Protein detail
IPSP
Plasma serine protease inhibitor (Acrosomal serine protease inhibitor) (Plasminogen activator inhibitor 3) (PAI-3) (PAI3) (Protein C inhibitor) (PCI) (Serpin A5)
Entry name IPSP | UniProt ID | EVMP confidence score 0.38 |
Supporting publications (n) | Transmembrane count | Protein classification Cancer-related genesCandidate cardiovascular disease genesPlasma proteinsPredicted secreted proteins |
EVMP confidence score
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40Basic Information10
Protein Names
Plasma serine protease inhibitor (Acrosomal serine protease inhibitor) (Plasminogen activator inhibitor 3) (PAI-3) (PAI3) (Protein C inhibitor) (PCI) (Serpin A5)
Protein Class (4)
Cancer-related genesCandidate cardiovascular disease genesPlasma proteinsPredicted secreted proteins
Protein Function (3)
- Candidate cardiovascular disease genes
- Cancer-related genes:Candidate cancer biomarkers
- Predicted secreted proteins
Ensembl
Entrez Gene Symbol
Gene Synonym (4)
PAI3PCIPLANH3PROCI
Gene Description
Serpin family A member 5
Chromosome
14
Position
94561442-94593118
EVMP confidence score
0.38
Fluorescence & Localization4
Tissue Specificbone marrowCell SpecificcDCBlood Cell Specificclassical monocyteBlood Lineage Specificdendritic cells
Function & Pathway7
Protein Function (3)
- Candidate cardiovascular disease genes
- Cancer-related genes:Candidate cancer biomarkers
- Predicted secreted proteins
Cellular Component (20)
- GO:0002080 acrosomal membrane
- GO:0005576 extracellular region
- GO:0005615 extracellular space
- GO:0009897 external side of plasma membrane
- GO:0016020 membrane
- GO:0031091 platelet alpha granule
- GO:0031094 platelet dense tubular network
- GO:0032991 protein-containing complex
- GO:0036024 protein C inhibitor-TMPRSS7 complex
- GO:0036025 protein C inhibitor-TMPRSS11E complex
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Molecular Function (8)
Biological Process (3)
Reactome (4)
Mediation Categories (3)
Clinical-translation mediationFusion and delivery mediationImmune mediation
Relations & Evidence20
Enzyme-Mediated Modification (1)
1 record.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| SERPINA5 | KLK2 | P20151 | R | 373 | cleavage | HPRD | HPRD:10209959 |
Ligand-Receptor Signaling (15)
15 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| ecm_regulator | ecm_regulator | OmniPath | Yes | No | Yes | No | No |
| secreted | secreted | UniProt_keyword | No | No | Yes | No | No |
| secreted | secreted | UniProt_location | No | No | Yes | No | No |
| secreted | secreted | HPA_secretome | No | No | Yes | No | No |
| secreted | secreted | OmniPath | No | No | Yes | No | No |
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Regulatory Interaction Network (1)
1 record.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| IPSP | P05154 | FINC | P02751 | Yes | No | Yes | SIGNOR | SIGNOR:24388360 |
Protein Complex Composition (3)
Sequence, Structure & Domains10
Sequences
Length
406
Mass
45,675
Sequence
MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRP
3D Structural Models
Turn
180..182; 248..251; 334..336
Helix
48..59; 69..81; 85..94; 101..117; 143..153; 165..179; 215..217; 275..281; 284..293; 314..316; 318..321; 325..327
Beta Strand
65..67; 123..135; 156..159; 195..211; 219..228; 230..247; 252..262; 264..270; 295..304; 306..313; 337..339; 343..355; 357..371; 372..375; 380..383; 388..404
3D Structure
X-ray crystallography (4)
Domain & Motif Annotations
Domain (CC)
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.
Protein Families
Serpin family
Sequence Similarities
Belongs to the serpin family.
Clinical Relevance5
Disease Involvement
Cancer-related genes
Related Diseases
Biomarker
Preclinical
Antibody