Alpha-1-antitrypsin

Details

Name
Alpha-1-antitrypsin
Synonyms
  • AAT
  • Alpha-1 protease inhibitor
  • Alpha-1-antiproteinase
  • PI
  • Serpin A1
Gene Name
SERPINA1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0001896|Alpha-1-antitrypsin
MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFS
LYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGF
QELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQ
INDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTV
KVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFL
ENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKA
VLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
Number of residues
418
Molecular Weight
46736.195
Theoretical pI
5.31
GO Classification
Functions
glycoprotein binding / identical protein binding / protease binding / serine-type endopeptidase inhibitor activity
Processes
acute-phase response / blood coagulation / cellular protein metabolic process / COPII vesicle coating / ER to Golgi vesicle-mediated transport / membrane organization / negative regulation of endopeptidase activity / platelet activation / platelet degranulation / post-translational protein modification / protein N-linked glycosylation via asparagine
Components
endoplasmic reticulum / endoplasmic reticulum lumen / endoplasmic reticulum-Golgi intermediate compartment membrane / ER to Golgi transport vesicle / extracellular exosome / extracellular region / extracellular space / Golgi apparatus / Golgi membrane / platelet alpha granule lumen / proteinaceous extracellular matrix
General Function
Serine-type endopeptidase inhibitor activity
Specific 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.Short peptide from AAT: 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).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0020495|Alpha-1-antitrypsin (SERPINA1)
ATGCCGTCTTCTGTCTCGTGGGGCATCCTCCTGCTGGCAGGCCTGTGCTGCCTGGTCCCT
GTCTCCCTGGCTGAGGATCCCCAGGGAGATGCTGCCCAGAAGACAGATACATCCCACCAT
GATCAGGATCACCCAACCTTCAACAAGATCACCCCCAACCTGGCTGAGTTCGCCTTCAGC
CTATACCGCCAGCTGGCACACCAGTCCAACAGCACCAATATCTTCTTCTCCCCAGTGAGC
ATCGCTACAGCCTTTGCAATGCTCTCCCTGGGGACCAAGGCTGACACTCACGATGAAATC
CTGGAGGGCCTGAATTTCAACCTCACGGAGATTCCGGAGGCTCAGATCCATGAAGGCTTC
CAGGAACTCCTCCGTACCCTCAACCAGCCAGACAGCCAGCTCCAGCTGACCACCGGCAAT
GGCCTGTTCCTCAGCGAGGGCCTGAAGCTAGTGGATAAGTTTTTGGAGGATGTTAAAAAG
TTGTACCACTCAGAAGCCTTCACTGTCAACTTCGGGGACACCGAAGAGGCCAAGAAACAG
ATCAACGATTACGTGGAGAAGGGTACTCAAGGGAAAATTGTGGATTTGGTCAAGGAGCTT
GACAGAGACACAGTTTTTGCTCTGGTGAATTACATCTTCTTTAAAGGCAAATGGGAGAGA
CCCTTTGAAGTCAAGGACACCGAGGAAGAGGACTTCCACGTGGACCAGGTGACCACCGTG
AAGGTGCCTATGATGAAGCGTTTAGGCATGTTTAACATCCAGCACTGTAAGAAGCTGTCC
AGCTGGGTGCTGCTGATGAAATACCTGGGCAATGCCACCGCCATCTTCTTCCTGCCTGAT
GAGGGGAAACTACAGCACCTGGAAAATGAACTCACCCACGATATCATCACCAAGTTCCTG
GAAAATGAAGACAGAAGGTCTGCCAGCTTACATTTACCCAAACTGTCCATTACTGGAACC
TATGATCTGAAGAGCGTCCTGGGTCAACTGGGCATCACTAAGGTCTTCAGCAATGGGGCT
GACCTCTCCGGGGTCACAGAGGAGGCACCCCTGAAGCTCTCCAAGGCCGTGCATAAGGCT
GTGCTGACCATCGACGAGAAAGGGACTGAAGCTGCTGGGGCCATGTTTTTAGAGGCCATA
CCCATGTCTATCCCCCCCGAGGTCAAGTTCAACAAACCCTTTGTCTTCTTAATGATTGAA
CAAAATACCAAGTCTCCCCTCTTCATGGGAAAAGTGGTGAATCCCACCCAAAAATAA
Chromosome Location
14
Locus
14q32.1
External Identifiers
ResourceLink
UniProtKB IDP01009
UniProtKB Entry NameA1AT_HUMAN
GenBank Protein ID177829
GenBank Gene IDK01396
GenAtlas IDSERPINA1
HGNC IDHGNC:8941
General References
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  63. Lovegrove JU, Jeremiah S, Gillett GT, Temple IK, Povey S, Whitehouse DB: A new alpha 1-antitrypsin mutation, Thr-Met 85, (PI Zbristol) associated with novel electrophoretic properties. Ann Hum Genet. 1997 Sep;61(Pt 5):385-91. [PubMed:9459000]
  64. Jardi R, Rodriguez F, Miravitlles M, Vidal R, Cotrina M, Quer J, Pascual C, Weidinger S: Identification and molecular characterization of the new alpha-1-antitrypsin deficient allele PI Y barcelona (Asp256-->Val and Pro391-->His). Mutations in brief no. 174. Online. Hum Mutat. 1998;12(3):213. [PubMed:10651487]
  65. Seixas S, Garcia O, Amorim A, Rocha J: A novel alpha-1-antitrypsin r281del variant found in a population sample from the Basque country. Hum Mutat. 2000 Jan;15(1):121-2. [PubMed:10612848]
  66. Marques PI, Ferreira Z, Martins M, Figueiredo J, Silva DI, Castro P, Morales-Hojas R, Simoes-Correia J, Seixas S: SERPINA2 is a novel gene with a divergent function from SERPINA1. PLoS One. 2013 Jun 24;8(6):e66889. doi: 10.1371/journal.pone.0066889. Print 2013. [PubMed:23826168]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB019982-[3,4-Dihydroxy-2-Hydroxymethyl-5-(2-Hydroxy-Nonyl)-Tetrahydro-Furan-2-Yloxy]-6-Hydroxymethyl-Tetra Hydro-Pyran-3,4,5-TriolexperimentalunknownDetails
DB03345MercaptoethanolexperimentalunknownDetails
DB05481Recombinant alpha 1-antitrypsininvestigationalunknownDetails
DB05961PPL-100investigationalunknownDetails
DB09130Copperapproved, investigationalunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB14007Pentetic acidapprovednosubstrateDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownDetails