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P05154

- IPSP_HUMAN

UniProt

P05154 - IPSP_HUMAN

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Protein

Plasma serine protease inhibitor

Gene

SERPINA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.18 Publications

Enzyme regulationi

Its inhibitory activity is greatly enhanced in the presence of glycosaminoglycans, heparin, thrombomodulin and phospholipids vesicles.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei373 – 3742Reactive bond

GO - Molecular functioni

  1. acrosin binding Source: UniProtKB
  2. glycosaminoglycan binding Source: UniProtKB
  3. heparin binding Source: UniProtKB
  4. phosphatidylcholine binding Source: UniProtKB
  5. protease binding Source: UniProtKB
  6. retinoic acid binding Source: UniProtKB
  7. serine-type endopeptidase inhibitor activity Source: UniProtKB

GO - Biological processi

  1. fusion of sperm to egg plasma membrane Source: UniProtKB
  2. lipid transport Source: UniProtKB-KW
  3. negative regulation of endopeptidase activity Source: RefGenome
  4. negative regulation of proteolysis Source: Ensembl
  5. regulation of proteolysis Source: RefGenome
  6. spermatogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Fertilization, Lipid transport, Transport

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_1439. Common Pathway.
REACT_326. Intrinsic Pathway.

Protein family/group databases

MEROPSiI04.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Plasma serine protease inhibitor
Alternative name(s):
Acrosomal serine protease inhibitor
Plasminogen activator inhibitor 3
Short name:
PAI-3
Short name:
PAI3
Protein C inhibitor
Short name:
PCI
Serpin A5
Gene namesi
Name:SERPINA5
Synonyms:PCI, PLANH3, PROCI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:8723. SERPINA5.

Subcellular locationi

Secretedextracellular space 6 Publications
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.

GO - Cellular componenti

  1. acrosomal membrane Source: UniProtKB
  2. external side of plasma membrane Source: UniProtKB
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. membrane Source: UniProtKB
  7. platelet alpha granule Source: UniProtKB
  8. platelet dense tubular network Source: UniProtKB
  9. protein C inhibitor-coagulation factor V complex Source: UniProtKB
  10. protein C inhibitor-coagulation factor Xa complex Source: UniProtKB
  11. protein C inhibitor-coagulation factor XI complex Source: UniProtKB
  12. protein C inhibitor-KLK3 complex Source: UniProtKB
  13. protein C inhibitor-plasma kallikrein complex Source: UniProtKB
  14. protein C inhibitor-PLAT complex Source: UniProtKB
  15. protein C inhibitor-PLAU complex Source: UniProtKB
  16. protein C inhibitor-thrombin complex Source: UniProtKB
  17. protein C inhibitor-TMPRSS11E complex Source: UniProtKB
  18. protein C inhibitor-TMPRSS7 complex Source: UniProtKB
  19. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi248 – 2481R → 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. 1 Publication
Mutagenesisi253 – 2531R → E: Inhibits strongly thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 1 Publication
Mutagenesisi272 – 2721E → K: Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 1 Publication
Mutagenesisi274 – 2741K → E: Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 1 Publication
Mutagenesisi285 – 2851K → 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. 2 Publications
Mutagenesisi288 – 2881R → 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. 2 Publications
Mutagenesisi289 – 2891K → 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. 2 Publications
Mutagenesisi292 – 2921K → 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. 2 Publications
Mutagenesisi360 – 3601T → R: Inhibits heterodimer formation with TMPRSS11E. 1 Publication
Mutagenesisi371 – 3711T → R: Increases inhibition of activated protein C/F5 and factor XI/F11 activities. Decreases inhibition of thrombin activity. 1 Publication
Mutagenesisi372 – 3721F → P or G: Increases inhibition of thrombin activity. 1 Publication
Mutagenesisi373 – 3731R → P: Increases inhibition of thrombin activity. Inhibits heterodimer formation with TMPRSS11E. 2 Publications
Mutagenesisi376 – 3761R → P: Does not change inhibition of thrombin, activated protein C/F5 and factor XI/F11 activities. 1 Publication
Mutagenesisi381 – 3811R → E: Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Propeptidei20 – 256Removed in mature formPRO_0000414091
Chaini26 – 406381Plasma serine protease inhibitorPRO_0000032427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391O-linked (GalNAc...)2 Publications
Glycosylationi249 – 2491N-linked (GlcNAc...)2 Publications
Glycosylationi262 – 2621N-linked (GlcNAc...)3 Publications
Glycosylationi338 – 3381N-linked (GlcNAc...)2 Publications

Post-translational modificationi

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.6 Publications
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.2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP05154.
PaxDbiP05154.
PRIDEiP05154.

PTM databases

PhosphoSiteiP05154.

Miscellaneous databases

PMAP-CutDBP05154.

Expressioni

Tissue specificityi

Predominantly expressed in the epithelium of seminal vesicles. Expressed in the proximal tubular epithelium of the kidney. Expressed in the superficial and more differentiated epidermal keratinocytes of the skin. Expressed in megakaryocytes and platelets. Expressed poorly in kidney tumor cells compared to non tumor kidney tissues. Expressed in spermatozoa. Present in very high concentration in seminal plasma. Present in high concentration in plasma, synovial and Graaf follicle fluids. Present in low concentration in breast milk and in amniotic fluids. Present in very low concentration in urine, cerebrospinal fluids, saliva and tears (at protein level). Strongly expressed in liver. Expressed in kidney, spleen, pancreas, skeletal muscle, heart, testes, ovary, interstitial Leydig cells, epididymal glands, seminal vesicles and prostate.7 Publications

Gene expression databases

BgeeiP05154.
CleanExiHS_SERPINA5.
ExpressionAtlasiP05154. baseline and differential.
GenevestigatoriP05154.

Organism-specific databases

HPAiHPA056919.
HPA061957.

Interactioni

Subunit structurei

Forms protease inhibiting heterodimers in extracellular body fluids with serine proteases such as activated protein C/coagulation factor V/F5, acrosin/ACR, chymotrypsinogen B/CTRB1, prothrombin/F2, factor Xa/F10, factor XI/F11, kallikrein/KLKB1, tissue kallikrein, trypsin/PRSS1, prostate specific antigen/KLK3, tissue plasminogen activator/PLAT and urinary plasminogen activator/PLAU. Forms membrane-anchored serine proteases inhibiting heterodimers with TMPRSS7 and TMPRSS11E. Interacts with SEMG2.2 Publications

Protein-protein interaction databases

BioGridi111135. 12 interactions.
DIPiDIP-29869N.
IntActiP05154. 6 interactions.
MINTiMINT-1386269.
STRINGi9606.ENSP00000333203.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 5912Combined sources
Beta strandi65 – 673Combined sources
Helixi69 – 8113Combined sources
Helixi85 – 9410Combined sources
Helixi101 – 11717Combined sources
Beta strandi123 – 13513Combined sources
Helixi143 – 15311Combined sources
Beta strandi156 – 1594Combined sources
Helixi165 – 17915Combined sources
Turni180 – 1823Combined sources
Beta strandi195 – 21117Combined sources
Helixi215 – 2173Combined sources
Beta strandi219 – 22810Combined sources
Beta strandi230 – 24718Combined sources
Turni248 – 2514Combined sources
Beta strandi252 – 26211Combined sources
Beta strandi264 – 2707Combined sources
Helixi275 – 2817Combined sources
Helixi284 – 29310Combined sources
Beta strandi295 – 30410Combined sources
Beta strandi306 – 3138Combined sources
Helixi314 – 3163Combined sources
Helixi318 – 3214Combined sources
Helixi325 – 3273Combined sources
Turni334 – 3363Combined sources
Beta strandi337 – 3393Combined sources
Beta strandi343 – 35513Combined sources
Beta strandi357 – 37115Combined sources
Beta strandi372 – 3754Combined sources
Beta strandi380 – 3834Combined sources
Beta strandi388 – 40417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LQ8X-ray2.40A/C/E/G30-375[»]
B/D/F/H376-406[»]
1PAImodel-A20-373[»]
B374-406[»]
2HI9X-ray2.30A/B/C44-406[»]
2OL2X-ray2.00A/B36-406[»]
2PAImodel-A20-373[»]
B374-406[»]
3DY0X-ray1.55A37-372[»]
B379-406[»]
ProteinModelPortaliP05154.
SMRiP05154. Positions 47-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05154.

Family & Domainsi

Domaini

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.

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP05154.
KOiK03913.
OMAiNFRDSAG.
PhylomeDBiP05154.
TreeFamiTF343201.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05154-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLFLLLCLV LLSPQGASLH RHHPREMKKR VEDLHVGATV APSSRRDFTF
60 70 80 90 100
DLYRALASAA PSQSIFFSPV SISMSLAMLS LGAGSSTKMQ ILEGLGLNLQ
110 120 130 140 150
KSSEKELHRG FQQLLQELNQ PRDGFQLSLG NALFTDLVVD LQDTFVSAMK
160 170 180 190 200
TLYLADTFPT NFRDSAGAMK QINDYVAKQT KGKIVDLLKN LDSNAVVIMV
210 220 230 240 250
NYIFFKAKWE TSFNHKGTQE QDFYVTSETV VRVPMMSRED QYHYLLDRNL
260 270 280 290 300
SCRVVGVPYQ GNATALFILP SEGKMQQVEN GLSEKTLRKW LKMFKKRQLE
310 320 330 340 350
LYLPKFSIEG SYQLEKVLPS LGISNVFTSH ADLSGISNHS NIQVSEMVHK
360 370 380 390 400
AVVEVDESGT RAAAATGTIF TFRSARLNSQ RLVFNRPFLM FIVDNNILFL

GKVNRP
Length:406
Mass (Da):45,675
Last modified:February 8, 2011 - v3
Checksum:i2A8FF3DC33C77E04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281K → E in CAB45766. (PubMed:17974005)Curated
Sequence conflicti221 – 2211Q → L in AAB26244. (PubMed:8471250)Curated
Sequence conflicti335 – 3351G → R in AAA35688. (PubMed:3027058)Curated
Sequence conflicti335 – 3351G → R in AAB26244. (PubMed:8471250)Curated
Sequence conflicti384 – 3841F → S in AAB26244. (PubMed:8471250)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441S → G.1 Publication
Corresponds to variant rs2069975 [ dbSNP | Ensembl ].
VAR_013080
Natural varianti55 – 551A → V in allele PCI*B. 3 Publications
Corresponds to variant rs6118 [ dbSNP | Ensembl ].
VAR_007100
Natural varianti64 – 641S → N.9 Publications
Corresponds to variant rs6115 [ dbSNP | Ensembl ].
VAR_013081
Natural varianti94 – 941G → V.1 Publication
Corresponds to variant rs2069976 [ dbSNP | Ensembl ].
VAR_013082
Natural varianti105 – 1051K → E in allele PCI*B. 3 Publications
Corresponds to variant rs6119 [ dbSNP | Ensembl ].
VAR_007101
Natural varianti115 – 1151L → P.1 Publication
Corresponds to variant rs2069999 [ dbSNP | Ensembl ].
VAR_013083
Natural varianti121 – 1211P → A.1 Publication
Corresponds to variant rs6120 [ dbSNP | Ensembl ].
VAR_013900
Natural varianti217 – 2171G → R.2 Publications
Corresponds to variant rs6114 [ dbSNP | Ensembl ].
VAR_013084

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02639 mRNA. Translation: AAA35688.1.
M68516 Genomic DNA. Translation: AAA02811.1.
S69366
, S69364, S69574, S69365 Genomic DNA. Translation: AAB30461.1.
U35464 mRNA. Translation: AAB60386.1.
AF361796 Genomic DNA. Translation: AAK27240.1.
AL049839 Genomic DNA. No translation available.
BC008915 mRNA. Translation: AAH08915.1.
S58545 mRNA. Translation: AAB26244.2.
AL080185 mRNA. Translation: CAB45766.1.
CCDSiCCDS9928.1.
PIRiA39339.
RefSeqiNP_000615.3. NM_000624.5.
UniGeneiHs.159628.
Hs.741309.

Genome annotation databases

EnsembliENST00000329597; ENSP00000333203; ENSG00000188488.
ENST00000553780; ENSP00000450837; ENSG00000188488.
ENST00000554276; ENSP00000451610; ENSG00000188488.
ENST00000554866; ENSP00000451126; ENSG00000188488.
GeneIDi5104.
KEGGihsa:5104.
UCSCiuc001ydm.3. human.

Polymorphism databases

DMDMi322510122.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02639 mRNA. Translation: AAA35688.1 .
M68516 Genomic DNA. Translation: AAA02811.1 .
S69366
, S69364 , S69574 , S69365 Genomic DNA. Translation: AAB30461.1 .
U35464 mRNA. Translation: AAB60386.1 .
AF361796 Genomic DNA. Translation: AAK27240.1 .
AL049839 Genomic DNA. No translation available.
BC008915 mRNA. Translation: AAH08915.1 .
S58545 mRNA. Translation: AAB26244.2 .
AL080185 mRNA. Translation: CAB45766.1 .
CCDSi CCDS9928.1.
PIRi A39339.
RefSeqi NP_000615.3. NM_000624.5.
UniGenei Hs.159628.
Hs.741309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LQ8 X-ray 2.40 A/C/E/G 30-375 [» ]
B/D/F/H 376-406 [» ]
1PAI model - A 20-373 [» ]
B 374-406 [» ]
2HI9 X-ray 2.30 A/B/C 44-406 [» ]
2OL2 X-ray 2.00 A/B 36-406 [» ]
2PAI model - A 20-373 [» ]
B 374-406 [» ]
3DY0 X-ray 1.55 A 37-372 [» ]
B 379-406 [» ]
ProteinModelPortali P05154.
SMRi P05154. Positions 47-406.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111135. 12 interactions.
DIPi DIP-29869N.
IntActi P05154. 6 interactions.
MINTi MINT-1386269.
STRINGi 9606.ENSP00000333203.

Chemistry

DrugBanki DB00055. Drotrecogin alfa.
DB00013. Urokinase.

Protein family/group databases

MEROPSi I04.004.

PTM databases

PhosphoSitei P05154.

Polymorphism databases

DMDMi 322510122.

Proteomic databases

MaxQBi P05154.
PaxDbi P05154.
PRIDEi P05154.

Protocols and materials databases

DNASUi 5104.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000329597 ; ENSP00000333203 ; ENSG00000188488 .
ENST00000553780 ; ENSP00000450837 ; ENSG00000188488 .
ENST00000554276 ; ENSP00000451610 ; ENSG00000188488 .
ENST00000554866 ; ENSP00000451126 ; ENSG00000188488 .
GeneIDi 5104.
KEGGi hsa:5104.
UCSCi uc001ydm.3. human.

Organism-specific databases

CTDi 5104.
GeneCardsi GC14P095047.
H-InvDB HIX0079547.
HGNCi HGNC:8723. SERPINA5.
HPAi HPA056919.
HPA061957.
MIMi 601841. gene.
neXtProti NX_P05154.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4826.
GeneTreei ENSGT00760000118839.
HOGENOMi HOG000238521.
HOVERGENi HBG005957.
InParanoidi P05154.
KOi K03913.
OMAi NFRDSAG.
PhylomeDBi P05154.
TreeFami TF343201.

Enzyme and pathway databases

Reactomei REACT_1439. Common Pathway.
REACT_326. Intrinsic Pathway.

Miscellaneous databases

ChiTaRSi SERPINA5. human.
EvolutionaryTracei P05154.
GeneWikii Protein_C_inhibitor.
GenomeRNAii 5104.
NextBioi 19698.
PMAP-CutDB P05154.
PROi P05154.
SOURCEi Search...

Gene expression databases

Bgeei P05154.
CleanExi HS_SERPINA5.
ExpressionAtlasi P05154. baseline and differential.
Genevestigatori P05154.

Family and domain databases

InterProi IPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view ]
PANTHERi PTHR11461. PTHR11461. 1 hit.
Pfami PF00079. Serpin. 1 hit.
[Graphical view ]
SMARTi SM00093. SERPIN. 1 hit.
[Graphical view ]
SUPFAMi SSF56574. SSF56574. 1 hit.
PROSITEi PS00284. SERPIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a cDNA for human protein C inhibitor. A new member of the plasma serine protease inhibitor superfamily."
    Suzuki K., Deyashiki Y., Nishioka J., Kurachi K., Akira M., Yamamoto S., Hashimoto S.
    J. Biol. Chem. 262:611-616(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-64.
  2. "Evidence for a glycine residue at position 316 in human protein C inhibitor."
    Meijers J.C.M., Chung D.W.
    Thromb. Res. 59:389-393(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-64.
  3. "Organization of the gene coding for human protein C inhibitor (plasminogen activator inhibitor-3). Assignment of the gene to chromosome 14."
    Meijers J.C.M., Chung D.W.
    J. Biol. Chem. 266:15028-15034(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-64.
  4. "Gene organization of human protein C inhibitor, a member of SERPIN family proteins encoded in five exons."
    Hayashi T., Suzuki K.
    Int. J. Hematol. 58:213-224(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "A two-allele polymorphism in protein C inhibitor with varying frequencies in different ethnic populations."
    Radtke K.-P., Greengard J.S., Fernandez J.A., Villoutreix B.O., Griffin J.H.
    Thromb. Haemost. 75:62-69(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-55; ASN-64 AND GLU-105.
    Tissue: Liver.
  6. SeattleSNPs variation discovery resource
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-44; VAL-55; ASN-64; VAL-94; GLU-105; PRO-115 AND ARG-217.
  7. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-64.
    Tissue: Skin.
  9. "Human sperm-egg binding is inhibited by peptides corresponding to core region of an acrosomal serine protease inhibitor."
    Moore A., Penfold L.M., Johnson J.L., Latchman D.S., Moore H.D.
    Mol. Reprod. Dev. 34:280-291(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-406, VARIANT ASN-64.
    Tissue: Testis.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-406, VARIANT ASN-64.
    Tissue: Testis.
  11. "Protein C inhibitor from human plasma: characterization of native and cleaved inhibitor and demonstration of inhibitor complexes with plasma kallikrein."
    Laurell M., Stenflo J.
    Thromb. Haemost. 62:885-891(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-39.
  12. "Mechanism of inhibition of activated protein C by protein C inhibitor."
    Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.
    J. Biochem. 95:187-195(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BLOOD PLASMA SERINE PROTEASE INHIBITION, HETERODIMER WITH F2; F5 AND F10.
  13. "Inhibition of urokinase by protein C-inhibitor (PCI). Evidence for identity of PCI and plasminogen activator inhibitor 3."
    Stief T.W., Radtke K.P., Heimburger N.
    Biol. Chem. Hoppe-Seyler 368:1427-1433(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BLOOD PLASMA PLAU INHIBITION, HETERODIMER WITH PLAU.
  14. "Inactivation of human plasma kallikrein and factor XIa by protein C inhibitor."
    Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M., Bouma B.N.
    Biochemistry 27:4231-4237(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BLOOD PLASMA SERINE PROTEASE INHIBITION, HETERODIMER WITH F5; F11 AND KLKB1.
  15. "Functionally active protein C inhibitor/plasminogen activator inhibitor-3 (PCI/PAI-3) is secreted in seminal vesicles, occurs at high concentrations in human seminal plasma and complexes with prostate-specific antigen."
    Espana F., Gilabert J., Estelles A., Romeu A., Aznar J., Cabo A.
    Thromb. Res. 64:309-320(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SEMINAL PLASMA KLK3 INHIBITION, HETERODIMER WITH KLK3, SUBCELLULAR LOCATION.
  16. "Protein C inhibitor in human body fluids. Seminal plasma is rich in inhibitor antigen deriving from cells throughout the male reproductive system."
    Laurell M., Christensson A., Abrahamsson P.A., Stenflo J., Lilja H.
    J. Clin. Invest. 89:1094-1101(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  17. "Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa."
    Zheng X., Geiger M., Ecke S., Bielek E., Donner P., Eberspacher U., Schleuning W.D., Binder B.R.
    Am. J. Physiol. 267:C466-C472(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SEMINAL PLASMA ACR INHIBITION, HETERODIMER WITH ACR, SUBCELLULAR LOCATION.
  18. "Intermolecular interactions between protein C inhibitor and coagulation proteases."
    Cooper S.T., Whinna H.C., Jackson T.P., Boyd J.M., Church F.C.
    Biochemistry 34:12991-12997(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SERINE PROTEASE INHIBITION, MUTAGENESIS OF THR-371; PHE-372; ARG-373 AND ARG-376.
  19. "Complexes of tissue kallikrein with protein C inhibitor in human semen and urine."
    Espana F., Fink E., Sanchez-Cuenca J., Gilabert J., Estelles A., Witzgall K.
    Eur. J. Biochem. 234:641-649(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SEMINAL PLASMA AND URINE KALLIKREIN INHIBITION, HETERODIMER WITH TISSUE KALLIKREIN, SUBCELLULAR LOCATION.
  20. "Characterization of semenogelin II and its molecular interaction with prostate-specific antigen and protein C inhibitor."
    Kise H., Nishioka J., Kawamura J., Suzuki K.
    Eur. J. Biochem. 238:88-96(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SEMINAL PLASMA KLK3 INHIBITION, HETERODIMER WITH F5, INTERACTION WITH SEMG2.
  21. "Protein C inhibitor acts as a procoagulant by inhibiting the thrombomodulin-induced activation of protein C in human plasma."
    Elisen M.G., von dem Borne P.A., Bouma B.N., Meijers J.C.
    Blood 91:1542-1547(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BLOOD PLASMA F5 INHIBITION.
  22. Cited for: FUNCTION IN FERTILIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  23. "Protein C inhibitor secreted from activated platelets efficiently inhibits activated protein C on phosphatidylethanolamine of platelet membrane and microvesicles."
    Nishioka J., Ning M., Hayashi T., Suzuki K.
    J. Biol. Chem. 273:11281-11287(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BLOOD PLASMA F5 INHIBITION, HETERODIMER WITH F5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  24. "Functionally inactive protein C inhibitor in seminal plasma may be associated with infertility."
    He S., Lin Y.L., Liu Y.X.
    Mol. Hum. Reprod. 5:513-519(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SEMINAL PLASMA SERINE PROTEASES INHIBITION, HETERODIMER WITH PLAT AND PLAU.
  25. "Binding of retinoic acid by the inhibitory serpin protein C inhibitor."
    Jerabek I., Zechmeister-Machhart M., Binder B.R., Geiger M.
    Eur. J. Biochem. 268:5989-5996(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RETINOIC ACID TRANSPORT.
  26. "Regulation of carcinoma cell invasion by protein C inhibitor whose expression is decreased in renal cell carcinoma."
    Wakita T., Hayashi T., Nishioka J., Tamaru H., Akita N., Asanuma K., Kamada H., Gabazza E.C., Ido M., Kawamura J., Suzuki K.
    Int. J. Cancer 108:516-523(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS REGULATOR OF TUMOR CELL INVASION, HETERODIMER WITH PLAU, TISSUE SPECIFICITY.
  27. "Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes."
    Hobson J.P., Netzel-Arnett S., Szabo R., Rehault S.M., Church F.C., Strickland D.K., Lawrence D.A., Antalis T.M., Bugge T.H.
    J. Biol. Chem. 279:46981-46994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS11E INHIBITION, HETERODIMER WITH TMPRSS11E, PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF THR-360 AND ARG-373.
  28. "Characterization of a novel human protein C inhibitor (PCI) gene transgenic mouse useful for studying the role of PCI in physiological and pathological conditions."
    Hayashi T., Nishioka J., Kamada H., Asanuma K., Kondo H., Gabazza E.C., Ido M., Suzuki K.
    J. Thromb. Haemost. 2:949-961(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BLOOD PLASMA F5 INHIBITION, HETERODIMER WITH F5, TISSUE SPECIFICITY.
  29. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
    Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
    Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249.
    Tissue: Plasma.
  30. "Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity."
    Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.
    Biochem. J. 390:231-242(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, HETERODIMER WITH TMPRSS7.
  31. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-262 AND ASN-338.
    Tissue: Plasma.
  32. "Immunolocalization of protein C inhibitor in differentiation of human epidermal keratinocytes."
    Zhang C., Li X., Lian X., Wang Y., Zeng Y., Yang K., Yu J., Gao Q., Yang T.
    Acta Histochem. 109:461-467(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  33. "N-glycans and the N terminus of protein C inhibitor affect the cofactor-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) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, GLYCOSYLATION AT ASN-249; ASN-262 AND ASN-338, STRUCTURE OF CARBOHYDRATES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  34. "Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex."
    Li W., Adams T.E., Nangalia J., Esmon C.T., Huntington J.A.
    Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-253; GLU-272; LYS-274; LYS-285; ARG-288; LYS-289; LYS-292 AND ARG-381.
  35. "Further insight into the roles of the glycans attached to human blood protein C inhibitor."
    Sun W., Parry S., Ubhayasekera W., Engstrom A., Dell A., Schedin-Weiss S.
    Biochem. Biophys. Res. Commun. 403:198-202(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-39, IDENTIFICATION BY MASS SPECTROMETRY.
  36. "Human urinary glycoproteomics; attachment site specific analysis of N-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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-39, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  37. "Elucidating the structural chemistry of glycosaminoglycan recognition by protein C inhibitor."
    Kuhn L.A., Griffin J.H., Fisher C.L., Greengard J.S., Bouma B.N., Espana F., Tainer J.A.
    Proc. Natl. Acad. Sci. U.S.A. 87:8506-8510(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  38. "Crystal structure of protein C inhibitor provides insights into hormone binding and heparin activation."
    Huntington J.A., Kjellberg M., Stenflo J.
    Structure 11:205-215(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 30-406, GLYCOSYLATION AT ASN-262.
  39. "Structure of native protein C inhibitor provides insight into its multiple functions."
    Li W., Adams T.E., Kjellberg M., Stenflo J., Huntington J.A.
    J. Biol. Chem. 282:13759-13768(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 36-406.
  40. "The heparin binding site of protein C inhibitor is protease-dependent."
    Li W., Huntington J.A.
    J. Biol. Chem. 283:36039-36045(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 37-406 IN COMPLEX WITH SYNTHETIC HEPARIN, HEPARIN-BINDING SITES, MUTAGENESIS OF ARG-248; LYS-285; ARG-288; LYS-289 AND LYS-292.
  41. Cited for: VARIANTS VAL-55; ASN-64; GLU-105; ALA-121 AND ARG-217.

Entry informationi

Entry nameiIPSP_HUMAN
AccessioniPrimary (citable) accession number: P05154
Secondary accession number(s): Q07616, Q9UG30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 8, 2011
Last modified: November 26, 2014
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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