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P98119 (URT1_DESRO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Salivary plasminogen activator alpha 1

EC=3.4.21.68
Alternative name(s):
DSPA alpha-1
OrganismDesmodus rotundus (Vampire bat)
Taxonomic identifier9430 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaChiropteraMicrochiropteraPhyllostomidaeDesmodontinaeDesmodus

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably essential to support the feeding habits of this exclusively haematophagous animal. Potent thrombolytic agent.

Catalytic activity

Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.

Enzyme regulation

Activity toward plasminogen is stimulated in the presence of fibrin I.

Subunit structure

Monomer.

Subcellular location

Secreted.

Domain

The fibronectin type-I domain mediates binding to fibrin, and the kringle domain apparently mediates fibrin-induced stimulation of activity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 EGF-like domain.

Contains 1 fibronectin type-I domain.

Contains 1 kringle domain.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processPlasminogen activation
   Cellular componentSecreted
   DomainEGF-like domain
Kringle
Signal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636 Potential
Chain37 – 477441Salivary plasminogen activator alpha 1
PRO_0000028340

Regions

Domain40 – 8243Fibronectin type-I
Domain83 – 12139EGF-like
Domain128 – 20982Kringle
Domain226 – 476251Peptidase S1

Sites

Active site2721Charge relay system
Active site3211Charge relay system
Active site4281Charge relay system

Amino acid modifications

Glycosylation1531N-linked (GlcNAc...)
CAR_000027
Glycosylation3981N-linked (GlcNAc...)
CAR_000028
Disulfide bond42 ↔ 72 By similarity
Disulfide bond70 ↔ 79 By similarity
Disulfide bond87 ↔ 98 By similarity
Disulfide bond92 ↔ 109 By similarity
Disulfide bond111 ↔ 120 By similarity
Disulfide bond128 ↔ 209 By similarity
Disulfide bond149 ↔ 191 By similarity
Disulfide bond180 ↔ 204 By similarity
Disulfide bond214 ↔ 345
Disulfide bond257 ↔ 273
Disulfide bond265 ↔ 334
Disulfide bond359 ↔ 434
Disulfide bond391 ↔ 407
Disulfide bond424 ↔ 452

Secondary structure

................................................... 477
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P98119 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: AA06FD1739C10E5E

FASTA47753,616
        10         20         30         40         50         60 
MVNTMKTKLL CVLLLCGAVF SLPRQETYRQ LARGSRAYGV ACKDEITQMT YRRQESWLRP 

        70         80         90        100        110        120 
EVRSKRVEHC QCDRGQARCH TVPVNSCSEP RCFNGGTCWQ AVYFSDFVCQ CPAGYTGKRC 

       130        140        150        160        170        180 
EVDTRATCYE GQGVTYRGTW STAESRVECI NWNSSLLTRR TYNGRMPDAF NLGLGNHNYC 

       190        200        210        220        230        240 
RNPNGAPKPW CYVIKAGKFT SESCSVPVCS KATCGLRKYK EPQLHSTGGL FTDITSHPWQ 

       250        260        270        280        290        300 
AAIFAQNRRS SGERFLCGGI LISSCWVLTA AHCFQESYLP DQLKVVLGRT YRVKPGEEEQ 

       310        320        330        340        350        360 
TFKVKKYIVH KEFDDDTYNN DIALLQLKSD SPQCAQESDS VRAICLPEAN LQLPDWTECE 

       370        380        390        400        410        420 
LSGYGKHKSS SPFYSEQLKE GHVRLYPSSR CAPKFLFNKT VTNNMLCAGD TRSGEIYPNV 

       430        440        450        460        470 
HDACQGDSGG PLVCMNDNHM TLLGIISWGV GCGEKDVPGV YTKVTNYLGW IRDNMHL 

« Hide

References

[1]"The plasminogen activator family from the salivary gland of the vampire bat Desmodus rotundus: cloning and expression."
Kraetzschmar J., Haendler B., Langer G., Boidol W., Bringmann P., Alagon A., Donner P., Schleuning W.-D.
Gene 105:229-237(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Salivary gland.
[2]"Plasminogen activators from the saliva of Desmodus rotundus (common vampire bat): unique fibrin specificity."
Schleuning W.-D., Alagon A., Boidol W., Bringmann P., Petri T., Kraetzschmar J., Haendler B., Langer G., Baldus B., Witt W., Donner P.
Ann. N. Y. Acad. Sci. 667:395-403(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[3]"Catalytic domain structure of vampire bat plasminogen activator: a molecular paradigm for proteolysis without activation cleavage."
Renatus M., Stubbs M.T., Huber R., Bringmann P., Donner P., Schleuning W.-D., Bode W.
Biochemistry 36:13483-13493(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
Tissue: Salivary gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63987 mRNA. Translation: AAA31591.1.
M63986 mRNA. Translation: AAA31592.1.
PIRJS0597.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5IX-ray2.90A213-477[»]
ProteinModelPortalP98119.
SMRP98119. Positions 37-127, 213-477.
ModBaseSearch...

Protein family/group databases

MEROPSS01.239.

PTM databases

GlycoSuiteDBP98119.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008633.

Family and domain databases

Gene3D2.40.20.10. 1 hit.
InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000083. Fibronectin_type1.
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]
PfamPF00008. EGF. 1 hit.
PF00039. fn1. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00181. EGF. 1 hit.
SM00058. FN1. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF57440. Kringle-like. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS01253. FN1_1. 1 hit.
PS51091. FN1_2. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP98119.

Entry information

Entry nameURT1_DESRO
AccessionPrimary (citable) accession number: P98119
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families