Q03044 · A1AT_DIDVI

Function

function

Inhibitor of serine proteases. The primary target is elastase, but also has a moderate affinity for plasmin and thrombin.

Features

Showing features for site.

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TypeIDPosition(s)Description
Site374-375Reactive bond

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular space
Molecular Functionserine-type endopeptidase inhibitor activity
Biological Processacute-phase response

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-1-antiproteinase
  • Alternative names
    • Alpha-1-antitrypsin
    • Alpha-1-proteinase inhibitor

Organism names

Accessions

  • Primary accession
    Q03044

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_000003238422-410Alpha-1-antiproteinase
Glycosylation63N-linked (GlcNAc...) asparagine
Glycosylation100N-linked (GlcNAc...) asparagine
Glycosylation264N-linked (GlcNAc...) asparagine
Modified residue375Phosphoserine

Keywords

Expression

Tissue specificity

Plasma.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region365-384RCL

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 (By similarity).

Sequence similarities

Belongs to the serpin family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    410
  • Mass (Da)
    46,441
  • Last updated
    1994-02-01 v1
  • Checksum
    2A6718C1B2FAA389
MMPSTLSLCLMLAGLCSLVTSHLTEEIQASNDTENEYSSTRRISPYMTDFSIDFYRLLVSKSNTTNIFFSPISIYTAFTLLALGAKSATRDQILTGLRFNRTEISEEHIFEGFQQLLNTFNLPENELQLTTSNGLFIDKNLKLVAKFLEDSKRLYASDTFSTNFEDNMAAKKQINDYVEKETQGKIVDLIQNLDSNVVFVLVNCIFFKGKWEKPFMTELTTECPFHVDSKTTVPVQTMRRLGMFNVFYDQDLSCWVLKMKYMGNATALFILPDTGKIEKVENALNKMLFHKWTRNLKRRAISLYFPKVSISGNYDLKILRELGITDVFGSNADLSGITEETNLKLSQAVHKAVVNIDEKGTEASGATFAEGIPMSIPPTVEFLRPFIFIILEENTKSVLFMGKVMNPTGN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z18906
EMBL· GenBank· DDBJ
CAA79343.1
EMBL· GenBank· DDBJ
mRNA
L06824
EMBL· GenBank· DDBJ
AAC02630.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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