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Details on Person UniProt:P01009 SERPINA1

Class:Id	ReferenceGeneProduct:49238
_chainChangeLog	signal peptide:1-24 added on Fri February 6 2015;chain:25-418 added on Fri February 6 2015;peptide:375-418 added on Fri February 6 2015
_displayName	UniProt:P01009 SERPINA1
_timestamp	2026-02-20 21:36:36
chain	signal peptide:1-24 chain:25-418 peptide:375-418
checksum	7016555F273B7F16
comment	FUNCTION Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.FUNCTION Reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).SUBUNIT Interacts with CELA2A (PubMed:31358993). Interacts with ERGIC3 and LMAN1/ERGIC53 (PubMed:31142615). Interacts with PRSS1/trypsin (PubMed:11057674). Interacts with PRSS1/Trypsin (PubMed:11057674). The variants S and Z interact with CANX and PDIA3 (PubMed:23826168).INTERACTION The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum.SUBCELLULAR LOCATION Ubiquitous. Expressed in leukocytes and plasma.DOMAIN The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.PTM N-glycosylated. Differential glycosylation produces a number of isoforms. N-linked glycan at Asn-107 is alternatively di-antennary, tri-antennary or tetra-antennary. The glycan at Asn-70 is di-antennary with trace amounts of tri-antennary. Glycan at Asn-271 is exclusively di-antennary. Structure of glycans at Asn-70 and Asn-271 is Hex5HexNAc4. The structure of the antennae is Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure Man(alpha1-6)[Man(alpha1-3)]Man(beta1-4)GlcNAc(beta1-4)GlcNAc. Some antennae are fucosylated, which forms a Lewis-X determinant.PTM Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.PTM (Microbial infection) Proteolytically processed by Staphylococcus aureus seryl, cysteinyl, and metallo-proteases.POLYMORPHISM The sequence shown is that of the M1V allele which is the most common form of PI (44 to 49%). Other frequent alleles are: M1A 20 to 23%; M2 10 to 11%; M3 14 to 19%.DISEASE The disease is caused by variants affecting the gene represented in this entry.MISCELLANEOUS The aberrant form is found in the plasma of chronic smokers, and persists after smoking is ceased. It can still be found ten years after smoking has ceased.MISCELLANEOUS May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.SIMILARITY Belongs to the serpin family.SEQUENCE CAUTION Extended N-terminus.SEQUENCE CAUTION Extended N-terminus.ONLINE INFORMATION Alpha-1 antitrypsin entry
description	recommendedName: fullName evidence="52"Alpha-1-antitrypsin alternativeName: Alpha-1 protease inhibitor alternativeName: Alpha-1-antiproteinase alternativeName: Serpin A1 component recommendedName: Short peptide from AAT shortName: SPAAT /component
geneName	SERPINA1 AAT PI PRO0684 PRO2209
identifier	P01009
isSequenceChanged	FALSE
keyword	3D-structure Acute phase Alternative splicing Blood coagulation Direct protein sequencing Endoplasmic reticulum Extracellular matrix Glycoprotein Hemostasis Phosphoprotein Protease inhibitor Proteomics identification Reference proteome Secreted Serine protease inhibitor Signal
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20
name	SERPINA1
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:9003356] ENSEMBL:ENSG00000197249 SERPINA1 [Homo sapiens]
secondaryIdentifier	A1AT_HUMAN A6PX14 B2RDQ8 Q0PVP5 Q13672 Q53XB8 Q5U0M1 Q7M4R2 Q86U18 Q86U19 Q96BF9 Q96ES1 Q9P1P0 Q9UCE6 Q9UCM3
sequenceLength	418
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:217471] UniProt:P01009-2 SERPINA1 [Homo sapiens] [ReferenceIsoform:217472] UniProt:P01009-3 SERPINA1 [Homo sapiens] [ReferenceIsoform:402237] UniProt:P01009-1 SERPINA1 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:141755] SERPINA1 [platelet alpha granule lumen] [Homo sapiens] [EntityWithAccessionedSequence:141757] SERPINA1 [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:5689435] (Glc)3(GlcNAc)2(Man)9-SERPINA1 [endoplasmic reticulum lumen] [Homo sapiens] [EntityWithAccessionedSequence:5689731] (Glc)3(GlcNAc)2(Man)9-SERPINA1 [COPII-coated ER to Golgi transport vesicle] [Homo sapiens] [EntityWithAccessionedSequence:5689734] (Glc)3(GlcNAc)2(Man)9-SERPINA1 [endoplasmic reticulum-Golgi intermediate compartment membrane] [Homo sapiens] [EntityWithAccessionedSequence:6804783] SERPINA1 [ficolin-1-rich granule lumen] [Homo sapiens] [EntityWithAccessionedSequence:8956709] SERPINA1 [endoplasmic reticulum lumen] [Homo sapiens] [EntityWithAccessionedSequence:8957062] p-SERPINA1 [endoplasmic reticulum lumen] [Homo sapiens]
(referenceSequence)	[GroupModifiedResidue:5689434] N4-(N-acetylamino)glucosyl-L-asparagine (N-{alpha-Glc-(1->2)-alpha-Glc-(1->3)-alpha-Glc-(1->3)-alpha-Man-(1->2)-alpha-Man-(1->2)-alpha-Man-(1->3)-(alpha-Man-(1->2)-alpha-Man-(1->3)-(alpha-Man-(1->2)-alpha-Man-(1->6))-alpha-Man-(1->6))-beta-Man-(1->4)-beta-GlcNAc-(1->4)-beta-GlcNAc}-L-Asn residue (ChEBI:59084)) at unknown position [ModifiedResidue:8957052] phosphorylated residue at unknown position
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