Annotations for this protein have been verified by the authors of the corresponding papers



DP00729: Pancreatic trypsin inhibitorFASTA viewXML view

General information
DisProt:DP00729
Name:Pancreatic trypsin inhibitor
Synonym(s):BPT1_BOVIN
Aprotinin
Basic protease inhibitor
BPTI
BPI
First appeared in release:Release 6.00 (07/01/2012)
UniProt:P00974
UniGene: 
SwissProt: BPT1_BOVIN
TrEMBL:  
NCBI (GI):  
Source organism:Bos taurus (Bovine)
Sequence length:100
Percent disordered:34%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MKMSRLCLSV ALLVLLGTLA ASTPGCDTSN QAKAQRPDFC LEPPYTGPCK ARIIRYFYNA - 60
KAGLCQTFVY GGCRAKRNNF KSAEDCMRTC GGAIGPWENL



Functional narrative    

Function: Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.


Subcellular Location: Secreted.
PHARMACEUTICAL: Available under the name Trasylol (Mile). Used for inhibiting coagulation so as to reduce blood loss during bypass surgery.
SIMILARITY: Contains 1 BPTI/Kunitz inhibitor domain.
WEB RESOURCE: Name=Trasylol; Note=Clinical information on Trasylol; URL='http://www.trasylol.com/';
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Region 1: 64-64 Region 2: 49-73 Region 3: 81-87 Region 4: 91-92

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:L64
Location:64 - 64
Length:1
Region sequence:

L

Modification type: Engineered
PDB: 1G6X:A
Structural/functional type: Function arises from the disordered state
Functional classes:  
Functional subclasses: Intraprotein interaction
Detection methods:
  1. X-ray crystallography (292 K; pH: 7.5; BPTI protein 4.5 mg/uL; PEG 400 2 %; Ammonium sulfate 2 M; Na-HEPES 0.1 M; Ethylene glycol (cryoprotectant))

References:
  1. Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. "Ultrahigh-resolution structure of a BPTI mutant." Acta Crystallogr. D Biol. Crystallogr.. 2001; 57(Pt 5): 649-63. PubMed: 11320305

Comments:
 



Region 2
Type:Disordered
Name:auxiliary loop
Location:49 - 73
Length:25
Region sequence:

CKARIIRYFYNAKAGLCQTFVYGGC

Modification type: Engineered
PDB: 1G6X:A
Structural/functional type: Function arises from the disordered state
Functional classes:  
Functional subclasses: Intraprotein interaction
Detection methods:
  1. X-ray crystallography (292 K; pH: 7.5; Ammonium sulfate 2 M; BPTI protein 4.5 mg/uL; Ethylene glycol (cryoprotectant); Na-HEPES 0.1 M; PEG 400 2 %)

References:
  1. Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. "Ultrahigh-resolution structure of a BPTI mutant." Acta Crystallogr. D Biol. Crystallogr.. 2001; 57(Pt 5): 649-63. PubMed: 11320305

Comments:
Residues C49 and C73 form a disulfide bridge.




Region 3
Type:Disordered
Name: 
Location:81 - 87
Length:7
Region sequence:

KSAEDCM

Modification type: Engineered
PDB: 1G6X:A
Structural/functional type: Function arises from the disordered state
Functional classes:  
Functional subclasses: Intraprotein interaction
Detection methods:
  1. X-ray crystallography (292 K; pH: 7.5; Ammonium sulfate 2 M; BPTI protein 4.5 mg/uL; Ethylene glycol (cryoprotectant); Na-HEPES 0.1 M; PEG 400 2 %)

References:
  1. Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. "Ultrahigh-resolution structure of a BPTI mutant." Acta Crystallogr. D Biol. Crystallogr.. 2001; 57(Pt 5): 649-63. PubMed: 11320305

Comments:
 



Region 4
Type:Disordered
Name:disordered GG
Location:91 - 92
Length:2
Region sequence:

GG

Modification type: Engineered
PDB: 1G6X:A
Structural/functional type: Function arises from the disordered state
Functional classes:  
Functional subclasses: Intraprotein interaction
Detection methods:
  1. X-ray crystallography (292 K; pH: 7.5; Ammonium sulfate 2 M; BPTI protein 4.5 mg/uL; Ethylene glycol (cryoprotectant); Na-HEPES 0.1 M; PEG 400 2 %)

References:
  1. Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. "Ultrahigh-resolution structure of a BPTI mutant." Acta Crystallogr. D Biol. Crystallogr.. 2001; 57(Pt 5): 649-63. PubMed: 11320305

Comments:
 



Comments


Addlagatta et al (2001) used mature BPTI (UniProt aa 36-93) engineered with the following mutations: T46A, P48A, K50R and M87L.

UniProt describes residue K50 as a "reactive bond for trypsin" and C40-C90 as "BPTI/Kunitz inhibitor" domain.



AV sent 6-26-2012 (PMID:11320305)
[AV received 6/26/12]


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