| Protein Name :
Plasma serine protease inhibitor
UniProtKB / Swiss-Prot ID : IPSP_HUMAN
Gene Name (Synonyms) :
SERPINA5, PCI, PLANH3, PROCI
Species : Homo sapiens (Human).
Subcellular Localization : Secreted, extracellular space. Note=Localized on the plasma membrane overlying the acrosomal head of spermatozoa of ependymal spermatozoa and ejaculated sperm. Localized at the equatorial segment of acrosome-reacted spematozoa. Localized in alpha granule
Protein Function : Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and proinflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary- type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue-and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as an hydrophobic hormone carrier by its binding to retinoic acid.
|Predicted Secondary Structure
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| Overview of Protein Modification Sites with Functional and Structural Information
|Accessible Surface Area (ASA)|
Experimental PTM Sites
|Predicted PTM Sites|
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Experimental Post-Translational Modification Sites
|There are no disease associations of PTM sites.|
|Related Literatures of Post-Translational Modification|
|"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";|
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249, AND MASSSPECTROMETRY.
|"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";|
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-262 AND ASN-338, AND MASSSPECTROMETRY.
|"N-glycans and the N terminus of protein C inhibitor affect thecofactor-enhanced rates of thrombin inhibition.";|
Sun W., Parry S., Panico M., Morris H.R., Kjellberg M., Engstrom A.,Dell A., Schedin-Weiss S.;
J. Biol. Chem. 283:18601-18611(2008).
Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, GLYCOSYLATION AT ASN-249; ASN-262 ANDASN-338, STRUCTURE OF CARBOHYDRATES, SUBCELLULAR LOCATION, TISSUESPECIFICITY, AND MASS SPECTROMETRY.
|"Crystal structure of protein C inhibitor provides insights intohormone binding and heparin activation.";|
Huntington J.A., Kjellberg M., Stenflo J.;
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 30-406, AND GLYCOSYLATION ATASN-262.
|"Further insight into the roles of the glycans attached to human bloodprotein C inhibitor.";|
Sun W., Parry S., Ubhayasekera W., Engstrom A., Dell A.,Schedin-Weiss S.;
Biochem. Biophys. Res. Commun. 403:198-202(2010).
Cited for: GLYCOSYLATION AT THR-39, AND MASS SPECTROMETRY.
|"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";|
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT THR-39, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.
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