ORM variants secreted into the serum of the mice.GENE STRUCTURE
Board et al. (1986) presented the complete nucleotide sequence encoding orosomucoid. Dente et al. (1987) cloned the genomic DNA segment encoding orosomucoid and showed that it contains 3 adjacent coding regions which they designated acid glycoprotein (AGP)-A, AGP-B, and AGP-B-prime. The regions were identical in exon-intron organization but had slightly different coding potentials. These results accounted for the heterogeneity observed by protein sequencing. Southern blot analysis indicated that the cloned cluster contains all the orosomucoid coding sequences present in the human genome. Most of the alpha-AGP mRNA in human liver is transcribed from AGP-A, whose promoter and cap site have been determined, while the level of AGP-B and B-prime mRNA in human liver is very low. The tandemly arranged ORM1 and ORM2 (138610) genes (also designated AGP1 and AGP2, respectively) span about 11.5 kb. Each gene contains 6 exons and encodes a 183-amino acid polypeptide (Yuasa et al., 1997).MAPPING
The structural gene for orosomucoid (ORM1) was assigned to the end of the long arm of chromosome 9 by demonstration of linkage to ABO and AK1 (Eiberg et al., 1982). The male lod score for ORM versus ABO was 5.06 at theta 0.27; for ABO versus AK, 6.27 at theta 0.13; for ORM versus AK, 1.63 at theta 0.17. Thus, the order was judged to be ORM-AK-ABO. Cox and Francke (1985) used hybrids of human fetal liver and rat hepatoma cells to study the location of the genes for serum proteins. In this way they gave direct assignment of the orosomucoid gene to chromosome 9 and the alpha-2-HS-glycoprotein gene to chromosome 3, these having been previously assigned by linkage to 'anchor' loci. Rocchi et al. (1986) confirmed the assignment of ORM to chromosome 9 by Southern blot analysis of DNA from somatic cell hybrids using a cDNA probe. On the basis of studies in members of 3 Newfoundland kindreds with the same specific chromosome 9 aberration, an inverted paracentric insertion, inv ins(9)(q22.1q34.3q34.1), Allderdice et al. (1986) concluded that ORM is located in 9q34.3-qter. Gene cloning studies by Dente et al. (1985) suggested that there are at least 2 genes coding for alpha-1-A ... More on the omim web site
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 25, 2017: Additional information
No protein expression data in P. Mayeux work for ORM1
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 138600 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed