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Protein

Urokinase-type plasminogen activator

Gene

PLAU

Organism
Sus scrofa (Pig)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei235 – 2351Charge relay system
Active sitei286 – 2861Charge relay system
Active sitei387 – 3871Charge relay system

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Chaini21 – 442422Urokinase-type plasminogen activatorPRO_0000028330Add
BLAST
Chaini21 – 188168Urokinase-type plasminogen activator long chain ABy similarityPRO_0000028331Add
BLAST
Chaini167 – 18822Urokinase-type plasminogen activator short chain ABy similarityPRO_0000285900Add
BLAST
Chaini190 – 442253Urokinase-type plasminogen activator chain BBy similarityPRO_0000028332Add
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
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi179 ↔ 310Interchain (between A and B chains)PROSITE-ProRule annotation
Disulfide bondi220 ↔ 236By similarity
Disulfide bondi228 ↔ 299By similarity
Disulfide bondi324 ↔ 393By similarity
Disulfide bondi356 ↔ 372By similarity
Disulfide bondi383 ↔ 411By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, 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

STRINGi9823.ENSSSCP00000010995.

Structurei

3D structure databases

ProteinModelPortaliP04185.
SMRiP04185. Positions 31-157, 177-437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 6537EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini72 – 15382KringlePROSITE-ProRule annotationAdd
BLAST
Domaini190 – 435246Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 5924Binds urokinase plasminogen activator surface receptorBy similarityAdd
BLAST
Regioni154 – 18936Connecting peptideAdd
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.
HOGENOMiHOG000237314.
HOVERGENiHBG008633.
InParanoidiP04185.
KOiK01348.

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.
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.

P04185-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLRACLSL CVLVVSDSKG SHELHQESGA SNCGCLNGGK CVSYKYFSNI
60 70 80 90 100
QRCSCPKKFQ GEHCEIDTSQ TCFEGNGHSY RGKANTNTGG RPCLPWNSAT
110 120 130 140 150
VLLNTYHAHR PDALQLGLGK HNYCRNPDNQ RRPWCYVQVG LKQLVQECMV
160 170 180 190 200
PNCSGGESHR PAYDGKNPFS TPEKVEFQCG QKALRPRFKI VGGKSTTIEN
210 220 230 240 250
QPWFAAIYRR HRGGSVTYVC GGSLISPCWV VSATHCFINY QQKEDYIVYL
260 270 280 290 300
GRQTLHSSTH GEMKFEVEKL ILHEDYSADS LAHHNDIALL KIRTDKGQCA
310 320 330 340 350
QPSRSIQTIC LPPVNGDAHF GASCEIVGFG KEDPSDYLYP EQLKMTVVKL
360 370 380 390 400
VSHRECQQPH YYGSEVTTKM LCAADPQWKT DSCQGDSGGP LVCSTQGRLT
410 420 430 440
LTGIVSWGRE CAMKDKPGVY TRVSRFLTWI HTHVGGENGL AH
Length:442
Mass (Da):49,117
Last modified:August 13, 1987 - v1
Checksum:iEE32FCEF501321EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti241 – 2411Q → H in CAA25806 (PubMed:6096832).Curated
Sequence conflicti242 – 2421Q → H in CAA26511 (PubMed:6096832).Curated
Sequence conflicti288 – 2881A → GS in CAA25806 (PubMed:6096832).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01648 Genomic DNA. Translation: CAA25806.1.
X02724 mRNA. Translation: CAA26511.1.
PIRiA00932. UKPG.
RefSeqiNP_999110.1. NM_213945.1.
UniGeneiSsc.11194.

Genome annotation databases

GeneIDi396985.
KEGGissc:396985.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01648 Genomic DNA. Translation: CAA25806.1.
X02724 mRNA. Translation: CAA26511.1.
PIRiA00932. UKPG.
RefSeqiNP_999110.1. NM_213945.1.
UniGeneiSsc.11194.

3D structure databases

ProteinModelPortaliP04185.
SMRiP04185. Positions 31-157, 177-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000010995.

Chemistry

ChEMBLiCHEMBL1075030.

Protein family/group databases

MEROPSiS01.231.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396985.
KEGGissc:396985.

Organism-specific databases

CTDi5328.

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000237314.
HOVERGENiHBG008633.
InParanoidiP04185.
KOiK01348.

Miscellaneous databases

PROiP04185.

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.
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...

Publicationsi

  1. "cDNA and gene nucleotide sequence of porcine plasminogen activator."
    Nagamine Y., Pearson D., Altus M.S., Reich E.
    Nucleic Acids Res. 12:9525-9541(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Kidney.
  2. Nagamine Y.
    Submitted (DEC-1986) to the PIR data bank
    Cited for: SEQUENCE REVISION TO 241.

Entry informationi

Entry nameiUROK_PIG
AccessioniPrimary (citable) accession number: P04185
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: August 13, 1987
Last modified: April 29, 2015
This is version 121 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.