Urokinase-type plasminogen activator long chain A
Urokinase-type plasminogen activator short chain A
Urokinase-type plasminogen activator chain B

Gene name

Name:

Plau

From

Rattus norvegicus (Rat)

[TaxID: 10116]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Fischer 344; PubMed=1568219 [NCBI, ExPASy, EBI, Israel, Japan] Henderson B.R., Tansey W.P., Phillips S.M., Ramshaw I.A., Kefford R.F.; "Transcriptional and posttranscriptional activation of urokinase plasminogen activator gene expression in metastatic tumor cells."; Cancer Res. 52:2489-2496(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Kidney; Rabbani S.A.; Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-62, AND IDENTIFICATION OF UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR BINDING DOMAIN. DOI=10.1016/0014-5793(92)80998-V; PubMed=1321734 [NCBI, ExPASy, EBI, Israel, Japan] Ragno P., Cassano S., Degen J., Kessler C., Blasi F., Rossi G.; "The receptor for the plasminogen activator of urokinase type is up-regulated in transformed rat thyroid cells."; FEBS Lett. 306:193-198(1992).

Comments

FUNCTION: Specifically cleave the zymogen plasminogen to form the active enzyme plasmin.
CATALYTIC ACTIVITY: Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.
SUBUNIT: 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. Binds LRP1B; binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity).
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 1 EGF-like domain.
SIMILARITY: Contains 1 kringle domain.
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X63434; CAA45028.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X65651; CAA46601.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X66907; CAA47356.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S24604; S18932.

UniGene

Rn.6064

3D structure databases

HSSP

P00749; 1KDU. [HSSP ENTRY / PDB]

SMR

P29598; 29-152, 179-427.

ModBase

P29598.

Protein family/group databases

MEROPS

S01.231; -.

Organism-specific databases

RGD

3343; Plau.

Gene expression databases

ArrayExpress

P29598; -.

GermOnline

ENSRNOG00000010516; Rattus norvegicus.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006210; EGF.
IPR000742; EGF_3.
IPR013111; EGF_extracell.
IPR013032; EGF_like_reg_CS.
IPR000001; Kringle.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.20.10; Kringle; 1.

Pfam

PF07974; EGF_2; 1.
PF00051; Kringle; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.
PR00018; KRINGLE.

ProDom

PD000395; Kringle; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00181; EGF; 1.
SM00130; KR; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00022; EGF_1; 1.
PS01186; EGF_2; FALSE_NEG.
PS50026; EGF_3; 1.
PS00021; KRINGLE_1; 1.
PS50070; KRINGLE_2; 1.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; FALSE_NEG.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000010516; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P29598; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

EGF-like domain; Hydrolase; Kringle; Plasminogen activation; Protease; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`	`Potential.`
`CHAIN`	`20 432`	`413`	`Urokinase-type plasminogen activator.`	`PRO_0000028333`
`CHAIN`	`20 177`	`158`	`Urokinase-type plasminogen activator long chain A (By similarity).`	`PRO_0000028334`
`CHAIN`	`156 177`	`22`	`Urokinase-type plasminogen activator short chain A (By similarity).`	`PRO_0000028335`
`CHAIN`	`179 432`	`254`	`Urokinase-type plasminogen activator chain B (By similarity).`	`PRO_0000028336`
`DOMAIN`	`27 63`	`37`	`EGF-like.`
`DOMAIN`	`70 151`	`82`	`Kringle.`
`DOMAIN`	`179 425`	`247`	`Peptidase S1.`
`REGION`	`34 57`	`24`	`Binds urokinase plasminogen activator surface receptor.`
`REGION`	`152 178`	`27`	`Connecting peptide.`
`ACT_SITE`	`225 225`		`Charge relay system.`
`ACT_SITE`	`276 276`		`Charge relay system.`
`ACT_SITE`	`377 377`		`Charge relay system.`
`DISULFID`	`31 39`		`By similarity.`
`DISULFID`	`33 51`		`By similarity.`
`DISULFID`	`53 62`		`By similarity.`
`DISULFID`	`70 151`		`By similarity.`
`DISULFID`	`91 133`		`By similarity.`
`DISULFID`	`122 146`		`By similarity.`
`DISULFID`	`168 300`		`Interchain (between A and B chains) (By similarity).`
`DISULFID`	`210 226`		`By similarity.`
`DISULFID`	`218 289`		`By similarity.`
`DISULFID`	`314 383`		`By similarity.`
`DISULFID`	`346 362`		`By similarity.`
`DISULFID`	`373 401`		`By similarity.`
`CONFLICT`	`16 16`		`N -> H (in Ref. 2; CAA46601).`
`CONFLICT`	`24 24`		`E -> G (in Ref. 2; CAA46601).`
`CONFLICT`	`332 332`		`D -> N (in Ref. 2; CAA46601).`

Sequence information

Length: 432 AA [This is the length of the unprocessed precursor]

Molecular weight: 47957 Da [This is the MW of the unprocessed precursor]

CRC64: 4EB1B96C716244C8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRVWLASLFL CALVANSEGG SELEASDESN CGCQNGGVCV SYKYFSSIRR CSCPKKFKGE 

        70         80         90        100        110        120 
HCEIDTSKTC YHGNGQSYRG KANTDTKGRP CLAWNSPAVL QQTYNAHRSD ALSLGLGKHN 

       130        140        150        160        170        180 
YCRNPDNQRR PWCYVQIGLK QFVQECMVQD CSLSKKPSST VDQQGFQCGQ KALRPRFKIV 

       190        200        210        220        230        240 
GGEFTVVENQ PWFAAIYLKN KGGSPPSFKC GGSLISPCWV ASATHCFVNQ PKKEEYVVYL 

       250        260        270        280        290        300 
GQSKRNSYNP GEMKFEVEQL ILHEDFSDET LAFHNDIALL KIRTSTGQCA QPSRTIQTIC 

       310        320        330        340        350        360 
LPPRFGDAPF GSDCEITGFG QESATDYFYP KDLKMSVVKI ISHEQCKQPH YYGSEINYKM 

       370        380        390        400        410        420 
LCAADPEWKT DSCSGDSGGP LICNIDGRPT LSGIVSWGSG CAEKNKPGVY TRVSYFLNWI 

       430 
QSHIGEENGL AF

P29598 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools