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Reviewed, UniProtKB/Swiss-Prot P15638 (URT2_DESRO)

Last modified June 16, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Salivary plasminogen activator alpha 2
    EC=3.4.21.68
Alternative name(s):
    DSPA alpha-2
    BAT-PA
    T-plasminogen activator
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. Probable 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 termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636 Potential
Chain37 – 477441Salivary plasminogen activator alpha 2
PRO_0000028341

Regions

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

Sites

Active site2721Charge relay system By similarity
Active site3211Charge relay system By similarity
Active site4281Charge relay system By similarity

Amino acid modifications

Glycosylation1851N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential
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 By similarity
Disulfide bond257 ↔ 273 By similarity
Disulfide bond265 ↔ 334 By similarity
Disulfide bond359 ↔ 434 By similarity
Disulfide bond391 ↔ 407 By similarity
Disulfide bond424 ↔ 452 By similarity

Experimental info

Sequence conflict4031N → K in AAA31596. Ref.2
Sequence conflict4171Y → H in AAA31596. Ref.2
Sequence conflict4351M → R in AAA31596. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P15638-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 17486555C0E5077C

FASTA47753,719
        10         20         30         40         50         60 
MVNTMKTKLL CVLLLCGAVF SLPRQETYRQ LARGSRAYGV ACRDEKTQMI YQQQESWLRP 

        70         80         90        100        110        120 
EVRSKRVEHC RCDRGLAQCH TVPVKSCSEL RCFNGGTCWQ AASFSDFVCQ CPKGYTGKQC 

       130        140        150        160        170        180 
EVDTHATCYK DQGVTYRGTW STSESGAQCI NWNSNLLTRR TYNGRRSDAI TLGLGNHNYC 

       190        200        210        220        230        240 
RNPDNNSKPW CYVIKASKFI LEFCSVPVCS KATCGLRKYK EPQLHSTGGL FTDITSHPWQ 

       250        260        270        280        290        300 
AAIFAQNRRS SGERFLCGGI LISSCWVLTA AHCFQERYPP QHLRVVLGRT YRVKPGKEEQ 

       310        320        330        340        350        360 
TFEVEKCIVH EEFDDDTYNN DIALLQLKSG SPQCAQESDS VRAICLPEAN LQLPDWTECE 

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

       430        440        450        460        470 
HDACQGDSGG PLVCMNDNHM TLLGIISWGV GCGEKDIPGV YTKVTNYLGW IRDNMRP 

« 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: 1937019] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Salivary gland.
[2]"Isolation, characterization, and cDNA cloning of a vampire bat salivary plasminogen activator."
Gardell S.J., Duong L.T., Diehl R.E., York J.D., Hare T.R., Register R.B., Jacobs J.W., Dixon R.A.F., Friedman P.A.
J. Biol. Chem. 264:17947-17952(1989) [PubMed: 2509450] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Salivary gland.
[3]"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: 1309059] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

M63988 mRNA. Translation: AAA31593.1.
J05082 mRNA. Translation: AAA31596.1.
PIRA34369.
JS0598.

3D structure databases

HSSPHSSP built from PDB template 1A5I based on UniProtKB P98119.
SMRP15638. Positions 37-127, 213-475.
ModBaseSearch...

Protein family/group databases

MEROPSS01.239.

Phylogenomic databases

HOVERGENP15638.

Enzyme and pathway databases

BRENDA3.4.21.68. 291428.

Family and domain databases

InterProIPR016060. Complement_control_module.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR000083. Fibrnctn1.
IPR000001. Kringle.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
Gene3DG3DSA:2.10.70.10. Complement_control_module. 1 hit.
G3DSA:2.40.20.10. Kringle. 1 hit.
PfamPF00008. EGF. 1 hit.
PF00039. fn1. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
PR00018. KRINGLE.
ProDomPD000395. Kringle. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00181. EGF. 1 hit.
SM00058. FN1. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
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...

Entry information

Entry nameURT2_DESRO
AccessionPrimary (citable) accession number: P15638
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents