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Reviewed, UniProtKB/Swiss-Prot P00760 (TRY1_BOVIN)

Last modified September 22, 2009. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Cofactor

Binds 1 calcium ion per subunit.

Subcellular location

Secretedextracellular 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 processDigestion
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium 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

SERPINA1P010091EBI-986385,EBI-986224From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.3
Propeptide18 – 236Activation peptide
PRO_0000028185
Chain24 – 246223Cationic trypsin
PRO_0000028186
Chain24 – 148125Alpha-trypsin chain 1
PRO_0000028187
Chain149 – 24698Alpha-trypsin chain 2
PRO_0000028188

Regions

Domain24 – 244221Peptidase S1
Region194 – 1952Substrate binding
Region197 – 1982Substrate binding

Sites

Active site631Charge relay system
Active site1071Charge relay system
Active site2001Charge relay system
Metal binding751Calcium
Metal binding771Calcium; via carbonyl oxygen
Metal binding801Calcium; via carbonyl oxygen
Metal binding851Calcium
Binding site2001Substrate

Amino acid modifications

Disulfide bond30 ↔ 160 Ref.3 Ref.7 Ref.10
Disulfide bond48 ↔ 64 Ref.3 Ref.7 Ref.10
Disulfide bond132 ↔ 233 Ref.3 Ref.7 Ref.10
Disulfide bond139 ↔ 206 Ref.3 Ref.7 Ref.10
Disulfide bond171 ↔ 185 Ref.3 Ref.7 Ref.10
Disulfide bond196 ↔ 220 Ref.3 Ref.7 Ref.10

Secondary structure

....................................... 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00760-1 [UniParc].

Last modified September 2, 2008. Version 3.
Checksum: 092E3D8ACCCCC4D3

FASTA24625,785
        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 

« Hide

References

« Hide '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.

Cross-references

Sequence databases

BC134797 mRNA. Translation: AAI34798.1.
BC146041 mRNA. Translation: AAI46042.1.
D38507 mRNA. Translation: BAA07516.1.
IPIIPI00706427.
PIRTRBOTR. A90164.
RefSeqNP_001107199.1.
XP_001790399.1.
XP_871686.2.
UniGeneBt.61325
Bt.91423

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AQ7X-ray2.20A24-246[»]
1AUJX-ray2.10A24-246[»]
1AZ8X-ray1.80A24-246[»]
1BJUX-ray1.80A24-246[»]
1BJVX-ray1.80A24-246[»]
1BTPX-ray2.20A18-246[»]
1BTWX-ray1.70A18-246[»]
1BTXX-ray1.70A18-246[»]
1BTYX-ray1.50A18-246[»]
1BTZX-ray2.00A18-246[»]
1C1NX-ray1.40A24-246[»]
1C1OX-ray1.40A24-246[»]
1C1PX-ray1.37A24-246[»]
1C1QX-ray1.37A24-246[»]
1C1RX-ray1.37A24-246[»]
1C1SX-ray1.63A24-246[»]
1C1TX-ray1.37A24-246[»]
1C2DX-ray1.65A24-246[»]
1C2EX-ray1.65A24-246[»]
1C2FX-ray1.70A24-246[»]
1C2GX-ray1.65A24-246[»]
1C2HX-ray1.40A24-246[»]
1C2IX-ray1.47A24-246[»]
1C2JX-ray1.40A24-246[»]
1C2KX-ray1.65A24-246[»]
1C2LX-ray1.50A24-246[»]
1C2MX-ray1.40A24-246[»]
1C5PX-ray1.43A24-246[»]
1C5QX-ray1.43A24-246[»]
1C5RX-ray1.47A24-246[»]
1C5SX-ray1.36A24-246[»]
1C5TX-ray1.37A24-246[»]
1C5UX-ray1.37A24-246[»]
1C5VX-ray1.48A24-246[»]
1C9TX-ray3.30A/B/C/D/E/F24-246[»]
1CE5X-ray1.90A24-246[»]
1CU7model-A24-246[»]
1CU8model-A24-246[»]
1CU9model-A24-246[»]
1D6RX-ray2.30A24-246[»]
1EB2X-ray2.00A24-246[»]
1EJMX-ray1.85A/C/E24-246[»]
1EZXX-ray2.60C1-246[»]
1F0TX-ray1.80A1-246[»]
1F0UX-ray1.90A1-246[»]
1F2SX-ray1.79E24-246[»]
1G36X-ray1.90A24-246[»]
1G3BX-ray1.80A19-246[»]
1G3CX-ray1.80A19-246[»]
1G3DX-ray1.80A19-246[»]
1G3EX-ray1.80A19-246[»]
1G9IX-ray2.20E24-246[»]
1GBTX-ray2.00A24-246[»]
1GHZX-ray1.39A24-246[»]
1GI0X-ray1.42A24-246[»]
1GI1X-ray1.42A24-246[»]
1GI2X-ray1.38A24-246[»]
1GI3X-ray1.44A24-246[»]
1GI4X-ray1.37A24-246[»]
1GI5X-ray1.60A24-246[»]
1GI6X-ray1.49A24-246[»]
1GJ6X-ray1.50A24-246[»]
1HJ9X-ray0.95A24-246[»]
1J8AX-ray1.21A24-246[»]
1JIRX-ray2.00A24-246[»]
1JRSX-ray1.80A24-246[»]
1JRTX-ray1.70A24-246[»]
1K1IX-ray2.20A24-246[»]
1K1JX-ray2.20A24-246[»]
1K1LX-ray2.50A24-246[»]
1K1MX-ray2.20A24-246[»]
1K1NX-ray2.00A24-246[»]
1K1OX-ray2.00A24-246[»]
1K1PX-ray1.90A24-246[»]
1LQEX-ray2.20A1-246[»]
1MAXX-ray1.80A24-246[»]
1MAYX-ray1.80A24-246[»]
1MTSX-ray1.90A24-246[»]
1MTUX-ray1.90A24-246[»]
1MTVX-ray1.90A24-246[»]
1MTWX-ray1.90A24-246[»]
1N6XX-ray1.40A24-246[»]
1N6YX-ray1.40A24-246[»]
1NC6X-ray1.90A24-246[»]
1NTPneutron diffraction1.80A24-246[»]
1O2HX-ray1.77A24-246[»]
1O2IX-ray1.50A24-246[»]
1O2JX-ray1.65A24-246[»]
1O2KX-ray1.63A24-246[»]
1O2LX-ray1.68A24-246[»]
1O2MX-ray1.69A24-246[»]
1O2NX-ray1.50A24-246[»]
1O2OX-ray1.63A24-246[»]
1O2PX-ray1.47A24-246[»]
1O2QX-ray1.50A24-246[»]
1O2RX-ray1.45A24-246[»]
1O2SX-ray1.65A24-246[»]
1O2TX-ray1.62A24-246[»]
1O2UX-ray1.41A24-246[»]
1O2VX-ray1.50A24-246[»]
1O2WX-ray1.38A24-246[»]
1O2XX-ray1.46A24-246[»]
1O2YX-ray1.45A24-246[»]
1O2ZX-ray1.65A24-246[»]
1O30X-ray1.55A24-246[»]
1O31X-ray1.66A24-246[»]
1O32X-ray1.78A24-246[»]
1O33X-ray1.46A24-246[»]
1O34X-ray1.50A24-246[»]
1O35X-ray1.41A24-246[»]
1O36X-ray1.70A24-246[»]
1O37X-ray1.45A24-246[»]
1O38X-ray1.38A24-246[»]
1O39X-ray1.59A24-246[»]
1O3AX-ray2.00A24-246[»]
1O3BX-ray1.75A24-246[»]
1O3CX-ray1.64A24-246[»]
1O3DX-ray1.33A24-246[»]
1O3EX-ray1.64A24-246[»]
1O3FX-ray1.55A24-246[»]
1O3GX-ray1.55A24-246[»]
1O3HX-ray1.53A24-246[»]
1O3IX-ray1.51A24-246[»]
1O3JX-ray1.40A24-246[»]
1O3KX-ray1.43A24-246[»]
1O3LX-ray1.40A24-246[»]
1O3MX-ray1.55A24-246[»]
1O3NX-ray1.55A24-246[»]
1O3OX-ray1.55A24-246[»]
1OPHX-ray2.30B1-246[»]
1OX1X-ray2.00A24-246[»]
1OYQX-ray1.90A24-246[»]
1P2IX-ray1.65A24-246[»]
1P2JX-ray1.35A24-246[»]
1P2KX-ray1.60A24-246[»]
1PPCX-ray1.80E24-246[»]
1PPEX-ray2.00E24-246[»]
1PPHX-ray1.90E24-246[»]
1QA0X-ray1.80A24-246[»]
1QB1X-ray1.80A24-246[»]
1QB6X-ray1.80A24-246[»]
1QB9X-ray1.80A24-246[»]
1QBNX-ray1.80A24-246[»]
1QBOX-ray1.80A24-246[»]
1QCPX-ray1.80A24-246[»]
1QL7X-ray2.10A24-246[»]
1QL8X-ray3.00A24-246[»]
1RXPX-ray1.70A24-246[»]
1S0QX-ray1.02A24-246[»]
1S0RX-ray1.02A24-246[»]
1SBWX-ray1.80A24-246[»]
1SFIX-ray1.65A24-246[»]
1SMFX-ray2.10E24-246[»]
1TABX-ray2.30E24-246[»]
1TAWX-ray1.80A24-246[»]
1TGBX-ray1.80A18-246[»]
1TGCX-ray1.80A18-246[»]
1TGNX-ray1.65A18-246[»]
1TGSX-ray1.80Z18-246[»]
1TGTX-ray1.70A18-246[»]
1TIOX-ray1.93A24-246[»]
1TLDX-ray1.50A24-246[»]
1TNGX-ray1.80A18-246[»]
1TNHX-ray1.80A18-246[»]
1TNIX-ray1.90A18-246[»]
1TNJX-ray1.80A18-246[»]
1TNKX-ray1.80A18-246[»]
1TNLX-ray1.90A18-246[»]
1TPAX-ray1.90E24-246[»]
1TPOX-ray1.70A24-246[»]
1TPPX-ray1.40A24-246[»]
1TPSX-ray1.90A24-246[»]
1TX7X-ray1.75A24-246[»]
1TX8X-ray1.70A24-246[»]
1TYNX-ray2.00A24-246[»]
1UTNX-ray1.15A1-246[»]
1UTOX-ray1.15A1-246[»]
1UTPX-ray1.30A1-246[»]
1UTQX-ray1.15A1-246[»]
1V2JX-ray1.90T24-246[»]
1V2KX-ray2.00T24-246[»]
1V2LX-ray1.60T24-246[»]
1V2MX-ray1.65T24-246[»]
1V2NX-ray1.80T24-246[»]
1V2OX-ray1.62T24-246[»]
1V2PX-ray1.92T24-246[»]
1V2QX-ray2.30T24-246[»]
1V2RX-ray1.70T24-246[»]
1V2SX-ray1.72T24-246[»]
1V2TX-ray1.90T24-246[»]
1V2UX-ray1.80T24-246[»]
1V2VX-ray1.80T24-246[»]
1V2WX-ray1.75T24-246[»]
1XUFX-ray1.90A24-246[»]
1XUGX-ray1.50A24-246[»]
1XUHX-ray2.20A24-246[»]
1XUIX-ray1.50A24-246[»]
1XUJX-ray1.92A24-246[»]
1XUKX-ray1.80A24-246[»]
1Y3UX-ray1.80A24-246[»]
1Y3VX-ray1.60A20-48[»]
1Y3WX-ray1.80A24-243[»]
1Y3XX-ray1.70A20-48[»]
1Y3YX-ray1.75A24-239[»]
1Y59X-ray1.20T24-246[»]
1Y5AX-ray1.40T24-246[»]
1Y5BX-ray1.65T24-246[»]
1Y5UX-ray1.60T24-246[»]
1YP9X-ray2.10A24-246[»]
1YYYX-ray2.10124-246[»]
1ZR0X-ray1.80A/C24-246[»]
1ZZZX-ray1.90A10-246[»]
2A7HX-ray2.10A24-246[»]
2AGEX-ray1.15X24-246[»]
2AGGX-ray1.28X24-246[»]
2AGIX-ray1.14X24-246[»]
2AH4X-ray1.13X24-246[»]
2AYWX-ray0.97A24-246[»]
2BLVX-ray1.20A24-246[»]
2BLWX-ray1.20A24-246[»]
2BTCX-ray1.50E24-246[»]
2BY5X-ray1.30X1-246[»]
2BY6X-ray1.30X1-246[»]
2BY7X-ray1.30X1-246[»]
2BY8X-ray1.30X1-246[»]
2BY9X-ray1.30X1-246[»]
2BYAX-ray1.30X1-246[»]
2BZAX-ray1.90A24-246[»]
2CMYX-ray2.25A24-246[»]
2D8WX-ray2.00A24-246[»]
2F3CX-ray2.50E24-246[»]
2FI3X-ray1.58E24-246[»]
2FI4X-ray1.58E24-246[»]
2FI5X-ray1.58E24-246[»]
2FTLX-ray1.62E24-246[»]
2FTMX-ray1.65A24-246[»]
2FX4X-ray1.65A24-246[»]
2FX6X-ray1.57A24-246[»]
2G55X-ray1.82A24-246[»]
2G5NX-ray1.51A24-246[»]
2G5VX-ray1.45A24-246[»]
2G81X-ray1.55E24-246[»]
2G8TX-ray1.41A24-246[»]
2ILNX-ray2.00A/B24-246[»]
2J9NX-ray1.50A24-246[»]
2O9QX-ray1.70A24-246[»]
2OTVX-ray1.56A24-246[»]
2OXSX-ray1.32A24-246[»]
2PLXX-ray1.56A24-246[»]
2PTCX-ray1.90E24-246[»]
2PTNX-ray1.55A24-246[»]
2QN5X-ray3.00T21-243[»]
2QYIX-ray2.60A/C21-243[»]
2TGAX-ray1.80A18-246[»]
2TGDX-ray2.10A18-246[»]
2TGPX-ray1.90Z18-246[»]
2TGTX-ray1.70A18-246[»]
2TIOX-ray1.93A24-246[»]
2TLDX-ray2.60E24-246[»]
2TPIX-ray2.10Z18-246[»]
2UUYX-ray1.15A24-246[»]
2ZDKX-ray1.67A24-246[»]
2ZDLX-ray1.80A24-246[»]
2ZDMX-ray1.93A24-246[»]
2ZDNX-ray1.98A24-246[»]
2ZFSX-ray1.51A24-246[»]
2ZFTX-ray1.76A24-246[»]
2ZHDX-ray1.94A24-246[»]
2ZQ1X-ray1.68A24-243[»]
2ZQ2X-ray1.40A24-243[»]
3BTDX-ray1.90E24-246[»]
3BTEX-ray1.85E24-246[»]
3BTFX-ray1.80E24-246[»]
3BTGX-ray1.90E24-246[»]
3BTHX-ray1.75E24-246[»]
3BTKX-ray1.85E24-246[»]
3BTMX-ray1.80E24-246[»]
3BTQX-ray1.90E24-246[»]
3BTTX-ray1.90E24-246[»]
3BTWX-ray2.05E24-246[»]
3D65X-ray1.64E24-243[»]
3E8LX-ray2.48A/B24-243[»]
3PTBX-ray1.70A24-246[»]
3PTNX-ray1.70A24-246[»]
3TPIX-ray1.90Z18-246[»]
4TPIX-ray2.20Z18-246[»]
5PTPX-ray1.34A24-246[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP00760. 1 interaction.

Protein family/group databases

MEROPSS01.151.

Genome annotation databases

EnsemblENSBTAT00000004737; ENSBTAP00000004737; ENSBTAG00000003633; Bos taurus. [Genome view]
ENSBTAT00000033479; ENSBTAP00000033392; ENSBTAG00000024245; Bos taurus. [Genome view]
GeneID615026.
780933.
KEGGbta:615026.
bta:780933.

Phylogenomic databases

HOVERGENP00760.

Enzyme and pathway databases

BRENDA3.4.21.4. 251.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP00760.
DrugBankDB01093. Dimethyl sulfoxide.
PMAP-CutDBP00760.

Entry information

Entry nameTRY1_BOVIN
AccessionPrimary (citable) accession number: P00760
Secondary accession number(s): A6H6Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 2, 2008
Last modified: September 22, 2009
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents