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P05154

- IPSP_HUMAN

UniProt

P05154 - IPSP_HUMAN

Protein

Plasma serine protease inhibitor

Gene

SERPINA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 3 (08 Feb 2011)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Keywords - Biological processi

    Fertilization, Lipid transport, Transport

    Keywords - Ligandi

    Heparin-binding

    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

    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

    ArrayExpressiP05154.
    BgeeiP05154.
    CleanExiHS_SERPINA5.
    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 – 5912
    Beta strandi65 – 673
    Helixi69 – 8113
    Helixi85 – 9410
    Helixi101 – 11717
    Beta strandi123 – 13513
    Helixi143 – 15311
    Beta strandi156 – 1594
    Helixi165 – 17915
    Turni180 – 1823
    Beta strandi195 – 21117
    Helixi215 – 2173
    Beta strandi219 – 22810
    Beta strandi230 – 24718
    Turni248 – 2514
    Beta strandi252 – 26211
    Beta strandi264 – 2707
    Helixi275 – 2817
    Helixi284 – 29310
    Beta strandi295 – 30410
    Beta strandi306 – 3138
    Helixi314 – 3163
    Helixi318 – 3214
    Helixi325 – 3273
    Turni334 – 3363
    Beta strandi337 – 3393
    Beta strandi343 – 35513
    Beta strandi357 – 37115
    Beta strandi372 – 3754
    Beta strandi380 – 3834
    Beta strandi388 – 40417

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MQLFLLLCLV LLSPQGASLH RHHPREMKKR VEDLHVGATV APSSRRDFTF    50
    DLYRALASAA PSQSIFFSPV SISMSLAMLS LGAGSSTKMQ ILEGLGLNLQ 100
    KSSEKELHRG FQQLLQELNQ PRDGFQLSLG NALFTDLVVD LQDTFVSAMK 150
    TLYLADTFPT NFRDSAGAMK QINDYVAKQT KGKIVDLLKN LDSNAVVIMV 200
    NYIFFKAKWE TSFNHKGTQE QDFYVTSETV VRVPMMSRED QYHYLLDRNL 250
    SCRVVGVPYQ GNATALFILP SEGKMQQVEN GLSEKTLRKW LKMFKKRQLE 300
    LYLPKFSIEG SYQLEKVLPS LGISNVFTSH ADLSGISNHS NIQVSEMVHK 350
    AVVEVDESGT RAAAATGTIF TFRSARLNSQ RLVFNRPFLM FIVDNNILFL 400
    GKVNRP 406
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMi HOG000238521.
    HOVERGENi HBG005957.
    InParanoidi P05154.
    KOi K03913.
    OMAi NFRDSAG.
    PhylomeDBi P05154.
    TreeFami TF343201.

    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

    ArrayExpressi P05154.
    Bgeei P05154.
    CleanExi HS_SERPINA5.
    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

    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: October 1, 2014
    This is version 169 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

    Dasty 3