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Protein

Urokinase-type plasminogen activator

Gene

PLAU

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei226 – 2261Charge relay systemBy similarity
Active sitei277 – 2771Charge relay systemBy similarity
Active sitei378 – 3781Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Chromosome 18

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 433417Urokinase-type plasminogen activatorPRO_0000285901Add
BLAST
Chaini21 – 179159Urokinase-type plasminogen activator long chain ABy similarityPRO_0000285902Add
BLAST
Chaini157 – 17923Urokinase-type plasminogen activator short chain ABy similarityPRO_0000285903Add
BLAST
Chaini181 – 433253Urokinase-type plasminogen activator chain BBy similarityPRO_0000285904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 41By similarity
Disulfide bondi35 ↔ 53By similarity
Disulfide bondi55 ↔ 64By similarity
Disulfide bondi72 ↔ 153By similarity
Disulfide bondi93 ↔ 135By similarity
Disulfide bondi124 ↔ 148By similarity
Disulfide bondi170 ↔ 301Interchain (between A and B chains)PROSITE-ProRule annotation
Disulfide bondi211 ↔ 227By similarity
Disulfide bondi219 ↔ 290By similarity
Disulfide bondi315 ↔ 384By similarity
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Modified residuei325 – 3251PhosphoserineBy similarity
Disulfide bondi347 ↔ 363By similarity
Disulfide bondi374 ↔ 402By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

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

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000023296.

Structurei

3D structure databases

ProteinModelPortaliQ8MHY7.
SMRiQ8MHY7. Positions 31-157, 168-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 6537EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini71 – 15383KringlePROSITE-ProRule annotationAdd
BLAST
Domaini181 – 426246Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 5924Binds urokinase plasminogen activator surface receptorBy similarityAdd
BLAST
Regioni154 – 18027Connecting peptideBy similarityAdd
BLAST

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

eggNOGiCOG5640.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000237314.
HOVERGENiHBG008633.
InParanoidiQ8MHY7.
KOiK01348.
OMAiKMLCAAD.
TreeFamiTF329901.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. EGF. 1 hit.
SM00130. 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.

Q8MHY7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLLVCLLL CALVVSDSEG SHELHGVSDA SNCGCLNGGT CVTYKYFSNI
60 70 80 90 100
WRCNCPKKFQ GEHCEIDTLK TCYHGDGHSY RGKANTDIMD RPCLAWNSAN
110 120 130 140 150
VLTKTYHAHR PDALQLGLGK HNYCRNPDHQ RRPWCYVQVG LKQLIQECKV
160 170 180 190 200
HDCSSGKKPA LPPGKLEFQC GQKALRPRFK IIGGEFTIIE NQPWFAAIYR
210 220 230 240 250
RHRGGSVTYV CGGSLISPCW VVSATHCFIN HQKKEDYIVY LGRSRLNSMT
260 270 280 290 300
PGEMKFEVEQ LILHEGYRAD TLAHHNDIAL LKILSNNGQC AQPSRSIQTI
310 320 330 340 350
CLPPWNADPN FGTSCEITGF GKENSTDYLY PEQLKMTVVK LVSYQECQQP
360 370 380 390 400
HYYGSEVTTK MLCAADPQWE TDSCQGDSGG PLVCSVQGRM TLTGIVSWGR
410 420 430
GCALKNKPGV YTRVSRFLPW IRSHIGEENG LAL
Length:433
Mass (Da):48,444
Last modified:October 1, 2002 - v1
Checksum:i6DD35A371010A6EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2681R → S in AAM83187 (PubMed:12149463).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY029517 mRNA. Translation: AAK40239.1.
AY122285 mRNA. Translation: AAM83187.1.
AB087224 mRNA. Translation: BAC02685.1.
AY453856 Genomic DNA. Translation: AAR21232.1.
RefSeqiNP_001075480.1. NM_001082011.1.
XP_008268125.1. XM_008269903.1.
UniGeneiOcu.2313.

Genome annotation databases

EnsembliENSOCUT00000029709; ENSOCUP00000023296; ENSOCUG00000003155.
GeneIDi100008633.
KEGGiocu:100008633.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY029517 mRNA. Translation: AAK40239.1.
AY122285 mRNA. Translation: AAM83187.1.
AB087224 mRNA. Translation: BAC02685.1.
AY453856 Genomic DNA. Translation: AAR21232.1.
RefSeqiNP_001075480.1. NM_001082011.1.
XP_008268125.1. XM_008269903.1.
UniGeneiOcu.2313.

3D structure databases

ProteinModelPortaliQ8MHY7.
SMRiQ8MHY7. Positions 31-157, 168-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000023296.

Protein family/group databases

MEROPSiS01.231.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000029709; ENSOCUP00000023296; ENSOCUG00000003155.
GeneIDi100008633.
KEGGiocu:100008633.

Organism-specific databases

CTDi5328.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000237314.
HOVERGENiHBG008633.
InParanoidiQ8MHY7.
KOiK01348.
OMAiKMLCAAD.
TreeFamiTF329901.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. EGF. 1 hit.
SM00130. 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...

Publicationsi

  1. "Downregulation of urokinase-type and tissue-type plasminogen activators in a rabbit model of renal ischemia/reperfusion."
    Sugiki M., Omura S., Yoshida E., Itoh H., Kataoka H., Maruyama M.
    J. Biochem. 132:501-508(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Increased expression of urokinase during atherosclerotic lesion development causes arterial constriction and lumen loss, and accelerates lesion growth."
    Falkenberg M., Tom C., DeYoung M.B., Wen S., Linnemann R., Dichek D.A.
    Proc. Natl. Acad. Sci. U.S.A. 99:10665-10670(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Oryctolagus cuniculus urokinase-type plasminogen activator, mRNA, complete cds."
    Yano W., Watanabe M.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Rabbit urokinase plasminogen activator (genomic DNA)."
    Graf S.K., Wen S., Dichek D.A.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiUROK_RABIT
AccessioniPrimary (citable) accession number: Q8MHY7
Secondary accession number(s): Q8MIL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 1, 2002
Last modified: June 24, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.