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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)DescriptionActionsGraphical viewLength
Active sitei48Charge relay system1
Metal bindingi60Calcium1
Metal bindingi62Calcium; via carbonyl oxygen1
Metal bindingi65Calcium; via carbonyl oxygen1
Metal bindingi70Calcium1
Active sitei92Charge relay system1
Sitei179Required for specificityBy similarity1
Active sitei185Charge relay system1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.4. 6170.
SABIO-RKP00761.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin (EC:3.4.21.4)
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2366.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000282051 – 8Activation peptide1 Publication8
ChainiPRO_00000282069 – 231TrypsinAdd BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

EPDiP00761.
PaxDbiP00761.
PeptideAtlasiP00761.
PRIDEiP00761.

Expressioni

Gene expression databases

GenevisibleiP00761. SS.

Interactioni

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP00761.

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 39Combined sources17
Beta strandi42 – 45Combined sources4
Helixi47 – 49Combined sources3
Beta strandi55 – 59Combined sources5
Beta strandi61 – 65Combined sources5
Beta strandi71 – 80Combined sources10
Turni86 – 88Combined sources3
Beta strandi94 – 100Combined sources7
Beta strandi105 – 108Combined sources4
Beta strandi123 – 130Combined sources8
Beta strandi134 – 136Combined sources3
Beta strandi144 – 150Combined sources7
Helixi153 – 159Combined sources7
Turni161 – 163Combined sources3
Beta strandi168 – 172Combined sources5
Beta strandi174 – 177Combined sources4
Turni182 – 186Combined sources5
Beta strandi188 – 191Combined sources4
Beta strandi194 – 201Combined sources8
Beta strandi203 – 206Combined sources4
Beta strandi212 – 216Combined sources5
Helixi217 – 219Combined sources3
Helixi221 – 230Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00761.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 229Peptidase S1PROSITE-ProRule annotationAdd BLAST221

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
OrthoDBiEOG091G0DF7.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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)DescriptionActionsGraphical viewLength
Natural varianti20I → V.1

Sequence databases

PIRiA90641. TRPGTR.

Cross-referencesi

Sequence databases

PIRiA90641. TRPGTR.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP00761.
ChEMBLiCHEMBL2366.

Proteomic databases

EPDiP00761.
PaxDbiP00761.
PeptideAtlasiP00761.
PRIDEiP00761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
OrthoDBiEOG091G0DF7.

Enzyme and pathway databases

BRENDAi3.4.21.4. 6170.
SABIO-RKP00761.

Miscellaneous databases

EvolutionaryTraceiP00761.

Gene expression databases

GenevisibleiP00761. SS.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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...

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: November 2, 2016
This is version 135 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

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 one 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.