SERPINA5
entrez
5104
canonical
uniprot
P05154
canonical
ensembl
ENSG00000188488
resolver
ensp
ENSP00000333203
resolver
ensp
ENSP00000450837
resolver
ensp
ENSP00000451126
resolver
ensp
ENSP00000451610
resolver
ensp
ENSP00000554803
resolver
ensp
ENSP00000554804
resolver
ensp
ENSP00000554805
resolver
ensp
ENSP00000554806
resolver
ensp
ENSP00000554808
resolver
ensp
ENSP00000554810
resolver
ensp
ENSP00000554811
resolver
ensp
ENSP00000554812
resolver
ensp
ENSP00000554813
resolver
ensp
ENSP00000554814
resolver
ensp
ENSP00000554815
resolver
ensp
ENSP00000639546
resolver
ensp
ENSP00000639547
resolver
ensp
ENSP00000639548
resolver
enst
ENST00000329597
resolver
enst
ENST00000553780
resolver
enst
ENST00000554276
resolver
enst
ENST00000554866
resolver
enst
ENST00000884744
resolver
enst
ENST00000884745
resolver
enst
ENST00000884746
resolver
enst
ENST00000884747
resolver
enst
ENST00000884749
resolver
enst
ENST00000884751
resolver
enst
ENST00000884752
resolver
enst
ENST00000884753
resolver
enst
ENST00000884754
resolver
enst
ENST00000884755
resolver
enst
ENST00000884756
resolver
enst
ENST00000969487
resolver
enst
ENST00000969488
resolver
enst
ENST00000969489
resolver
genesymbol
SERPINA5
resolver
genesymbol_syn
PCI
resolver
genesymbol_syn
PLANH3
resolver
genesymbol_syn
PROCI
resolver
hgnc
HGNC:8723
resolver
uniprot
B4DDH1
resolver
uniprot
Q07616
resolver
uniprot
Q9UG30
resolver
uniprot_entry
B4DDH1_HUMAN
resolver
uniprot_entry
IPSP_HUMAN
resolver
uniprot_sec
Q07616
resolver
uniprot_sec
Q9UG30
resolver
activity_regulation
ACTIVITY REGULATION: Its inhibitory activity is greatly enhanced in the presence of glycosaminoglycans, heparin, thrombomodulin and phospholipids vesicles.
uniprot
proteins
amino_acid_sequence
MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRP
uniprot
proteins
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 pro-inflammatory 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}.
uniprot
proteins
mass_dalton
45675
uniprot
proteins
mutagenesis
MUTAGEN 248; /note="R->E: Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Strongly reduces the rate of thrombin inhibition in the presence of heparin."; /evidence="ECO:0000269|PubMed:18974053"; MUTAGEN 253; /note="R->E: Inhibits strongly thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin."; /evidence="ECO:0000269|PubMed:18362344"; MUTAGEN 272; /note="E->K: Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin."; /evidence="ECO:0000269|PubMed:18362344"; MUTAGEN 274; /note="K->E: Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin."; /evidence="ECO:0000269|PubMed:18362344"; MUTAGEN 285; /note="K->E: Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Slightly reduces the rate of thrombin inhibition in the presence of heparin. Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin."; /evidence="ECO:0000269|PubMed:18362344, ECO:0000269|PubMed:18974053"; MUTAGEN 288; /note="R->E: Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Slightly reduces the rate of thrombin inhibition in the presence of heparin. Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin."; /evidence="ECO:0000269|PubMed:18362344, ECO:0000269|PubMed:18974053"; MUTAGEN 289; /note="K->E: Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Slightly reduces the rate of thrombin inhibition in the presence of heparin. Inhibits weakly thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin."; /evidence="ECO:0000269|PubMed:18362344, ECO:0000269|PubMed:18974053"; MUTAGEN 292; /note="K->E: Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Slightly reduces the rate of thrombin inhibition in the presence of heparin. Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin."; /evidence="ECO:0000269|PubMed:18362344, ECO:0000269|PubMed:18974053"; MUTAGEN 360; /note="T->R: Inhibits heterodimer formation with TMPRSS11E."; /evidence="ECO:0000269|PubMed:15328353"; MUTAGEN 371; /note="T->R: Increases inhibition of activated protein C/F5 and factor XI/F11 activities. Decreases inhibition of thrombin activity."; /evidence="ECO:0000269|PubMed:7548057"; MUTAGEN 372; /note="F->P,G: Increases inhibition of thrombin activity."; /evidence="ECO:0000269|PubMed:7548057"; MUTAGEN 373; /note="R->P: Increases inhibition of thrombin activity. Inhibits heterodimer formation with TMPRSS11E."; /evidence="ECO:0000269|PubMed:15328353, ECO:0000269|PubMed:7548057"; MUTAGEN 376; /note="R->P: Does not change inhibition of thrombin, activated protein C/F5 and factor XI/F11 activities."; /evidence="ECO:0000269|PubMed:7548057"; MUTAGEN 381; /note="R->E: Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin."; /evidence="ECO:0000269|PubMed:18362344
uniprot
proteins
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}.
uniprot
proteins
protein_family
Serpin family
uniprot
proteins
pubmed
10340997
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
11722589
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12575940
uniprot
proteins
pubmed
1372913
uniprot
proteins
pubmed
14696115
uniprot
proteins
pubmed
14760718
uniprot
proteins
pubmed
15140131
uniprot
proteins
pubmed
15328353
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15853774
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
1714450
uniprot
proteins
pubmed
1725227
uniprot
proteins
pubmed
17337440
uniprot
proteins
pubmed
17706750
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18362344
uniprot
proteins
pubmed
18467335
uniprot
proteins
pubmed
18974053
uniprot
proteins
pubmed
21056543
uniprot
proteins
pubmed
2172989
uniprot
proteins
pubmed
2173165
uniprot
proteins
pubmed
22171320
uniprot
proteins
pubmed
2556811
uniprot
proteins
pubmed
2844223
uniprot
proteins
pubmed
3027058
uniprot
proteins
pubmed
3501295
uniprot
proteins
pubmed
6323392
uniprot
proteins
pubmed
7521127
uniprot
proteins
pubmed
7548057
uniprot
proteins
pubmed
8148499
uniprot
proteins
pubmed
8471250
uniprot
proteins
pubmed
8536714
uniprot
proteins
pubmed
8665956
uniprot
proteins
pubmed
8713781
uniprot
proteins
pubmed
9473218
uniprot
proteins
pubmed
9510955
uniprot
proteins
pubmed
9556620
uniprot
proteins
sequence_length
406
uniprot
proteins
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 spermatozoa. Localized in alpha granules in resting platelets and on the external plasma membrane and within the surface-connected cannalicular system in activated platelets.
uniprot
proteins