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P00763

- TRY2_RAT

UniProt

P00763 - TRY2_RAT

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Protein

Anionic trypsin-2

Gene

Prss2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 Ca(2+) ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Charge relay system
Metal bindingi75 – 751Calcium
Metal bindingi77 – 771Calcium; via carbonyl oxygen
Metal bindingi80 – 801Calcium; via carbonyl oxygen
Metal bindingi85 – 851Calcium
Active sitei107 – 1071Charge relay system
Sitei194 – 1941Required for specificityBy similarity
Active sitei200 – 2001Charge relay system

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. collagen catabolic process Source: UniProtKB
  2. digestion Source: RGD
  3. proteolysis Source: UniProtKB
  4. 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

ReactomeiREACT_198590. Activation of Matrix Metalloproteinases.
REACT_199179. Alpha-defensins.
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
ProteomesiUP000002494: Chromosome 4

Organism-specific databases

RGDi3418. Prss2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Add
BLAST
Propeptidei16 – 238Activation peptidePRO_0000028209
Chaini24 – 246223Anionic trypsin-2PRO_0000028210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

PhosphoSiteiP00763.

Expressioni

Gene expression databases

GenevestigatoriP00763.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

DIPiDIP-6112N.
IntActiP00763. 2 interactions.
MINTiMINT-202469.
STRINGi10116.ENSRNOP00000062302.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni32 – 343Combined sources
Beta strandi38 – 5417Combined sources
Beta strandi57 – 604Combined sources
Helixi62 – 643Combined sources
Beta strandi70 – 745Combined sources
Beta strandi76 – 805Combined sources
Beta strandi86 – 9510Combined sources
Turni101 – 1033Combined sources
Beta strandi109 – 1157Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi138 – 1458Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi159 – 1657Combined sources
Helixi168 – 1747Combined sources
Turni176 – 1783Combined sources
Beta strandi183 – 1875Combined sources
Beta strandi192 – 1943Combined sources
Turni197 – 2015Combined sources
Beta strandi203 – 2064Combined sources
Beta strandi209 – 2168Combined sources
Beta strandi218 – 2214Combined sources
Beta strandi227 – 2315Combined sources
Helixi232 – 2343Combined sources
Helixi236 – 24510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 24-246.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00763.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 244221Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP00763.
KOiK01312.
OMAiGHCYKSA.
OrthoDBiEOG75B84T.
PhylomeDBiP00763.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841N → D(PubMed:6094547)Curated
Sequence conflicti88 – 881V → I(PubMed:6094547)Curated

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_012729.1.
UniGeneiRn.1584.

Genome annotation databases

EnsembliENSRNOT00000018852; ENSRNOP00000018853; ENSRNOG00000032916.
ENSRNOT00000066789; ENSRNOP00000060784; ENSRNOG00000049576.
GeneIDi25052.
KEGGirno:100912089.
rno: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 .
PIRi A22657. TRRT2.
RefSeqi NP_036861.1. NM_012729.1.
UniGenei Rn.1584.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 15-246 [» ]
1F7Z X-ray 1.55 A 15-246 [» ]
1FY8 X-ray 1.70 E 15-246 [» ]
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 24-239 [» ]
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 15-237 [» ]
ProteinModelPortali P00763.
SMRi P00763. Positions 24-246.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6112N.
IntActi P00763. 2 interactions.
MINTi MINT-202469.
STRINGi 10116.ENSRNOP00000062302.

Chemistry

BindingDBi P00763.
ChEMBLi CHEMBL4290.

Protein family/group databases

MEROPSi S01.119.

PTM databases

PhosphoSitei P00763.

Proteomic databases

PaxDbi P00763.
PRIDEi P00763.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000018852 ; ENSRNOP00000018853 ; ENSRNOG00000032916 .
ENSRNOT00000066789 ; ENSRNOP00000060784 ; ENSRNOG00000049576 .
GeneIDi 25052.
KEGGi rno:100912089.
rno:25052.
UCSCi RGD:3418. rat.

Organism-specific databases

CTDi 5645.
RGDi 3418. Prss2.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118862.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P00763.
KOi K01312.
OMAi GHCYKSA.
OrthoDBi EOG75B84T.
PhylomeDBi P00763.

Enzyme and pathway databases

Reactomei REACT_198590. Activation of Matrix Metalloproteinases.
REACT_199179. Alpha-defensins.
SABIO-RK P00763.

Miscellaneous databases

EvolutionaryTracei P00763.
NextBioi 605250.

Gene expression databases

Genevestigatori P00763.

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. "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).

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 26, 2014
This is version 149 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

External Data

Dasty 3