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0PEDF_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSERPINF1
DescriptionPigment epithelium-derived factor precursor (pedf) (epc-1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005576 extracellular region (IDA)
0004867 serine-type endopeptidase inhibitor activity (TAS)
0008283 cell proliferation (TAS)
0007275 development (TAS)
0016525 negative regulation of angiogenesis (IDA)
0050769 positive regulation of neurogenesis (IDA)

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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:-123.568636235841 
Location:63-415
SequencesProtein: PEDF_HUMAN (418 aa)
mRNA: NM_002615
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 50 residues, 1612008-1612157Exon2: 32 residues, 1616946-1617038Exon3: 68 residues, 1619895-1620094Exon4: 54 residues, 1621072-1621228Exon5: 70 residues, 1621915-1622119Exon6: 49 residues, 1625101-1625244Exon7: 72 residues, 1626575-1626786Exon8: 131 residues, 1627230-1627617Exon9: 2 residues, -Jump to PEDF_HUMAN  
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Loci Cluster (Details)Loci: 4246 1314874-1342745 ~-28K 14799(MYO1C)(-)Loci: 4247 1483902-1495791 ~-12K 14809(SCARF1)(-)Loci: 2965 1612008-1627617 ~-16K 14821(SERPINF1)(+)Loci: 4245 1194594-1250267 ~-56K 14796(YWHAE)(-)Link out to UCSC