Serpin B12 (SERPINB12)
The protein contains 405 amino acids for an estimated molecular weight of 46276 Da.
Inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator. (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.
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.
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| Variant | Description |
|---|---|
| dbSNP:rs35582068 | |
| dbSNP:rs35352345 | |
| dbSNP:rs11664907 |
No binding partner found
Biological Process
Hematopoietic progenitor cell differentiation
Negative regulation of endopeptidase activity
Negative regulation of protein catabolic process
Neutrophil degranulation
The reference OMIM entry for this protein is 615662
Serpin peptidase inhibitor, clade b (ovalbumin), member 12; serpinb12
DESCRIPTION
Serpins inhibit serine or cysteine proteases via a 'suicide substrate' mechanism. Upon proteolytic cleavage of their pseudosubstrate bait sequence, serpins undergo a conformational change and form an inactivating covalent bond with the protease. SERPINB12 is a clade B serpin that shares sequence similarity with chicken ovalbumin. Clade B serpins lack an N-terminal signal sequence and N- and C-terminal extensions, and they localize predominantly to the cytoplasm (summary by Askew et al., 2001).CLONING
By searching a genomic database for clade B serpin sequences, followed by PCR of a testis cDNA library, Askew et al. (2001) cloned SERPINB12. The deduced 405-amino acid protein has a calculated molecular mass of 46.3 kD. SERPINB12 has a transmembrane domain near the N terminus and an alanine-rich hinge region and reactive-site loop near the C terminus. The reactive-site loop has an arg-ser pseudosubstrate bait sequence. SERPINB12 also has 6 putative N-glycosylation sites. Hemi-nested PCR detected SERPINB12 expression in approximately half of the 26 adult and fetal human tissues examined, including brain, lymphoid tissues, heart, lung, liver, pancreas, kidney, ovary, testis, and intestine.GENE FUNCTION
Askew et al. (2001) showed that recombinant human SERPINB12 completely inhibited the enzymatic activities of trypsin (see 276000)-like serine proteinases, including human and bovine trypsin and plasmin (173350), but not other serine or cysteine proteinases examined. SDS-PAGE analysis revealed that SERPINB12 formed a covalent complex with plasmin. Mass spectroscopy of the complex confirmed that SERPINB12 was cleaved at the arg-ser bond.GENE STRUCTURE
Askew et al. (2001) determined that the SERPINB12 gene contains 8 exons and spans over 10.8 kb. Exon 2 contains the translational start site.MAPPING
By genomic sequence analysis, Askew et al. (2001) mapped the SERPINB12 gene to an approximately 800-kb serpin gene cluster on chromosome 18q21.3. ... 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for SERPINB12
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 615662 was added.