UniProt Accession

 A1AT_HUMAN; P01009; A6PX14; B2RDQ8; Q0PVP5; Q13672; Q53XB8; Q5U0M1; Q7M4R2; Q86U18; Q86U19; Q96BF9; Q96ES1; Q9P1P0; Q9UCE6; Q9UCM3 

Genbank Protein ID

 K01396; K02212; X01683; M11465; J02619; DQ682455; AM048838; AF113676; AF130068; BX161449; BX247968; BX248002; BX248257; AK315637; BT019455; BC011991; BC015642; J00064; J00066; J00065; J00067; X02920; V00496; M26123 

Genbank Nucleotide ID

 AAB59375.1; AAB59495.1; CAA25838.1; AAA51546.1; AAA51547.1; ABG73380.1; CAJ15161.1; AAF29581.1; AAG35496.1; CAD61914.1; CAD62306.1; CAD62334.1; CAD62585.1; BAG38005.1; AAV38262.1; AAH11991.1; AAH15642.1; AAB59369.1; AAB59370.1; AAB59370.1; AAB59371.1; CAA26677.1; CAA23755.1; AAA51545.1 

Protein Name

 Alpha-1-antitrypsin 

Protein Synonyms/Alias

 Alpha-1 protease inhibitor; Alpha-1-antiproteinase; Serpin A1; Short peptide from AAT; SPAAT 

Gene Name

 SERPINA1 

Gene Synonyms/Alias

 AAT; PI; PRO0684; PRO2209 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
153	EGLKLVDKFLEDVKK	glycation	[1]
187	QINDYVEKGTQGKIV	glycation	[1]
192	VEKGTQGKIVDLVKE	glycation	[1]
198	GKIVDLVKELDRDTV	acetylation	[2]

Reference

 [1] Proteomic profiling of nonenzymatically glycated proteins in human plasma and erythrocyte membranes.
 Zhang Q, Tang N, Schepmoes AA, Phillips LS, Smith RD, Metz TO.
 J Proteome Res. 2008 May;7(5):2025-32. [PMID: 18396901]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

Functional Description

 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. 

Sequence Annotation

 REGION 368 392 RCL.
 MOD_RES 256 256 S-cysteinyl cysteine.
 CARBOHYD 70 70 N-linked (GlcNAc...) (complex).
 CARBOHYD 107 107 N-linked (GlcNAc...) (complex).
 CARBOHYD 271 271 N-linked (GlcNAc...) (complex).  

Keyword

 3D-structure; Acute phase; Alternative splicing; Blood coagulation; Complete proteome; Direct protein sequencing; Extracellular matrix; Glycoprotein; Hemostasis; Polymorphism; Protease inhibitor; Reference proteome; Secreted; Serine protease inhibitor; Signal. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 418 AA 

Protein Sequence

Gene Ontology

 GO:0005615; C:extracellular space; IMP:UniProtKB.
 GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
 GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
 GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB.
 GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0030162; P:regulation of proteolysis; IBA:RefGenome. 

Interpro

 IPR023795; Protease_inhib_I4_serpin_CS.
 IPR023796; Serpin_dom.
 IPR000215; Serpin_fam. 

Pfam

 PF00079; Serpin 

SMART

 SM00093; SERPIN 

PROSITE

 PS00284; SERPIN 

PRINTS