| IED ID | IndEnz0002006506 |
| Enzyme Type ID | protease006506 |
| Protein Name |
Plasma serine protease inhibitor Acrosomal serine protease inhibitor Plasminogen activator inhibitor 3 PAI-3 PAI3 Protein C inhibitor PCI Serpin A5 |
| Gene Name | SERPINA5 PCI PLANH3 PROCI |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRP |
| Enzyme Length | 406 |
| Uniprot Accession Number | P05154 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Its inhibitory activity is greatly enhanced in the presence of glycosaminoglycans, heparin, thrombomodulin and phospholipids vesicles. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | 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 a hydrophobic hormone carrier by its binding to retinoic acid. {ECO:0000269|PubMed:10340997, ECO:0000269|PubMed:11722589, ECO:0000269|PubMed:14696115, ECO:0000269|PubMed:15140131, ECO:0000269|PubMed:15328353, ECO:0000269|PubMed:15853774, ECO:0000269|PubMed:1725227, ECO:0000269|PubMed:18467335, ECO:0000269|PubMed:2844223, ECO:0000269|PubMed:3501295, ECO:0000269|PubMed:6323392, ECO:0000269|PubMed:7521127, ECO:0000269|PubMed:7548057, ECO:0000269|PubMed:8536714, ECO:0000269|PubMed:8665956, ECO:0000269|PubMed:9473218, ECO:0000269|PubMed:9510955, ECO:0000269|PubMed:9556620}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (16); Chain (1); Glycosylation (4); Helix (12); Mutagenesis (14); Natural variant (8); Propeptide (1); Sequence conflict (5); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Direct protein sequencing;Fertilization;Glycoprotein;Heparin-binding;Lipid transport;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor;Signal;Transport |
| Interact With | P02751 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:1725227, ECO:0000269|PubMed:18467335, ECO:0000269|PubMed:7521127, ECO:0000269|PubMed:8536714, ECO:0000269|PubMed:9510955, ECO:0000269|PubMed:9556620}. 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 granules in resting platelets and on the external plasma membrane and within the surface-connected cannalicular system in activated platelets. |
| Modified Residue | |
| Post Translational Modification | PTM: N- and O-glycosylated. N-glycosylation consists of a mixture of sialylated bi- (including sialyl-Lewis X epitopes), tri- and tetra-antennary complex-type chains; affects the maximal heparin- and thrombomodulin-enhanced rates of thrombin inhibition. O-glycosylated with core 1 or possibly core 8 glycans. Further modified with 2 sialic acid residues. {ECO:0000269|PubMed:12575940, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18467335, ECO:0000269|PubMed:21056543, ECO:0000269|PubMed:22171320}.; PTM: Proteolytically cleaved. Inhibition of proteases is accompanied by formation of a stable enzyme-inhibitor complex and by degradation of the serpin to lower molecular weight derivatives. Proteolytically cleaved at the N-terminus; inhibits slightly the heparin- and thrombomodulin-enhanced rates of thrombin inhibition. {ECO:0000269|PubMed:15328353, ECO:0000269|PubMed:18467335}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:2556811 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1LQ8; 2HI9; 2OL2; 3DY0; |
| Mapped Pubmed ID | 10781579; 11161981; 11686324; 11864713; 14982929; 15377716; 15878512; 16169070; 17258797; 17332248; 17450526; 18184931; 18193533; 19765701; 19913121; 20019810; 2019570; 20409682; 20628086; 20711500; 21102419; 21988832; 22205989; 22206708; 23520464; 23670045; 24222120; 24388360; 2502206; 2505252; 25814554; 25887633; 27207655; 2742826; 28270177; 2866798; 29187436; 30715578; 3082357; 31336797; 3134349; 34009669; 8338946; 9888880; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,675 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |