Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Urokinase-type plasminogen activator

Gene

PLAU

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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)DescriptionActionsGraphical viewLength
Active sitei224Charge relay systemBy similarity1
Active sitei275Charge relay systemBy similarity1
Active sitei376Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processPlasminogen 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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Chromosome 10

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000028589621 – 431Urokinase-type plasminogen activatorAdd BLAST411
ChainiPRO_000028589721 – 177Urokinase-type plasminogen activator long chain ABy similarityAdd BLAST157
ChainiPRO_0000285898156 – 177Urokinase-type plasminogen activator short chain ABy similarityAdd BLAST22
ChainiPRO_0000285899179 – 431Urokinase-type plasminogen activator chain BBy similarityAdd BLAST253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 39By similarity
Disulfide bondi33 ↔ 51By similarity
Disulfide bondi53 ↔ 62By similarity
Disulfide bondi70 ↔ 151By similarity
Disulfide bondi91 ↔ 133By similarity
Disulfide bondi122 ↔ 146By similarity
Modified residuei158PhosphoserineBy similarity1
Disulfide bondi168 ↔ 299Interchain (between A and B chains)PROSITE-ProRule annotation
Disulfide bondi209 ↔ 225By similarity
Disulfide bondi217 ↔ 288By similarity
Disulfide bondi313 ↔ 382By similarity
Glycosylationi322N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei323PhosphoserineBy similarity1
Disulfide bondi345 ↔ 361By similarity
Disulfide bondi372 ↔ 400By similarity

Post-translational modificationi

Phosphorylation of Ser-158 and Ser-323 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

STRINGi9601.ENSPPYP00000002700.

Structurei

3D structure databases

ProteinModelPortaliQ5RF29.
SMRiQ5RF29.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 63EGF-likePROSITE-ProRule annotationAdd BLAST37
Domaini69 – 151KringlePROSITE-ProRule annotationAdd BLAST83
Domaini179 – 424Peptidase S1PROSITE-ProRule annotationAdd BLAST246

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni34 – 57Binds urokinase plasminogen activator surface receptorBy similarityAdd BLAST24
Regioni152 – 178Connecting peptideBy similarityAdd BLAST27

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Kringle, Signal

Phylogenomic databases

eggNOGiENOG410IGFI. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOVERGENiHBG008633.
InParanoidiQ5RF29.
KOiK01348.
OMAiQPWFAAI.
OrthoDBiEOG091G0AH5.
TreeFamiTF329901.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiView protein in InterPro
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
IPR034814. Urokinase.
PANTHERiPTHR24264:SF38. PTHR24264:SF38. 1 hit.
PfamiView protein in Pfam
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiView protein in SMART
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEiView protein in PROSITE
PS00022. 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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5RF29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALLARLLL CVLVVSDSKG SNELHQVPSN CDCLNGGTCV SNKYFSNIHW
60 70 80 90 100
CNCPKKFGGQ HCEIDKSKTC YEGNGHFYRG KASTDTMGRP CLAWNSATVL
110 120 130 140 150
QQTYHAHRSD ALQLGLGKHN YCRNPDNRWR PWCYVQVGLK PLVQECMVHD
160 170 180 190 200
CADGKKPSSP PEELKFQCGQ KTLRPRFKIV GGEFTTIENQ PWFAAIYRRH
210 220 230 240 250
RGGSVTYVCG GSLISPCWVV SATHCFIDYP KKEDYIVYLG RSRLNSHTQG
260 270 280 290 300
EMKFEVENLI LHKDYSADTL AHHNDIALLK IHSKEGRCAQ PSRTIQTICL
310 320 330 340 350
PSMYNDPPFG TSCEITGFGK ENSTDYLYPE QLKMTVVKLI SHRECQQPHY
360 370 380 390 400
YGSEVTTKML CAADPQWKTD SCQGDSGGPL VCSLQGRMTL TGIVSWGRGC
410 420 430
ALKDKPGVYT RVSYFLPWIR SHTKEENGLA L
Length:431
Mass (Da):48,482
Last modified:December 21, 2004 - v1
Checksum:i62E7E952C870408F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857332 mRNA. Translation: CAH89628.1.
RefSeqiNP_001124729.1. NM_001131257.2.

Genome annotation databases

EnsembliENSPPYT00000002791; ENSPPYP00000002700; ENSPPYG00000002324.
GeneIDi100171578.
KEGGipon:100171578.

Similar proteinsi

Entry informationi

Entry nameiUROK_PONAB
AccessioniPrimary (citable) accession number: Q5RF29
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: December 21, 2004
Last modified: October 25, 2017
This is version 90 of the entry and version 1 of the sequence. See 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