SERPINA3 Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2. Belongs to the serpin family. Plasma. Synthesized in the liver. Like the related alpha-1-antitrypsin, its concentration increases in the acute phase of inflammation or infection. Found in the amyloid plaques from the hippocampus of Alzheimer disease brains. 3 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 12|12 E
Cellular Component:  extracellular region; extracellular space
Molecular Function:  peptidase inhibitor activity; serine-type endopeptidase inhibitor activity
Biological Process:  acute-phase response; negative regulation of endopeptidase activity; negative regulation of peptidase activity; response to bacterium; response to cytokine; response to peptide hormone
Reference #:  Q91WP6 (UniProtKB)
Alt. Names/Synonyms: alpha-1 antiproteinase; antitrypsin; OTTMUSP00000017513; serine (or cysteine) peptidase inhibitor, clade A, member 3N; serine (or cysteine) proteinase inhibitor, clade A, member 3N; serine protease inhibitor 2-2; Serine protease inhibitor A3N; Serpin A3N; SERPINA3; Serpina3n; SPA3N; Spi2; Spi2-2; Spi2.2; Spi2/eb.4
Gene Symbols: Serpina3n
Molecular weight: 46,718 Da
Basal Isoelectric point: 5.59  Predict pI for various phosphorylation states
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Protein Structure Not Found.

Cross-references to other databases:  STRING  |  BioGPS  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene