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Q5RF29

- UROK_PONAB

UniProt

Q5RF29 - UROK_PONAB

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Protein

Urokinase-type plasminogen activator

Gene

PLAU

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei224 – 2241Charge relay systemBy similarity
Active sitei275 – 2751Charge relay systemBy similarity
Active sitei376 – 3761Charge relay systemBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. fibrinolysis Source: Ensembl
  2. regulation of cell adhesion mediated by integrin Source: Ensembl
  3. regulation of cell proliferation Source: Ensembl
  4. regulation of receptor activity Source: Ensembl
  5. regulation of smooth muscle cell-matrix adhesion Source: Ensembl
  6. regulation of smooth muscle cell migration Source: Ensembl
  7. response to hypoxia Source: Ensembl
  8. smooth muscle cell migration Source: Ensembl
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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Chromosome 10

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 431411Urokinase-type plasminogen activatorPRO_0000285896Add
BLAST
Chaini21 – 177157Urokinase-type plasminogen activator long chain ABy similarityPRO_0000285897Add
BLAST
Chaini156 – 17722Urokinase-type plasminogen activator short chain ABy similarityPRO_0000285898Add
BLAST
Chaini179 – 431253Urokinase-type plasminogen activator chain BBy similarityPRO_0000285899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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 residuei158 – 1581PhosphoserineBy similarity
Disulfide bondi168 ↔ 299Interchain (between A and B chains)PROSITE-ProRule annotation
Disulfide bondi209 ↔ 225By similarity
Disulfide bondi217 ↔ 288By similarity
Disulfide bondi313 ↔ 382By similarity
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
Modified residuei323 – 3231PhosphoserineBy similarity
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

Structurei

3D structure databases

ProteinModelPortaliQ5RF29.
SMRiQ5RF29. Positions 26-155, 166-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 6337EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini69 – 15183KringlePROSITE-ProRule annotationAdd
BLAST
Domaini179 – 424246Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 5724Binds urokinase plasminogen activator surface receptorBy similarityAdd
BLAST
Regioni152 – 17827Connecting peptideBy similarityAdd
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

GeneTreeiENSGT00760000119133.
HOVERGENiHBG008633.
InParanoidiQ5RF29.
KOiK01348.
OMAiKMLCAAD.
OrthoDBiEOG75B84T.
TreeFamiTF329901.

Family and domain databases

Gene3Di2.40.20.10. 1 hit.
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.
SMARTiSM00181. EGF. 1 hit.
SM00130. 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.

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:
EMBL
GenBank
DDBJ
Links Updated
CR857332 mRNA. Translation: CAH89628.1.
RefSeqiNP_001124729.1. NM_001131257.2.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857332 mRNA. Translation: CAH89628.1 .
RefSeqi NP_001124729.1. NM_001131257.2.

3D structure databases

ProteinModelPortali Q5RF29.
SMRi Q5RF29. Positions 26-155, 166-426.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S01.231.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSPPYT00000002791 ; ENSPPYP00000002700 ; ENSPPYG00000002324 .
GeneIDi 100171578.
KEGGi pon:100171578.

Organism-specific databases

CTDi 5328.

Phylogenomic databases

GeneTreei ENSGT00760000119133.
HOVERGENi HBG008633.
InParanoidi Q5RF29.
KOi K01348.
OMAi KMLCAAD.
OrthoDBi EOG75B84T.
TreeFami TF329901.

Family and domain databases

Gene3Di 2.40.20.10. 1 hit.
InterProi IPR000742. 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 ]
Pfami PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00181. EGF. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiUROK_PONAB
AccessioniPrimary (citable) accession number: Q5RF29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 69 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