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P00761

- TRYP_PIG

UniProt

P00761 - TRYP_PIG

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Protein

Trypsin

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

Functioni

Catalytic activityi

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

Cofactori

Binds 1 calcium 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

MEROPSiS01.120.

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 region Source: UniProtKB-KW
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 – 3917
Beta strandi42 – 454
Helixi47 – 493
Beta strandi55 – 595
Beta strandi61 – 655
Beta strandi71 – 8010
Turni86 – 883
Beta strandi94 – 1007
Beta strandi105 – 1084
Beta strandi123 – 1308
Beta strandi134 – 1363
Beta strandi144 – 1507
Helixi153 – 1597
Turni161 – 1633
Beta strandi168 – 1725
Beta strandi174 – 1774
Turni182 – 1865
Beta strandi188 – 1914
Beta strandi194 – 2018
Beta strandi203 – 2064
Beta strandi212 – 2165
Helixi217 – 2193
Helixi221 – 23010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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

PIRi A90641. TRPGTR.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AKS X-ray 1.80 A 9-133 [» ]
B 134-231 [» ]
1AN1 X-ray 2.03 E 9-231 [» ]
1AVW X-ray 1.75 A 9-231 [» ]
1AVX X-ray 1.90 A 9-231 [» ]
1C9P X-ray 2.80 A 9-231 [» ]
1D3O model - A 9-231 [» ]
1DF2 model - A 9-231 [» ]
1EJA X-ray 2.70 A 9-231 [» ]
1EPT X-ray 1.80 A 9-51 [» ]
B 52-133 [» ]
C 134-231 [» ]
1EWU model - A 9-231 [» ]
1FMG X-ray 1.90 A 9-231 [» ]
1FN6 X-ray 1.80 A 9-231 [» ]
1FNI X-ray 1.60 A 9-231 [» ]
1H9H X-ray 1.50 E 9-231 [» ]
1H9I X-ray 1.90 E 9-231 [» ]
1LDT X-ray 1.90 T 9-231 [» ]
1LT2 model - A 9-231 [» ]
1MCT X-ray 1.60 A 9-231 [» ]
1QQU X-ray 1.63 A 9-231 [» ]
1S5S X-ray 1.40 A 9-231 [» ]
1S6F X-ray 1.80 A 9-231 [» ]
1S6H X-ray 1.45 A 9-231 [» ]
1S81 X-ray 1.70 A 9-231 [» ]
1S82 X-ray 1.85 A 9-231 [» ]
1S83 X-ray 1.25 A 9-231 [» ]
1S84 X-ray 1.85 A 9-231 [» ]
1S85 X-ray 2.20 A 9-231 [» ]
1TFX X-ray 2.60 A/B 9-231 [» ]
1TX6 X-ray 2.20 A/B/C/D 9-231 [» ]
1UHB X-ray 2.15 A 9-133 [» ]
B 134-231 [» ]
P 177-185 [» ]
1V6D X-ray 1.90 A 9-231 [» ]
1YF4 X-ray 1.98 A 9-231 [» ]
1Z7K X-ray 1.90 A 9-231 [» ]
2A31 X-ray 1.25 A 9-231 [» ]
2A32 X-ray 1.50 A 9-231 [» ]
3MYW X-ray 2.50 A/B 9-231 [» ]
4AN7 X-ray 2.23 A 1-231 [» ]
4DOQ X-ray 2.00 A/C/E 9-231 [» ]
ProteinModelPortali P00761.
SMRi P00761. Positions 9-231.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6083N.
IntActi P00761. 1 interaction.
MINTi MINT-1512991.
STRINGi 9823.ENSSSCP00000017465.

Chemistry

BindingDBi P00761.
ChEMBLi CHEMBL2366.

Protein family/group databases

MEROPSi S01.120.

Proteomic databases

PaxDbi P00761.
PRIDEi P00761.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.

Miscellaneous databases

EvolutionaryTracei P00761.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 120 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