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P00761 (TRYP_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trypsin

EC=3.4.21.4
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length231 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.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 88Activation peptide
PRO_0000028205
Chain9 – 231223Trypsin
PRO_0000028206

Regions

Domain9 – 229221Peptidase S1

Sites

Active site481Charge relay system
Active site921Charge relay system
Active site1851Charge relay system
Metal binding601Calcium
Metal binding621Calcium; via carbonyl oxygen
Metal binding651Calcium; via carbonyl oxygen
Metal binding701Calcium
Site1791Required for specificity By similarity

Amino acid modifications

Disulfide bond15 ↔ 145
Disulfide bond33 ↔ 49
Disulfide bond117 ↔ 218
Disulfide bond124 ↔ 191
Disulfide bond156 ↔ 170
Disulfide bond181 ↔ 205

Natural variations

Natural variant201I → V.

Secondary structure

.............................................. 231
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00761 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: A0A125CF7FC138C2

FASTA23124,409
        10         20         30         40         50         60 
FPTDDDDKIV GGYTCAANSI PYQVSLNSGS HFCGGSLINS QWVVSAAHCY KSRIQVRLGE 

        70         80         90        100        110        120 
HNIDVLEGNE QFINAAKIIT HPNFNGNTLD NDIMLIKLSS PATLNSRVAT VSLPRSCAAA 

       130        140        150        160        170        180 
GTECLISGWG NTKSSGSSYP SLLQCLKAPV LSDSSCKSSY PGQITGNMIC VGFLEGGKDS 

       190        200        210        220        230 
CQGDSGGPVV CNGQLQGIVS WGYGCAQKNK PGVYTKVCNY VNWIQQTIAA N 

« Hide

References

[1]"On trypsinogen and trypsin of pig."
Charles M., Rovery M., Guidoni A.A., Desnuelle P.
Biochim. Biophys. Acta 69:115-129(1963) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10.
[2]"Determination of the amino acid sequence of porcine trypsin by sequenator analysis."
Hermodson M.A., Ericsson L.H., Neurath H., Walsh K.A.
Biochemistry 12:3146-3153(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 9-231.
[3]"Refined 1.6-A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex."
Huang Q., Liu S., Tang Y.
J. Mol. Biol. 229:1022-1036(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[4]"Amino acid sequencing of a trypsin inhibitor by refined 1.6 A X-ray crystal structure of its complex with porcine beta-trypsin."
Huang Q., Liu S., Tang Y., Zeng F., Qian R.
FEBS Lett. 297:143-146(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[5]"Refined 1.8-A resolution crystal structure of the porcine epsilon-trypsin."
Huang Q., Wang Z., Li Y., Liu S., Tang Y.
Biochim. Biophys. Acta 1209:77-82(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[6]"The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition."
Stubbs M.T., Morenweiser R., Stuerzebecher J., Bauer M., Bode W., Huber R., Piechottka G.P., Matschiner G., Sommerhoff C.P., Fritz H., Auerswald E.A.
J. Biol. Chem. 272:19931-19937(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH LDTI.
[7]"Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LDTI-tryptase system."
di Marco S., Priestle J.P.
Structure 5:1465-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF COMPLEX WITH LDTI.
[8]"L-isoaspartate 115 of porcine beta-trypsin promotes crystallization of its complex with bdellastasin."
Rester U., Moser M., Huber R., Bode W.
Acta Crystallogr. D 56:581-588(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH BDELLASTASIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRTRPGTR. A90641.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKSX-ray1.80A9-133[»]
B134-231[»]
1AN1X-ray2.03E9-231[»]
1AVWX-ray1.75A9-231[»]
1AVXX-ray1.90A9-231[»]
1C9PX-ray2.80A9-231[»]
1D3Omodel-A9-231[»]
1DF2model-A9-231[»]
1EJAX-ray2.70A9-231[»]
1EPTX-ray1.80A9-51[»]
B52-133[»]
C134-231[»]
1EWUmodel-A9-231[»]
1FMGX-ray1.90A9-231[»]
1FN6X-ray1.80A9-231[»]
1FNIX-ray1.60A9-231[»]
1H9HX-ray1.50E9-231[»]
1H9IX-ray1.90E9-231[»]
1LDTX-ray1.90T9-231[»]
1LT2model-A9-231[»]
1MCTX-ray1.60A9-231[»]
1QQUX-ray1.63A9-231[»]
1S5SX-ray1.40A9-231[»]
1S6FX-ray1.80A9-231[»]
1S6HX-ray1.45A9-231[»]
1S81X-ray1.70A9-231[»]
1S82X-ray1.85A9-231[»]
1S83X-ray1.25A9-231[»]
1S84X-ray1.85A9-231[»]
1S85X-ray2.20A9-231[»]
1TFXX-ray2.60A/B9-231[»]
1TX6X-ray2.20A/B/C/D9-231[»]
1UHBX-ray2.15A9-133[»]
B134-231[»]
P177-185[»]
1V6DX-ray1.90A9-231[»]
1YF4X-ray1.98A9-231[»]
1Z7KX-ray1.90A9-231[»]
2A31X-ray1.25A9-231[»]
2A32X-ray1.50A9-231[»]
3MYWX-ray2.50A/B9-231[»]
4AN7X-ray2.23A1-231[»]
4DOQX-ray2.00A/C/E9-231[»]
ProteinModelPortalP00761.
SMRP00761. Positions 9-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6083N.
IntActP00761. 1 interaction.
MINTMINT-1512991.
STRING9823.ENSSSCP00000017465.

Chemistry

BindingDBP00761.
ChEMBLCHEMBL2366.

Proteomic databases

PaxDbP00761.
PRIDEP00761.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.

Gene expression databases

ArrayExpressP00761.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00761.

Entry information

Entry nameTRYP_PIG
AccessionPrimary (citable) accession number: P00761
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references