DP00728: Cationic trypsinFASTA viewXML view

General information
DisProt:DP00728
Name:Cationic trypsin
Synonym(s):TRY1_BOVIN
Beta-trypsin
Alpha-trypsin chain 1 [cleavage product 1] (aa 24-148)
Alpha-trypsin chain 2 [cleavage product 2] (aa 149-246)
Trypsinogen
First appeared in release:Release 6.00 (07/01/2012)
UniProt:P00760
UniGene: 
SwissProt: TRY1_BOVIN
TrEMBL:  
NCBI (GI):  
Source organism:Bos taurus (Bovine)
Sequence length:246
Percent disordered:17%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MKTFIFLALL GAAVAFPVDD DDKIVGGYTC GANTVPYQVS LNSGYHFCGG SLINSQWVVS - 60
AAHCYKSGIQ VRLGEDNINV VEGNEQFISA SKSIVHPSYN SNTLNNDIML IKLKSAASLN - 120
SRVASISLPT SCASAGTQCL ISGWGNTKSS GTSYPDVLKC LKAPILSDSS CKSAYPGQIT - 180
SNMFCAGYLE GGKDSCQGDS GGPVVCSGKL QGIVSWGSGC AQKNKPGVYT KVCNYVSWIK - 240
QTIASN



Functional narrative    

CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
COFACTOR: Binds 1 calcium ion per subunit. P01009:SERPINA1 (xeno); NbExp=3; IntAct=EBI-986385, EBI-986224;


Subcellular Location: Secreted, extracellular space.
TISSUE SPECIFICITY: Synthesized in the acinar cells of the pancreas.
PTM: Autocatalytic cleavage after Lys-23 leads to beta-trypsin by releasing a terminal hexapeptide. Subsequent cleavage after Lys- 148 leads to alpha-trypsin. Further cleavage after Lys-193 yields pseudotrypsin. A cleavage may also occur after Arg-122.
PTM: Not sulfated on tyrosine residue(s).
SIMILARITY: Belongs to the peptidase S1 family.
SIMILARITY: Contains 1 peptidase S1 domain.
WEB RESOURCE: Name=Worthington enzyme manual; URL='http://www.worthington-biochem.com/TRY/';
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Region 1: 18-27 Region 2: 145-155 Region 3: 187-198 Region 4: 217-224

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:Activation domain, segment 1
Location:18 - 27
Length:10
Region sequence:

VDDDDKIVGG

Modification type: Complex
PDB: 2TPI:Z
Structural/functional type: Function arises from the disordered state
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (298 K; pH: 7; Ile-Val dipeptide 1 mM; MgSO4 2.4 M; PTI (pancreatic trypsin inhibitor (4:1 M ratio)) 1 M; TgHg (alone or in complex) (Trypsinogen with bound mercury) 4 M)

References:
  1. Walter J, Steigemann W, Singh TP, Bartunik H, Bode W, Huber R. "On the Disordered Activation Domain in Trypsinogen. Chemical Labelling and Low-Temperature Crystallography." Acta Crystallographica, Section B. 1982; 38(5): 1462–1472.

Comments:
 



Region 2
Type:Disordered
Name:Activation domain, segment 2
Location:145 - 155
Length:11
Region sequence:

GNTKSSGTSYP

Modification type: Complex
PDB: 2TPI:Z
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (298 K; pH: 7; Ile-Val dipeptide 1 mM; MgSO4 2.4 M; PTI (pancreatic trypsin inhibitor (4:1 M ratio)) 1 M; TgHg (alone or in complex) (Trypsinogen with bound mercury) 4 M)

References:
  1. Walter J, Steigemann W, Singh TP, Bartunik H, Bode W, Huber R. "On the Disordered Activation Domain in Trypsinogen. Chemical Labelling and Low-Temperature Crystallography." Acta Crystallographica, Section B. 1982; 38(5): 1462–1472.

Comments:
 



Region 3
Type:Disordered
Name:Activation domain, segment 3
Location:187 - 198
Length:12
Region sequence:

GYLEGGKDSCQG

Modification type: Complex
PDB: 2TPI:Z
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (298 K; pH: 7; Ile-Val dipeptide 1 mM; MgSO4 2.4 M; PTI (pancreatic trypsin inhibitor (4:1 M ratio)) 1 M; TgHg (alone or in complex) (Trypsinogen with bound mercury) 4 M)

References:
  1. Walter J, Steigemann W, Singh TP, Bartunik H, Bode W, Huber R. "On the Disordered Activation Domain in Trypsinogen. Chemical Labelling and Low-Temperature Crystallography." Acta Crystallographica, Section B. 1982; 38(5): 1462–1472.

Comments:
 



Region 4
Type:Disordered
Name:Activation domain, segment 4
Location:217 - 224
Length:8
Region sequence:

GSGCAQKN

Modification type: Complex
PDB: 2TPI:Z
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (298 K; pH: 7; Ile-Val dipeptide 1 mM; MgSO4 2.4 M; PTI (pancreatic trypsin inhibitor (4:1 M ratio)) 1 M; TgHg (alone or in complex) (Trypsinogen with bound mercury) 4 M)

References:
  1. Walter J, Steigemann W, Singh TP, Bartunik H, Bode W, Huber R. "On the Disordered Activation Domain in Trypsinogen. Chemical Labelling and Low-Temperature Crystallography." Acta Crystallographica, Section B. 1982; 38(5): 1462–1472.

Comments:
 



Comments


UniProt describes a signal peptide at aa M1-P17.

Walter et al (1982) describe a disordered activation domain comprising four segments that "is rigidified upon forming a complex with PTI and the dipeptide."



AV sent to Dr. W. Bode (6-26-2012)


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