Anionic trypsin-2 precursor - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P00763 (TRY2_RAT)

Last modified June 16, 2009. Version 102. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Anionic trypsin-2
    EC=3.4.21.4
Alternative name(s):
    Anionic trypsin II
    Pretrypsinogen II
    Serine protease 2

Gene names

Name:	Prss2
Synonyms:	Try2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Biological process	Digestion
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from sequence or structural similarity. Source: UniProtKB digestion Ref.2 Traceable author statement. Source: RGD proteolysis Inferred from sequence or structural similarity. Source: UniProtKB response to nutrient Inferred from expression pattern. Source: RGD
Cellular component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from sequence or structural similarity. Source: UniProtKB serine-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P14754	1	EBI-1029166,EBI-1032177	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

Propeptide

16 – 23

Activation peptide

PRO_0000028209

Chain

24 – 246

223

Anionic trypsin-2

PRO_0000028210

Regions

Domain

24 – 244

221

Peptidase S1

Sites

Active site

Charge relay system

Active site

107

Charge relay system

Active site

200

Charge relay system

Metal binding

Calcium

Metal binding

Calcium; via carbonyl oxygen

Metal binding

Calcium; via carbonyl oxygen

Metal binding

Calcium

Site

194

Required for specificity By similarity

Amino acid modifications

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Experimental info

Sequence conflict

N → D Ref.1

Sequence conflict

V → I Ref.1

Secondary structure

246

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00763-1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: A8D3630809AEE606
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FASTA

246

26,228

        10         20         30         40         50         60 
MRALLFLALV GAAVAFPVDD DDKIVGGYTC QENSVPYQVS LNSGYHFCGG SLINDQWVVS 

        70         80         90        100        110        120 
AAHCYKSRIQ VRLGEHNINV LEGNEQFVNA AKIIKHPNFD RKTLNNDIML IKLSSPVKLN 

       130        140        150        160        170        180 
ARVATVALPS SCAPAGTQCL ISGWGNTLSS GVNEPDLLQC LDAPLLPQAD CEASYPGKIT 

       190        200        210        220        230        240 
DNMVCVGFLE GGKDSCQGDS GGPVVCNGEL QGIVSWGYGC ALPDNPGVYT KVCNYVDWIQ 


DTIAAN

« Hide

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References

[1]	"Structure of two related rat pancreatic trypsin genes." Craik C.S., Choo Q.L., Swift G.H., Quinto C., MacDonald R.J., Rutter W.J. J. Biol. Chem. 259:14255-14264(1984) [PubMed: 6094547] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Two similar but nonallelic rat pancreatic trypsinogens. Nucleotide sequences of the cloned cDNAs." MacDonald R.J., Stary S.J., Swift G.H. J. Biol. Chem. 257:9724-9732(1982) [PubMed: 6896710] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 9-246. Strain: Sprague-Dawley. Tissue: Pancreas.
[3]	"The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis." Sprang S., Standing T., Fletterick R.J., Stroud R.M., Finer-Moore J., Xuong N.-H., Hamlin R., Rutter W.J., Craik C.S. Science 237:905-909(1987) [PubMed: 3112942] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[4]	"1.59-A structure of trypsin at 120 K: comparison of low temperature and room temperature structures." Earnest T., Fauman E., Craik C.S., Stroud R. Proteins 10:171-187(1991) [PubMed: 1881877] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS).
[5]	"X-ray structures of a designed binding site in trypsin show metal-dependent geometry." Brinen L.S., Willett W.S., Craik C.S., Fletterick R.J. Biochemistry 35:5999-6009(1996) [PubMed: 8634241] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

V01274 mRNA. Translation: CAA24581.1.
L00131, L00130 Genomic DNA. Translation: AAA98517.1.

IPI

IPI00212769.

PIR

TRRT2. A22657.

RefSeq

NP_036861.1.

UniGene

Rn.1584

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AMH	X-ray	2.50	A/B	24-246	[»]
1ANB	X-ray	2.80	A	24-246	[»]
1ANC	X-ray	2.20	A	24-246	[»]
1AND	X-ray	2.30	A	24-246	[»]
1ANE	X-ray	2.20	A	24-246	[»]
1BRA	X-ray	2.20	A	24-246	[»]
1BRB	X-ray	2.10	E	24-246	[»]
1BRC	X-ray	2.50	E	24-246	[»]
1CO7	X-ray	1.90	E	2-246	[»]
1DPO	X-ray	1.59	A	24-246	[»]
1EZS	X-ray	2.30	C/D	24-246	[»]
1EZU	X-ray	2.40	C/D	24-246	[»]
1F5R	X-ray	1.65	A	26-246	[»]
1F7Z	X-ray	1.55	A	15-246	[»]
1FY8	X-ray	1.70	E	26-246	[»]
1J14	X-ray	2.40	A	24-246	[»]
1J15	X-ray	2.00	A	24-246	[»]
1J16	X-ray	1.60	A	24-246	[»]
1J17	X-ray	2.00	T	24-246	[»]
1K9O	X-ray	2.30	E	24-246	[»]
1QL9	X-ray	2.30	A	24-246	[»]
1SLU	X-ray	1.80	B	24-246	[»]
1SLV	X-ray	2.30	B	24-246	[»]
1SLW	X-ray	2.00	B	24-246	[»]
1SLX	X-ray	2.20	B	24-246	[»]
1TRM	X-ray	2.30	A/B	24-246	[»]
1YKT	X-ray	1.70	A	24-246	[»]
1YLC	X-ray	1.70	A	24-246	[»]
1YLD	X-ray	1.70	A	24-246	[»]
2TRM	X-ray	2.80	A	24-246	[»]
3FP6	X-ray	1.49	E	24-246	[»]
3FP7	X-ray	1.46	E	24-246	[»]
3FP8	X-ray	1.46	E	24-246	[»]
3TGI	X-ray	1.80	E	24-246	[»]
3TGJ	X-ray	2.20	E	15-246	[»]
3TGK	X-ray	1.70	E	26-237	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6112N.

IntAct

P00763. 2 interactions.

Protein family/group databases

MEROPS

S01.119.

PTM databases

PhosphoSite

P00763.

Proteomic databases

PRIDE

P00763.

Genome annotation databases

Ensembl

ENSRNOG00000029326. Rattus norvegicus. [Contig view]

GeneID

25052.

KEGG

rno:25052.

Organism-specific databases

RGD

3418. Prss2.

Phylogenomic databases

HOVERGEN

P00763.

OMA

P00763. PAVINSR.

Enzyme and pathway databases

BRENDA

3.4.21.4. 248.

Gene expression databases

ArrayExpress

P00763.

GermOnline

ENSRNOG00000029326. Rattus norvegicus.

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...

Other Resources

NextBio

605250.

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Entry information

Entry name

TRY2_RAT

Accession

Primary (citable) accession number: P00763

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 15, 1998
Last modified:	June 16, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents