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0AACT_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSERPINA3
DescriptionAlpha-1-antichymotrypsin precursor (act) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005576 extracellular region (NAS)
0005622 intracellular (NAS)
0030569 chymotrypsin inhibitor activity (NAS)
0003677 DNA binding (IC)
0005515 protein binding (IPI)
0006954 inflammatory response (NAS)
0019216 regulation of lipid metabolism (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors.espectively. In many cases they are synthesised as part of a larger precursor protein.ither as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Serpins (SERine Proteinase INhibitors) belong to MEROPS inhibitor family I4.lan ID. Serpins are proteins that are primarily known as irreversible serine protease inhibitors active against S1 ().8 () and C14 () peptidases. There are both extra- and intra-cellular serpins.hich are found in all groups of organisms with the notable exception of fungi .Serpins and their homologues are a group of high molecular weight (40 to 50 kDa) structurally related proteins involved in a number of fundamental biological processes such as blood coagulation.omplement activation.ibrinolysis.ngiogenesis.nflammation.umour suppression and hormone transport. All known serpins have been classified into 16 clades and 10 orphan sequences.he vertebrate serpins can be conveniently classified into six sub-groups . In human plasma they represent approximately 2% of the total protein.f which 70% is alpha-1-antitrypsin. In contrast to "rigid" proteinase inhibitors.uch as those of the Kunitz or Kazal families.he serpins are metastable proteins (active-state proteins) which interact with their substrate and irreversibly trap the acyl intermediate as a result of a major conformational change ; they are best described as suicide substrate inhibitors. The common structure of these proteins is a multi-domain fold containing a bundle of 8 or 9 alphahelices and a beta sandwich formed by 3 beta sheets. The reactive centre loop (RCL) is found in the C-terminal part of these proteins. On the basis of strong sequence similarities. number of proteins with noknown inhibitory activity are said to belong to this family.hese include: angiotensinogen.orticosteroid-binding globulin and thyroxin-binding globulin .
  IPR000215:Proteinase inhibitor I4, serpin
IPR000215:Serpin 
Evalue:-217.552841186523 
Location:43-420
SequencesProtein: AACT_HUMAN (423 aa)
mRNA: NM_001085
Local Annotation
Synapse Ontology
Microglias, one kind of glias in CNS, are responsible for removing most of the waste and cellular debris from the CNS
sdb:0267 removing metabolic mass  (Evidence:keywords)
KO assignmentK04525
  Level 3 annotation:
    serine (or cysteine) proteinase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3
  Level 2 annotation:
    Non-enzyme
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 24 residues, 94148466-94148537Exon2: 219 residues, 94150523-94151174Exon3: 93 residues, 94155284-94155558Exon4: 52 residues, 94158430-94158581Exon5: 149 residues, 94159700-94160142Exon6: 2 residues, -Jump to AACT_HUMAN  
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