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Protein

Trypsin

Gene
N/A
Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei48 – 481Charge relay system
Metal bindingi60 – 601Calcium
Metal bindingi62 – 621Calcium; via carbonyl oxygen
Metal bindingi65 – 651Calcium; via carbonyl oxygen
Metal bindingi70 – 701Calcium
Active sitei92 – 921Charge relay system
Sitei179 – 1791Required for specificityBy similarity
Active sitei185 – 1851Charge relay system

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. digestion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

MEROPSiS01.151.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin (EC:3.4.21.4)
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 88Activation peptide1 PublicationPRO_0000028205
Chaini9 – 231223TrypsinPRO_0000028206Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi15 ↔ 145
Disulfide bondi33 ↔ 49
Disulfide bondi117 ↔ 218
Disulfide bondi124 ↔ 191
Disulfide bondi156 ↔ 170
Disulfide bondi181 ↔ 205

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP00761.
PRIDEiP00761.

Interactioni

Protein-protein interaction databases

DIPiDIP-6083N.
IntActiP00761. 1 interaction.
MINTiMINT-1512991.
STRINGi9823.ENSSSCP00000017465.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 3917Combined sources
Beta strandi42 – 454Combined sources
Helixi47 – 493Combined sources
Beta strandi55 – 595Combined sources
Beta strandi61 – 655Combined sources
Beta strandi71 – 8010Combined sources
Turni86 – 883Combined sources
Beta strandi94 – 1007Combined sources
Beta strandi105 – 1084Combined sources
Beta strandi123 – 1308Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi144 – 1507Combined sources
Helixi153 – 1597Combined sources
Turni161 – 1633Combined sources
Beta strandi168 – 1725Combined sources
Beta strandi174 – 1774Combined sources
Turni182 – 1865Combined sources
Beta strandi188 – 1914Combined sources
Beta strandi194 – 2018Combined sources
Beta strandi203 – 2064Combined sources
Beta strandi212 – 2165Combined sources
Helixi217 – 2193Combined sources
Helixi221 – 23010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00761.
SMRiP00761. Positions 9-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00761.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 229221Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00761-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
FPTDDDDKIV GGYTCAANSI PYQVSLNSGS HFCGGSLINS QWVVSAAHCY
60 70 80 90 100
KSRIQVRLGE HNIDVLEGNE QFINAAKIIT HPNFNGNTLD NDIMLIKLSS
110 120 130 140 150
PATLNSRVAT VSLPRSCAAA GTECLISGWG NTKSSGSSYP SLLQCLKAPV
160 170 180 190 200
LSDSSCKSSY PGQITGNMIC VGFLEGGKDS CQGDSGGPVV CNGQLQGIVS
210 220 230
WGYGCAQKNK PGVYTKVCNY VNWIQQTIAA N
Length:231
Mass (Da):24,409
Last modified:July 21, 1986 - v1
Checksum:iA0A125CF7FC138C2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201I → V.

Sequence databases

PIRiA90641. TRPGTR.

Cross-referencesi

Sequence databases

PIRiA90641. TRPGTR.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00761.
SMRiP00761. Positions 9-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6083N.
IntActiP00761. 1 interaction.
MINTiMINT-1512991.
STRINGi9823.ENSSSCP00000017465.

Chemistry

BindingDBiP00761.
ChEMBLiCHEMBL2366.

Protein family/group databases

MEROPSiS01.151.

Proteomic databases

PaxDbiP00761.
PRIDEiP00761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.

Miscellaneous databases

EvolutionaryTraceiP00761.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. 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.

Entry informationi

Entry nameiTRYP_PIG
AccessioniPrimary (citable) accession number: P00761
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 4, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.