Reviewed, UniProtKB/Swiss-Prot P00761 (TRYP_PIG)

Names and origin

Protein names	Recommended name:     Trypsin     EC=3.4.21.4
Organism	Sus scrofa (Pig)
Taxonomic identifier	9823 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Cofactor	Binds 1 calcium ion per subunit.
Subcellular location	Secreted › extracellular space.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Digestion
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	digestion Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 8

8

Activation peptide Ref.2

PRO_0000028205

Chain

9 – 231

223

Trypsin

PRO_0000028206

Regions

Domain

9 – 229

221

Peptidase S1

Sites

Active site

48

1

Charge relay system

Active site

92

1

Charge relay system

Active site

185

1

Charge relay system

Metal binding

60

1

Calcium

Metal binding

62

1

Calcium; via carbonyl oxygen

Metal binding

65

1

Calcium; via carbonyl oxygen

Metal binding

70

1

Calcium

Site

179

1

Required for specificity By similarity

Amino acid modifications

Disulfide bond

15 ↔ 145

Disulfide bond

33 ↔ 49

Disulfide bond

117 ↔ 218

Disulfide bond

124 ↔ 191

Disulfide bond

156 ↔ 170

Disulfide bond

181 ↔ 205

Natural variations

Natural variant

20

1

I → V

Secondary structure

1

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231

Helix Strand Turn

Details...

Beta strand

23 – 39

17

Beta strand

42 – 45

4

Helix

47 – 49

3

Beta strand

55 – 59

5

Beta strand

71 – 80

10

Turn

86 – 88

3

Beta strand

94 – 100

7

Beta strand

105 – 107

3

Beta strand

123 – 130

8

Beta strand

134 – 136

3

Beta strand

144 – 150

7

Helix

153 – 159

7

Turn

161 – 163

3

Beta strand

168 – 172

5

Beta strand

188 – 191

4

Beta strand

194 – 201

8

Beta strand

203 – 206

4

Beta strand

212 – 216

5

Helix

217 – 220

4

Helix

221 – 229

9

Sequences

	Sequence		Length	Mass (Da)
	P00761-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: A0A125CF7FC138C2	FASTA	231	24,409
	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

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: 14020231] [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: 4738933] [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: 8445634] [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: 1551419] [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: 7947985] [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: 9242660] [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: 9384562] [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: 10771427] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH BDELLASTASIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

TRPGTR. A90641.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6083N.

Protein family/group databases

MEROPS

S01.151.

Proteomic databases

PRIDE

P00761.

Phylogenomic databases

HOVERGEN

P00761.

Enzyme and pathway databases

BRENDA

3.4.21.4. 249.

Family and domain databases

InterPro

IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TRYP_PIG

Accession

Primary (citable) accession number: P00761

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)