Reviewed, UniProtKB/Swiss-Prot Q8MHY7 (UROK_RABIT)

Names and origin

Protein names

Recommended name:
    Urokinase-type plasminogen activator
      Short name=uPA
      Short name=U-plasminogen activator
    EC=3.4.21.73
Cleaved into the following 3 chains:
    1- Recommended name:
            Urokinase-type plasminogen activator long chain A
    2- Recommended name:
            Urokinase-type plasminogen activator short chain A
    3- Recommended name:
            Urokinase-type plasminogen activator chain B

Gene names

Name:

PLAU

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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 structure	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.
Post-translational modification	Phosphorylation of Ser-325 abolishes proadhesive ability but does not interfere with receptor binding By similarity.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 EGF-like domain. Contains 1 kringle domain. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Plasminogen activation
Cellular component	Secreted
Domain	EGF-like domain Kringle Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Phosphoprotein Zymogen
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	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
Regions
	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
Sites
	Active site	226	1	Charge relay system By similarity
	Active site	277	1	Charge relay system By similarity
	Active site	378	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	325	1	Phosphoserine By similarity
	Glycosylation	324	1	N-linked (GlcNAc...) Potential
	Disulfide bond	33 ↔ 41		By similarity
	Disulfide bond	35 ↔ 53		By similarity
	Disulfide bond	55 ↔ 64		By similarity
	Disulfide bond	72 ↔ 153		By similarity
	Disulfide bond	93 ↔ 135		By similarity
	Disulfide bond	124 ↔ 148		By similarity
	Disulfide bond	170 ↔ 301		Interchain (between A and B chains) By similarity
	Disulfide bond	211 ↔ 227		By similarity
	Disulfide bond	219 ↔ 290		By similarity
	Disulfide bond	315 ↔ 384		By similarity
	Disulfide bond	347 ↔ 363		By similarity
	Disulfide bond	374 ↔ 402		By similarity
Experimental info
	Sequence conflict	268	1	R → S in AAM83187. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8MHY7-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 6DD35A371010A6EE	FASTA	433	48,444
	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

References

[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: 12204121] [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: 12149463] [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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY029517 mRNA. Translation: AAK40239.1. AY122285 mRNA. Translation: AAM83187.1. AB087224 mRNA. Translation: BAC02685.1. AY453856 Genomic DNA. Translation: AAR21232.1.
RefSeq	NP_001075480.1.
UniGene	Ocu.2313
3D structure databases
HSSP	HSSP built from PDB template 1LMW based on UniProtKB P00749.
SMR	Q8MHY7. Positions 31-154, 181-428.
ModBase	Search...
Protein family/group databases
MEROPS	S01.231.
Genome annotation databases
GeneID	100008633.
Phylogenomic databases
HOVERGEN	Q8MHY7.
Enzyme and pathway databases
BRENDA	3.4.21.73. 255.
Family and domain databases
InterPro	IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR000001. Kringle. IPR018056. Kringle_CS. IPR018059. Kringle_sub. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Gene3D	G3DSA:2.40.20.10. Kringle. 1 hit.
Pfam	PF00051. Kringle. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN. PR00018. KRINGLE.
ProDom	PD000395. Kringle. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00181. EGF. 1 hit. SM00130. KR. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS00022. EGF_1. 1 hit. PS01186. EGF_2. False negative. 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]
ProtoNet	Search...

Entry information

Entry name

UROK_RABIT

Accession

Primary (citable) accession number: Q8MHY7
Secondary accession number(s): Q8MIL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)