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
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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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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.
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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:
- 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:
- 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:
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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:
- 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:
- 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:
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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:
- 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:
- 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:
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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:
- 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:
- 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:
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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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