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

Oryctolagus cuniculus (Rabbit)

[TaxID: 9986]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.

Protein existence

2: Evidence at transcript level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=12204121 [NCBI, ExPASy, EBI, Israel, Japan] Sugiki M., Omura S., Yoshida E., Itoh H., Kataoka H., Maruyama M.; "Downregulation of urokinase-type and tissue-type plasminogen activators in a rabbit model of renal ischemia/reperfusion."; J. Biochem. 132:501-508(2002).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1073/pnas.162236599; PubMed=12149463 [NCBI, ExPASy, EBI, Israel, Japan] Falkenberg M., Tom C., DeYoung M.B., Wen S., Linnemann R., Dichek D.A.; "Increased expression of urokinase during atherosclerotic lesion development causes arterial constriction and lumen loss, and accelerates lesion growth."; Proc. Natl. Acad. Sci. U.S.A. 99:10665-10670(2002).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. Yano W., Watanabe M.; "Oryctolagus cuniculus urokinase-type plasminogen activator, mRNA, complete cds."; Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Graf S.K., Wen S., Dichek D.A.; "Rabbit urokinase plasminogen activator (genomic DNA)."; Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.

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).
PTM: Phosphorylation of Ser-325 abolishes proadhesive ability but does not interfere with receptor binding (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

AY029517; AAK40239.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY122285; AAM83187.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB087224; BAC02685.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY453856; AAR21232.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001075480.1; -.

UniGene

Ocu.2313

3D structure databases

HSSP

P00749; 1LMW. [HSSP ENTRY / PDB]

SMR

Q8MHY7; 31-154, 181-428.

ModBase

Q8MHY7.

Protein family/group databases

MEROPS

S01.231; -.

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.
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

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; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8MHY7.

Genome annotation databases

GeneID

100008633; -.

Phylogenomic databases

HOVERGEN

Q8MHY7; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`	`Potential.`
`CHAIN`	`17 433`	`417`	`Urokinase-type plasminogen activator.`	`PRO_0000285901`
`CHAIN`	`21 179`	`159`	`Urokinase-type plasminogen activator long chain A (By similarity).`	`PRO_0000285902`
`CHAIN`	`157 179`	`23`	`Urokinase-type plasminogen activator short chain A (By similarity).`	`PRO_0000285903`
`CHAIN`	`181 433`	`253`	`Urokinase-type plasminogen activator chain B (By similarity).`	`PRO_0000285904`
`DOMAIN`	`29 65`	`37`	`EGF-like.`
`DOMAIN`	`71 153`	`83`	`Kringle.`
`DOMAIN`	`181 426`	`246`	`Peptidase S1.`
`REGION`	`36 59`	`24`	`Binds urokinase plasminogen activator surface receptor (By similarity).`
`REGION`	`154 180`	`27`	`Connecting peptide (By similarity).`
`ACT_SITE`	`226 226`		`Charge relay system (By similarity).`
`ACT_SITE`	`277 277`		`Charge relay system (By similarity).`
`ACT_SITE`	`378 378`		`Charge relay system (By similarity).`
`MOD_RES`	`325 325`		`Phosphoserine (By similarity).`
`CARBOHYD`	`324 324`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`33 41`		`By similarity.`
`DISULFID`	`35 53`		`By similarity.`
`DISULFID`	`55 64`		`By similarity.`
`DISULFID`	`72 153`		`By similarity.`
`DISULFID`	`93 135`		`By similarity.`
`DISULFID`	`124 148`		`By similarity.`
`DISULFID`	`170 301`		`Interchain (between A and B chains) (By similarity).`
`DISULFID`	`211 227`		`By similarity.`
`DISULFID`	`219 290`		`By similarity.`
`DISULFID`	`315 384`		`By similarity.`
`DISULFID`	`347 363`		`By similarity.`
`DISULFID`	`374 402`		`By similarity.`
`CONFLICT`	`268 268`		`R -> S (in Ref. 2; AAM83187).`

Sequence information

Length: 433 AA [This is the length of the unprocessed precursor]

Molecular weight: 48444 Da [This is the MW of the unprocessed precursor]

CRC64: 6DD35A371010A6EE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRVLLVCLLL CALVVSDSEG SHELHGVSDA SNCGCLNGGT CVTYKYFSNI WRCNCPKKFQ 

        70         80         90        100        110        120 
GEHCEIDTLK TCYHGDGHSY RGKANTDIMD RPCLAWNSAN VLTKTYHAHR PDALQLGLGK 

       130        140        150        160        170        180 
HNYCRNPDHQ RRPWCYVQVG LKQLIQECKV HDCSSGKKPA LPPGKLEFQC GQKALRPRFK 

       190        200        210        220        230        240 
IIGGEFTIIE NQPWFAAIYR RHRGGSVTYV CGGSLISPCW VVSATHCFIN HQKKEDYIVY 

       250        260        270        280        290        300 
LGRSRLNSMT PGEMKFEVEQ LILHEGYRAD TLAHHNDIAL LKILSNNGQC AQPSRSIQTI 

       310        320        330        340        350        360 
CLPPWNADPN FGTSCEITGF GKENSTDYLY PEQLKMTVVK LVSYQECQQP HYYGSEVTTK 

       370        380        390        400        410        420 
MLCAADPQWE TDSCQGDSGG PLVCSVQGRM TLTGIVSWGR GCALKNKPGV YTRVSRFLPW 

       430 
IRSHIGEENG LAL

Q8MHY7 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