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O97398 (CTR_PHACE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Serine protease with chymotryptic and collagenolytic activities By similarity. UniProtKB Q00871

Catalytic activity

Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa. UniProtKB Q00871

Subcellular location

Secretedextracellular space By similarity UniProtKB Q00871.

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 processCollagen degradation
Digestion
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological_processcollagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

digestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

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 – 4529Activation peptide By similarity UniProtKB Q00871
PRO_0000314680
Chain46 – 276231Chymotrypsin
PRO_5000147324

Regions

Domain46 – 272227Peptidase S1

Sites

Active site891Charge relay system By similarity UniProtKB P00771
Active site1351Charge relay system By similarity UniProtKB P00771
Active site2291Charge relay system By similarity UniProtKB P00771

Amino acid modifications

Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Disulfide bond74 ↔ 90 By similarity UniProtKB P00771
Disulfide bond202 ↔ 215 By similarity UniProtKB P00771
Disulfide bond225 ↔ 250 By similarity UniProtKB P00771

Sequences

Sequence LengthMass (Da)Tools
O97398 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: FC5FD05DB882A1DE

FASTA27629,868
        10         20         30         40         50         60 
MKVALVVLAL FGVSLAASID NIEIPPSKNI YVEPINQPEV DPSLEIVNGQ EVVPHSIPYQ 

        70         80         90        100        110        120 
IFLVASAGET SWTCGGSLIT KRYVLTAAHC IQGAKSVHVT LGAHNLAKHE ASKVTVNGRS 

       130        140        150        160        170        180 
WVIHEKYDST NIDNDIGVIQ LERNLTLTRS IQLARLPSLR DVGINLEGRT ATVSGWGLTN 

       190        200        210        220        230        240 
GIFQTTTDVL RANNTIISNK ECNDVFKIVQ PTEVCLSIAG GRSACSGDSG GPLVIDNVQH 

       250        260        270 
GIVSYGSSYC RSTPSVFTRV SSYLNWLQTH SEWRAQ 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Larval gut.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y17904 mRNA. Translation: CAA76928.1.

3D structure databases

ProteinModelPortalO97398.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.082.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameCTR_PHACE
AccessionPrimary (citable) accession number: O97398
Secondary accession number(s): P81521
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 1999
Last modified: October 16, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries