Reviewed, UniProtKB/Swiss-Prot P00760 (TRY1_BOVIN)

Names and origin

Protein names	Recommended name:     Cationic trypsin     EC=3.4.21.4 Alternative name(s):     Beta-trypsin Cleaved into the following 2 chains:     1- Recommended name:             Alpha-trypsin chain 1     2- Recommended name:             Alpha-trypsin chain 2
Organism	Bos taurus (Bovine)
Taxonomic identifier	9913 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Cofactor	Binds 1 calcium ion per subunit.
Subcellular location	Secreted › extracellular space.
Tissue specificity	Synthesized in the acinar cells of the pancreas.
Post-translational modification	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. Not sulfated on tyrosine residue(s).
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Digestion
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	digestion Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SERPINA1	P01009	1	EBI-986385,EBI-986224	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Propeptide

18 – 23

6

Activation peptide

PRO_0000028185

Chain

24 – 246

223

Cationic trypsin

PRO_0000028186

Chain

24 – 148

125

Alpha-trypsin chain 1

PRO_0000028187

Chain

149 – 246

98

Alpha-trypsin chain 2

PRO_0000028188

Regions

Domain

24 – 244

221

Peptidase S1

Region

194 – 195

2

Substrate binding

Region

197 – 198

2

Substrate binding

Sites

Active site

63

1

Charge relay system

Active site

107

1

Charge relay system

Active site

200

1

Charge relay system

Metal binding

75

1

Calcium

Metal binding

77

1

Calcium; via carbonyl oxygen

Metal binding

80

1

Calcium; via carbonyl oxygen

Metal binding

85

1

Calcium

Binding site

200

1

Substrate

Amino acid modifications

Disulfide bond

30 ↔ 160

Disulfide bond

48 ↔ 64

Disulfide bond

132 ↔ 233

Disulfide bond

139 ↔ 206

Disulfide bond

171 ↔ 185

Disulfide bond

196 ↔ 220

Secondary structure

1

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246

Helix Strand Turn

Details...

Beta strand

38 – 54

17

Beta strand

57 – 60

4

Helix

62 – 64

3

Beta strand

70 – 74

5

Beta strand

86 – 95

10

Turn

101 – 104

4

Beta strand

109 – 115

7

Beta strand

120 – 123

4

Beta strand

138 – 144

7

Beta strand

149 – 151

3

Beta strand

159 – 165

7

Helix

168 – 174

7

Turn

176 – 178

3

Beta strand

183 – 187

5

Beta strand

203 – 206

4

Beta strand

209 – 216

8

Beta strand

218 – 221

4

Beta strand

227 – 231

5

Helix

232 – 235

4

Helix

236 – 244

9

Sequences

	Sequence		Length	Mass (Da)
	P00760-1 [UniParc]. Last modified September 2, 2008. Version 3. Checksum: 092E3D8ACCCCC4D3	FASTA	246	25,785
	10 20 30 40 50 60 MKTFIFLALL GAAVAFPVDD DDKIVGGYTC GANTVPYQVS LNSGYHFCGG SLINSQWVVS 70 80 90 100 110 120 AAHCYKSGIQ VRLGEDNINV VEGNEQFISA SKSIVHPSYN SNTLNNDIML IKLKSAASLN 130 140 150 160 170 180 SRVASISLPT SCASAGTQCL ISGWGNTKSS GTSYPDVLKC LKAPILSDSS CKSAYPGQIT 190 200 210 220 230 240 SNMFCAGYLE GGKDSCQGDS GGPVVCSGKL QGIVSWGSGC AQKNKPGVYT KVCNYVSWIK QTIASN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal pancreas.
[2]	Okajima T., Maniwa M., Nagao S., Fujikawa H., Goto S. Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-246. Tissue: Pancreas.
[3]	"Covalent structure of bovine trypsinogen. The position of the remaining amides." Mikes O., Holeysovsky V., Tomasek V., Sorm F. Biochem. Biophys. Res. Commun. 24:346-352(1966) [PubMed: 5967094] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-246, DISULFIDE BONDS.
[4]	"Homologies in serine proteinases." Hartley B.S. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 257:77-87(1970) [PubMed: 4399051] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"Amino acid sequence of dogfish trypsin." Titani K., Ericsson L.H., Neurath H., Walsh K.A. Biochemistry 14:1358-1366(1975) [PubMed: 1092332] [Abstract] Cited for: SEQUENCE REVISION.
[6]	"Human cationic trypsinogen is sulfated on Tyr154." Sahin-Toth M., Kukor Z., Nemoda Z. FEBS J. 273:5044-5050(2006) [PubMed: 17087724] [Abstract] Cited for: ABSENCE OF SULFATED TYROSINE.
[7]	"The disulphide bridges of trypsin." Kauffman D.L. J. Mol. Biol. 12:929-932(1965) [PubMed: 5892911] [Abstract] Cited for: DISULFIDE BONDS.
[8]	"The refined crystal structure of bovine beta-trypsin at 1.8-A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0." Bode W., Schwager P. J. Mol. Biol. 98:693-717(1975) [PubMed: 512] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF CALCIUM-BINDING SITE.
[9]	"Structure of bovine trypsinogen at 1.9-A resolution." Kossiakoff A.A., Chambers J.L., Kay L.M., Stroud R.M. Biochemistry 16:654-664(1977) [PubMed: 556951] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[10]	"An unusual helix-turn-helix protease inhibitory motif in a novel trypsin inhibitor from seeds of Veronica (Veronica hederifolia L.)." Conners R., Konarev A.V., Forsyth J., Lovegrove A., Marsh J., Joseph-Horne T., Shewry P., Brady R.L. J. Biol. Chem. 282:27760-27768(2007) [PubMed: 17640870] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 24-246 IN COMPLEX WITH V.HEDERIFOLIA TRYPSIN INHIBITOR, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBLGenBankDDBJ

BC134797 mRNA. Translation: AAI34798.1.
BC146041 mRNA. Translation: AAI46042.1.
D38507 mRNA. Translation: BAA07516.1.

PIR

TRBOTR. A90164.

RefSeq

NP_001107199.1.
XP_001790399.1.
XP_871686.2.

UniGene

Bt.56229
Bt.61325
Bt.63955
Bt.67677
Bt.72554
Bt.91178
Bt.91252
Bt.91405
Bt.91423
Bt.91858
Bt.92689

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AQ7	X-ray	2.20	A	24-246	[»]
1AUJ	X-ray	2.10	A	24-246	[»]
1AZ8	X-ray	1.80	A	24-246	[»]
1BJU	X-ray	1.80	A	24-246	[»]
1BJV	X-ray	1.80	A	24-246	[»]
1BTP	X-ray	2.20	A	18-246	[»]
1BTW	X-ray	1.70	A	18-246	[»]
1BTX	X-ray	1.70	A	18-246	[»]
1BTY	X-ray	1.50	A	18-246	[»]
1BTZ	X-ray	2.00	A	18-246	[»]
1C1N	X-ray	1.40	A	24-246	[»]
1C1O	X-ray	1.40	A	24-246	[»]
1C1P	X-ray	1.37	A	24-246	[»]
1C1Q	X-ray	1.37	A	24-246	[»]
1C1R	X-ray	1.37	A	24-246	[»]
1C1S	X-ray	1.63	A	24-246	[»]
1C1T	X-ray	1.37	A	24-246	[»]
1C2D	X-ray	1.65	A	24-246	[»]
1C2E	X-ray	1.65	A	24-246	[»]
1C2F	X-ray	1.70	A	24-246	[»]
1C2G	X-ray	1.65	A	24-246	[»]
1C2H	X-ray	1.40	A	24-246	[»]
1C2I	X-ray	1.47	A	24-246	[»]
1C2J	X-ray	1.40	A	24-246	[»]
1C2K	X-ray	1.65	A	24-246	[»]
1C2L	X-ray	1.50	A	24-246	[»]
1C2M	X-ray	1.40	A	24-246	[»]
1C5P	X-ray	1.43	A	24-246	[»]
1C5Q	X-ray	1.43	A	24-246	[»]
1C5R	X-ray	1.47	A	24-246	[»]
1C5S	X-ray	1.36	A	24-246	[»]
1C5T	X-ray	1.37	A	24-246	[»]
1C5U	X-ray	1.37	A	24-246	[»]
1C5V	X-ray	1.48	A	24-246	[»]
1C9T	X-ray	3.30	A/B/C/D/E/F	24-246	[»]
1CE5	X-ray	1.90	A	24-246	[»]
1CU7	model	-	A	24-246	[»]
1CU8	model	-	A	24-246	[»]
1CU9	model	-	A	24-246	[»]
1D6R	X-ray	2.30	A	24-246	[»]
1EB2	X-ray	2.00	A	24-246	[»]
1EJM	X-ray	1.85	A/C/E	24-246	[»]
1EZX	X-ray	2.60	C	1-246	[»]
1F0T	X-ray	1.80	A	1-246	[»]
1F0U	X-ray	1.90	A	1-246	[»]
1F2S	X-ray	1.79	E	24-246	[»]
1G36	X-ray	1.90	A	24-246	[»]
1G3B	X-ray	1.80	A	19-246	[»]
1G3C	X-ray	1.80	A	19-246	[»]
1G3D	X-ray	1.80	A	19-246	[»]
1G3E	X-ray	1.80	A	19-246	[»]
1G9I	X-ray	2.20	E	24-246	[»]
1GBT	X-ray	2.00	A	24-246	[»]
1GHZ	X-ray	1.39	A	24-246	[»]
1GI0	X-ray	1.42	A	24-246	[»]
1GI1	X-ray	1.42	A	24-246	[»]
1GI2	X-ray	1.38	A	24-246	[»]
1GI3	X-ray	1.44	A	24-246	[»]
1GI4	X-ray	1.37	A	24-246	[»]
1GI5	X-ray	1.60	A	24-246	[»]
1GI6	X-ray	1.49	A	24-246	[»]
1GJ6	X-ray	1.50	A	24-246	[»]
1HJ9	X-ray	0.95	A	24-246	[»]
1J8A	X-ray	1.21	A	24-246	[»]
1JIR	X-ray	2.00	A	24-246	[»]
1JRS	X-ray	1.80	A	24-246