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Protein

Urokinase-type plasminogen activator

Gene

PLAU

Organism
Papio cynocephalus (Yellow baboon)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.

Catalytic activityi

Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.

Enzyme regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei223Charge relay system1
Active sitei274Charge relay system1
Active sitei378Charge relay system1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Plasminogen activation

Protein family/group databases

MEROPSiS01.231.

Names & Taxonomyi

Protein namesi
Recommended name:
Urokinase-type plasminogen activator (EC:3.4.21.73)
Short name:
U-plasminogen activator
Short name:
uPA
Cleaved into the following 3 chains:
Gene namesi
Name:PLAU
OrganismiPapio cynocephalus (Yellow baboon)
Taxonomic identifieri9556 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaePapio

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000002832621 – 433Urokinase-type plasminogen activatorAdd BLAST413
ChainiPRO_000002832721 – 176Urokinase-type plasminogen activator long chain ABy similarityAdd BLAST156
ChainiPRO_0000028328155 – 176Urokinase-type plasminogen activator short chain ABy similarityAdd BLAST22
ChainiPRO_0000028329178 – 433Urokinase-type plasminogen activator chain BBy similarityAdd BLAST256

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 38By similarity
Disulfide bondi32 ↔ 50By similarity
Disulfide bondi52 ↔ 61By similarity
Disulfide bondi69 ↔ 150By similarity
Disulfide bondi90 ↔ 132By similarity
Disulfide bondi121 ↔ 145By similarity
Modified residuei157PhosphoserineBy similarity1
Disulfide bondi167 ↔ 298Interchain (between A and B chains)PROSITE-ProRule annotation
Disulfide bondi208 ↔ 224By similarity
Disulfide bondi216 ↔ 287By similarity
Disulfide bondi315 ↔ 384By similarity
Glycosylationi324N-linked (GlcNAc...)Sequence analysis1
Modified residuei325PhosphoserineBy similarity1
Disulfide bondi347 ↔ 363By similarity
Disulfide bondi374 ↔ 402By similarity

Post-translational modificationi

Phosphorylation of Ser-157 and Ser-325 abolishes proadhesive ability but does not interfere with receptor binding.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PRIDEiP16227.

Interactioni

Subunit structurei

Found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A which is cleaved to yield a short chain A. Forms heterodimer with SERPINA5. Binds LRP1B; binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP16227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 62EGF-likePROSITE-ProRule annotationAdd BLAST37
Domaini69 – 150KringlePROSITE-ProRule annotationAdd BLAST82
Domaini178 – 426Peptidase S1PROSITE-ProRule annotationAdd BLAST249

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 56Binds urokinase plasminogen activator surface receptorBy similarityAdd BLAST24
Regioni151 – 177Connecting peptideAdd BLAST27

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 kringle domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Kringle, Signal

Phylogenomic databases

HOVERGENiHBG008633.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.
PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16227-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALLAHLLL CVLVVSASKG SRELQVPSDC GCLNGGTCMS NKYFSSIHWC
60 70 80 90 100
NCPKKFGGQH CEIDKSKTCY EGNGHFYRGK ASTDTMGRSC LAWNSATVLQ
110 120 130 140 150
QTYHAHRSDA LQLGLGKHNY CRNPDNRRRP WCYVQVGLKQ RVQECMVHNC
160 170 180 190 200
ADGKKPSSPP EELQFQCGQR TLRPRFKIVG GEFTTIENQP WFAAIYRRHR
210 220 230 240 250
GGSVTYVCGG SLISPCWVVS ATHCFINYPK KEDYIVYLGR SRLNSNTQGE
260 270 280 290 300
MKFEVENLIL HEDYSADTLA HHNDIALLKI RSKEGRCAQP SRTIQTICLP
310 320 330 340 350
SMYNDPNDPP FGTSCEITGF GKENSTDYLY PEQLKMTVVK LVSHQKCQQP
360 370 380 390 400
HYYGSEVTTK MLCAADPQWE TDSCQGDSGG PLVCSIQGHM TLTGIVSWGR
410 420 430
GCALKDKPGV YTRVSRFLPW IHSHTREQNG LAL
Length:433
Mass (Da):48,595
Last modified:April 1, 1990 - v1
Checksum:i816D22DFEDDC8792
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51935 mRNA. Translation: CAA36200.1.
PIRiS14687. UKBAY.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51935 mRNA. Translation: CAA36200.1.
PIRiS14687. UKBAY.

3D structure databases

ProteinModelPortaliP16227.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.231.

Proteomic databases

PRIDEiP16227.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008633.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.
PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUROK_PAPCY
AccessioniPrimary (citable) accession number: P16227
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 5, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.