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Reviewed, UniProtKB/Swiss-Prot O97399 (TRYP_PHACE)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Trypsin
    EC=3.4.21.4
OrganismPhaedon cochleariae (Mustard beetle)
Taxonomic identifier80249 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaCucujiformiaChrysomeloideaChrysomelidaeChrysomelinaeChrysomeliniPhaedon

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. UniProtKB P35049

Subcellular location

Secreted By similarity. UniProtKB P35049

Tissue specificity

Expressed in larval carcasses and gut, and adult gut. Ref.1

Developmental stage

Ovarial and mature eggs, larvae and adult. Ref.1

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 3014Activation peptide By similarity UniProtKB P35049
PRO_0000314681
Chain30 – 258229Trypsin UniProtKB P35049
PRO_5000147327

Regions

Domain30 – 257228Peptidase S1

Sites

Active site701Charge relay system By similarity UniProtKB P35049
Active site1171Charge relay system By similarity UniProtKB P35049
Active site2131Charge relay system By similarity UniProtKB P35049
Site2071Required for specificity By similarity UniProtKB P35049

Amino acid modifications

Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Disulfide bond55 ↔ 71 By similarity UniProtKB P35049
Disulfide bond182 ↔ 197 By similarity UniProtKB P35049
Disulfide bond209 ↔ 233 By similarity UniProtKB P35049

Sequences

Sequence LengthMass (Da)Tools
O97399-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: BDBDFAFECB86866C

FASTA25828,071
        10         20         30         40         50         60 
MIRFTLALAV IGVTFAASTP QIETNPNLEI IGGHDANIID YPWQISFQHR LHHFCGGFLI 

        70         80         90        100        110        120 
SDTWVVTAAH CIYEGYSDTE NLNIRVGSSE WSAKGKLHDV KRYITHPQYN ITTMDNDIAL 

       130        140        150        160        170        180 
LELALPVDLN QSVRPAKLPV AGQEIPDNAQ LTITGWGATY VGGYNEYTLQ VVTIPTVNIN 

       190        200        210        220        230        240 
VCQSAITNDT ITNNMFCAGL IGVGGKDSCS GDSGGPAVID GQVVGIVSWG YSCADPKYPG 

       250 
IYTKVSAFRD WINEETEI 

« Hide

References

[1]"Molecular cloning of cDNAs encoding a range of digestive enzymes from a phytophagous beetle, Phaedon cochleariae."
Girard C., Jouanin L.
Insect Biochem. Mol. Biol. 29:1129-1142(1999) [PubMed: 10612046] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Larval gut.

Cross-references

Sequence databases

Y17905 mRNA. Translation: CAA76929.1.

3D structure databases

HSSPHSSP built from PDB template 1EZX based on UniProtKB P00760.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.4.21.4. 290922.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRYP_PHACE
AccessionPrimary (citable) accession number: O97399
Secondary accession number(s): P81524
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents