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Protein

Anionic trypsin-2

Gene

Prss2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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 sitei63Charge relay system1
Metal bindingi75Calcium1
Metal bindingi77Calcium; via carbonyl oxygen1
Metal bindingi80Calcium; via carbonyl oxygen1
Metal bindingi85Calcium1
Active sitei107Charge relay system1
Sitei194Required for specificityBy similarity1
Active sitei200Charge relay system1

GO - Molecular functioni

GO - Biological processi

  • collagen catabolic process Source: UniProtKB
  • digestion Source: RGD
  • proteolysis Source: UniProtKB
  • response to nutrient Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-1442490. Collagen degradation.
R-RNO-1462054. Alpha-defensins.
R-RNO-1592389. Activation of Matrix Metalloproteinases.
R-RNO-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
R-RNO-6798695. Neutrophil degranulation.
R-RNO-6803157. Antimicrobial peptides.
SABIO-RKP00763.

Protein family/group databases

MEROPSiS01.119.

Names & Taxonomyi

Protein namesi
Recommended name:
Anionic trypsin-2 (EC:3.4.21.4)
Alternative name(s):
Anionic trypsin II
Pretrypsinogen II
Serine protease 2
Gene namesi
Name:Prss2
Synonyms:Try2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi3418. Prss2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4290.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 15Add BLAST15
PropeptideiPRO_000002820916 – 23Activation peptide8
ChainiPRO_000002821024 – 246Anionic trypsin-2Add BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 160
Disulfide bondi48 ↔ 64
Disulfide bondi132 ↔ 233
Disulfide bondi139 ↔ 206
Disulfide bondi171 ↔ 185
Disulfide bondi196 ↔ 220

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP00763.
PRIDEiP00763.

PTM databases

iPTMnetiP00763.
PhosphoSitePlusiP00763.

Expressioni

Gene expression databases

GenevisibleiP00763. RN.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ecoP238272EBI-1029166,EBI-1029159From a different organism.

Protein-protein interaction databases

DIPiDIP-6112N.
IntActiP00763. 2 interactors.
MINTiMINT-202469.
STRINGi10116.ENSRNOP00000060784.

Chemistry databases

BindingDBiP00763.

Structurei

Secondary structure

1246
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni32 – 34Combined sources3
Beta strandi38 – 54Combined sources17
Beta strandi57 – 60Combined sources4
Helixi62 – 64Combined sources3
Beta strandi70 – 74Combined sources5
Beta strandi76 – 80Combined sources5
Beta strandi86 – 95Combined sources10
Turni101 – 103Combined sources3
Beta strandi109 – 115Combined sources7
Beta strandi120 – 123Combined sources4
Beta strandi138 – 145Combined sources8
Beta strandi149 – 151Combined sources3
Beta strandi159 – 165Combined sources7
Helixi168 – 174Combined sources7
Turni176 – 178Combined sources3
Beta strandi183 – 187Combined sources5
Beta strandi192 – 194Combined sources3
Turni197 – 201Combined sources5
Beta strandi203 – 206Combined sources4
Beta strandi209 – 216Combined sources8
Beta strandi218 – 221Combined sources4
Beta strandi227 – 231Combined sources5
Helixi232 – 234Combined sources3
Helixi236 – 245Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP00763.
SMRiP00763.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00763.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 244Peptidase S1PROSITE-ProRule annotationAdd BLAST221

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP00763.
KOiK01312.
OMAiWIQATID.
OrthoDBiEOG091G0DF7.
PhylomeDBiP00763.

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.

P00763-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALLFLALV GAAVAFPVDD DDKIVGGYTC QENSVPYQVS LNSGYHFCGG
60 70 80 90 100
SLINDQWVVS AAHCYKSRIQ VRLGEHNINV LEGNEQFVNA AKIIKHPNFD
110 120 130 140 150
RKTLNNDIML IKLSSPVKLN ARVATVALPS SCAPAGTQCL ISGWGNTLSS
160 170 180 190 200
GVNEPDLLQC LDAPLLPQAD CEASYPGKIT DNMVCVGFLE GGKDSCQGDS
210 220 230 240
GGPVVCNGEL QGIVSWGYGC ALPDNPGVYT KVCNYVDWIQ DTIAAN
Length:246
Mass (Da):26,228
Last modified:July 15, 1998 - v2
Checksum:iA8D3630809AEE606
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti84N → D (PubMed:6094547).Curated1
Sequence conflicti88V → I (PubMed:6094547).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01274 mRNA. Translation: CAA24581.1.
L00131, L00130 Genomic DNA. Translation: AAA98517.1.
PIRiA22657. TRRT2.
RefSeqiNP_036861.1. NM_012729.2.
UniGeneiRn.1584.

Genome annotation databases

EnsembliENSRNOT00000018852; ENSRNOP00000018853; ENSRNOG00000032916.
GeneIDi25052.
KEGGirno:25052.
UCSCiRGD:3418. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01274 mRNA. Translation: CAA24581.1.
L00131, L00130 Genomic DNA. Translation: AAA98517.1.
PIRiA22657. TRRT2.
RefSeqiNP_036861.1. NM_012729.2.
UniGeneiRn.1584.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP00763.
SMRiP00763.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6112N.
IntActiP00763. 2 interactors.
MINTiMINT-202469.
STRINGi10116.ENSRNOP00000060784.

Chemistry databases

BindingDBiP00763.
ChEMBLiCHEMBL4290.

Protein family/group databases

MEROPSiS01.119.

PTM databases

iPTMnetiP00763.
PhosphoSitePlusiP00763.

Proteomic databases

PaxDbiP00763.
PRIDEiP00763.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018852; ENSRNOP00000018853; ENSRNOG00000032916.
GeneIDi25052.
KEGGirno:25052.
UCSCiRGD:3418. rat.

Organism-specific databases

CTDi5645.
RGDi3418. Prss2.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP00763.
KOiK01312.
OMAiWIQATID.
OrthoDBiEOG091G0DF7.
PhylomeDBiP00763.

Enzyme and pathway databases

ReactomeiR-RNO-1442490. Collagen degradation.
R-RNO-1462054. Alpha-defensins.
R-RNO-1592389. Activation of Matrix Metalloproteinases.
R-RNO-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
R-RNO-6798695. Neutrophil degranulation.
R-RNO-6803157. Antimicrobial peptides.
SABIO-RKP00763.

Miscellaneous databases

EvolutionaryTraceiP00763.
PROiP00763.

Gene expression databases

GenevisibleiP00763. RN.

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 nameiTRY2_RAT
AccessioniPrimary (citable) accession number: P00763
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1998
Last modified: November 30, 2016
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.