Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00763 (TRY2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ecoP238272EBI-1029166,EBI-1029159From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515
Propeptide16 – 238Activation peptide
PRO_0000028209
Chain24 – 246223Anionic trypsin-2
PRO_0000028210

Regions

Domain24 – 244221Peptidase S1

Sites

Active site631Charge relay system
Active site1071Charge relay system
Active site2001Charge relay system
Metal binding751Calcium
Metal binding771Calcium; via carbonyl oxygen
Metal binding801Calcium; via carbonyl oxygen
Metal binding851Calcium
Site1941Required for specificity By similarity

Amino acid modifications

Disulfide bond30 ↔ 160
Disulfide bond48 ↔ 64
Disulfide bond132 ↔ 233
Disulfide bond139 ↔ 206
Disulfide bond171 ↔ 185
Disulfide bond196 ↔ 220

Experimental info

Sequence conflict841N → D Ref.1
Sequence conflict881V → I Ref.1

Secondary structure

................................................ 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00763 [UniParc].

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

FASTA24626,228
        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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01274 mRNA. Translation: CAA24581.1.
L00131, L00130 Genomic DNA. Translation: AAA98517.1.
PIRTRRT2. A22657.
RefSeqNP_036861.1. NM_012729.1.
XP_003749781.1. XM_003749733.1.
UniGeneRn.1584.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AMHX-ray2.50A/B24-246[»]
1ANBX-ray2.80A24-246[»]
1ANCX-ray2.20A24-246[»]
1ANDX-ray2.30A24-246[»]
1ANEX-ray2.20A24-246[»]
1BRAX-ray2.20A24-246[»]
1BRBX-ray2.10E24-246[»]
1BRCX-ray2.50E24-246[»]
1CO7X-ray1.90E2-246[»]
1DPOX-ray1.59A24-246[»]
1EZSX-ray2.30C/D24-246[»]
1EZUX-ray2.40C/D24-246[»]
1F5RX-ray1.65A15-246[»]
1F7ZX-ray1.55A15-246[»]
1FY8X-ray1.70E15-246[»]
1J14X-ray2.40A24-246[»]
1J15X-ray2.00A24-246[»]
1J16X-ray1.60A24-246[»]
1J17X-ray2.00T24-246[»]
1K9OX-ray2.30E24-246[»]
1QL9X-ray2.30A24-246[»]
1SLUX-ray1.80B24-246[»]
1SLVX-ray2.30B24-246[»]
1SLWX-ray2.00B24-246[»]
1SLXX-ray2.20B24-246[»]
1TRMX-ray2.30A/B24-246[»]
1YKTX-ray1.70A24-246[»]
1YLCX-ray1.70A24-246[»]
1YLDX-ray1.70A24-239[»]
2TRMX-ray2.80A24-246[»]
3FP6X-ray1.49E24-246[»]
3FP7X-ray1.46E24-246[»]
3FP8X-ray1.46E24-246[»]
3TGIX-ray1.80E24-246[»]
3TGJX-ray2.20E15-246[»]
3TGKX-ray1.70E15-237[»]
ProteinModelPortalP00763.
SMRP00763. Positions 24-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6112N.
IntActP00763. 2 interactions.
MINTMINT-202469.
STRING10116.ENSRNOP00000062302.

Chemistry

BindingDBP00763.
ChEMBLCHEMBL4290.

Protein family/group databases

MEROPSS01.119.

PTM databases

PhosphoSiteP00763.

Proteomic databases

PaxDbP00763.
PRIDEP00763.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000018852; ENSRNOP00000018853; ENSRNOG00000032916.
ENSRNOT00000066789; ENSRNOP00000060784; ENSRNOG00000049576.
GeneID100912089.
25052.
KEGGrno:100912089.
rno:25052.
UCSCRGD:3418. rat.

Organism-specific databases

CTD5645.
RGD3418. Prss2.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00740000115192.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP00763.
KOK01312.
OMAGHCYKSA.
OrthoDBEOG75B84T.
PhylomeDBP00763.

Enzyme and pathway databases

SABIO-RKP00763.

Gene expression databases

GenevestigatorP00763.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00763.
NextBio605250.

Entry information

Entry nameTRY2_RAT
AccessionPrimary (citable) accession number: P00763
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references