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Protein

Plasminogen activator inhibitor 1

Gene

Serpine1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Serine protease inhibitor. Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair. It is involved in cellular and replicative senescence (By similarity). Plays a role in alveolar type 2 cells senescence in the lung (By similarity). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei369 – 370Reactive bond2

GO - Molecular functioni

  • protease binding Source: RGD
  • serine-type endopeptidase inhibitor activity Source: RGD

GO - Biological processi

  • cellular response to aldosterone Source: RGD
  • cellular response to angiotensin Source: RGD
  • cellular response to ATP Source: RGD
  • cellular response to cAMP Source: RGD
  • cellular response to cGMP Source: RGD
  • cellular response to cycloheximide Source: RGD
  • cellular response to dexamethasone stimulus Source: RGD
  • cellular response to drug Source: RGD
  • cellular response to fibroblast growth factor stimulus Source: RGD
  • cellular response to follicle-stimulating hormone stimulus Source: RGD
  • cellular response to glucagon stimulus Source: RGD
  • cellular response to glucose stimulus Source: RGD
  • cellular response to gravity Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to hydrogen peroxide Source: RGD
  • cellular response to hypoxia Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to leukemia inhibitory factor Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to low-density lipoprotein particle stimulus Source: RGD
  • cellular response to mechanical stimulus Source: RGD
  • cellular response to metal ion Source: RGD
  • cellular response to nerve growth factor stimulus Source: RGD
  • cellular response to nicotine Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • cellular response to platelet-derived growth factor stimulus Source: RGD
  • cellular response to potassium ion Source: RGD
  • cellular response to resveratrol Source: RGD
  • cellular response to transforming growth factor beta stimulus Source: RGD
  • decidualization Source: RGD
  • female gonad development Source: RGD
  • glucose homeostasis Source: RGD
  • mast cell activation Source: RGD
  • negative regulation of cell migration Source: RGD
  • negative regulation of endopeptidase activity Source: RGD
  • negative regulation of gene expression Source: RGD
  • negative regulation of proteolysis Source: RGD
  • positive regulation of calcium ion import Source: RGD
  • positive regulation of coagulation Source: RGD
  • positive regulation of collagen biosynthetic process Source: RGD
  • positive regulation of fibroblast proliferation Source: RGD
  • positive regulation of gene expression Source: RGD
  • positive regulation of keratinocyte migration Source: RGD
  • positive regulation of receptor-mediated endocytosis Source: BHF-UCL
  • replicative senescence Source: UniProtKB
  • response to cytokine Source: RGD
  • response to epidermal growth factor Source: RGD
  • response to estrogen Source: RGD
  • response to hyperoxia Source: RGD
  • response to laminar fluid shear stress Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to nutrient levels Source: RGD
  • response to reactive oxygen species Source: RGD
  • response to starvation Source: RGD
  • response to transforming growth factor beta Source: RGD
  • tissue regeneration Source: RGD
  • wound healing Source: RGD

Keywordsi

Molecular functionProtease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI04.020

Names & Taxonomyi

Protein namesi
Recommended name:
Plasminogen activator inhibitor 1
Short name:
PAI
Short name:
PAI-1
Alternative name(s):
Endothelial plasminogen activator inhibitor
Serpin E1
Gene namesi
Name:Serpine1
Synonyms:Pai1, Planh1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3249 Serpine1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2155

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23By similarityAdd BLAST23
ChainiPRO_000003250324 – 402Plasminogen activator inhibitor 1Add BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi88N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi232N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi288N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi352N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP20961
PRIDEiP20961

PTM databases

PhosphoSitePlusiP20961

Interactioni

Subunit structurei

Forms a heterodimer with TMPRSS7. Interacts with VTN. Binds LRP1B; binding is followed by internalization and degradation. Interacts with PPP1CB.By similarity

GO - Molecular functioni

  • protease binding Source: RGD

Protein-protein interaction databases

BioGridi246756, 2 interactors
STRINGi10116.ENSRNOP00000001916

Chemistry databases

BindingDBiP20961

Structurei

3D structure databases

ProteinModelPortaliP20961
SMRiP20961
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2392 Eukaryota
COG4826 LUCA
HOGENOMiHOG000238519
HOVERGENiHBG106493
InParanoidiP20961
KOiK03982
PhylomeDBiP20961

Family and domain databases

InterProiView protein in InterPro
IPR023795 Serpin_CS
IPR023796 Serpin_dom
IPR000215 Serpin_fam
IPR036186 Serpin_sf
PANTHERiPTHR11461 PTHR11461, 1 hit
PfamiView protein in Pfam
PF00079 Serpin, 1 hit
SMARTiView protein in SMART
SM00093 SERPIN, 1 hit
SUPFAMiSSF56574 SSF56574, 1 hit
PROSITEiView protein in PROSITE
PS00284 SERPIN, 1 hit

Sequencei

Sequence statusi: Complete.

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

P20961-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQMSSALTCL TLGLVLVFGK GFASPLPESH TAQQATNFGV KVFQHVVQAS
60 70 80 90 100
KDRNVVFSPY GVSSVLAMLQ LTTAGKTRQQ IQDAMGFNIS ERGTAPALRK
110 120 130 140 150
LSKELMGSWN KNEISTADAI FVQRDLELVQ GFMPHFFKLF RTTVKQVDFS
160 170 180 190 200
EVERARFIIN DWVERHTKGM ISDLLAKGAV NELTRLVLVN ALYFNGQWKT
210 220 230 240 250
PFLEASTHQR LFHKSDGSTI SVPMMAQNNK FNYTEFTTPD GHEYDILELP
260 270 280 290 300
YHGETLSMFI AAPFEKDVPL SAITNILDAE LIRQWKSNMT RLPRLLILPK
310 320 330 340 350
FSLETEVDLR GPLEKLGMTD IFSSTQADFT SLSDQEQLSV AQALQKVKIE
360 370 380 390 400
VNESGTVASS STAILVSARM APTEMVLDRS FLFVVRHNPT ETILFMGQLM

EP
Length:402
Mass (Da):45,010
Last modified:February 1, 1991 - v1
Checksum:i2B639140F475EB53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05206 Genomic DNA Translation: AAA41796.1
M24067 mRNA Translation: AAA56856.1
PIRiA35032
RefSeqiNP_036752.1, NM_012620.1
UniGeneiRn.29367

Genome annotation databases

GeneIDi24617
KEGGirno:24617
UCSCiRGD:3249 rat

Similar proteinsi

Entry informationi

Entry nameiPAI1_RAT
AccessioniPrimary (citable) accession number: P20961
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 23, 2018
This is version 130 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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