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Q17025 (CTR2_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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 namesRecommended name:
Chymotrypsin-2

EC=3.4.21.1
Alternative name(s):
AnChym2
Gene names
Name:CHYM2
ORF Names:AGAP006711
OrganismAnopheles gambiae (African malaria mosquito) [Reference proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

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: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.

Subcellular location

Secreted Ref.1.

Tissue specificity

After blood feeding, expression is induced in the midgut epithelium, followed by secretion into the midgut lumen. 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
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 1717 Potential
Propeptide18 – 3215Activation peptide Potential
PRO_0000027656
Chain33 – 258226Chymotrypsin-2
PRO_0000027657

Regions

Domain33 – 255223Peptidase S1

Sites

Active site741Charge relay system By similarity
Active site1191Charge relay system By similarity
Active site2121Charge relay system By similarity
Site2061Required for specificity By similarity

Amino acid modifications

Disulfide bond59 ↔ 75 By similarity
Disulfide bond182 ↔ 198 By similarity
Disulfide bond208 ↔ 232 By similarity

Experimental info

Sequence conflict211T → P in CAA79326. Ref.1
Sequence conflict211T → P in CAA83567. Ref.1
Sequence conflict281H → N in CAA79326. Ref.1
Sequence conflict281H → N in CAA83567. Ref.1
Sequence conflict371E → V in CAA79326. Ref.1
Sequence conflict371E → V in CAA83567. Ref.1
Sequence conflict421G → C in CAA79326. Ref.1
Sequence conflict421G → C in CAA83567. Ref.1
Sequence conflict661N → D in CAA79326. Ref.1
Sequence conflict661N → D in CAA83567. Ref.1
Sequence conflict1661P → R in CAA79326. Ref.1
Sequence conflict1901K → E in CAA79326. Ref.1
Sequence conflict1901K → E in CAA83567. Ref.1
Sequence conflict194 – 1963LGH → FPD in CAA79326. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q17025 [UniParc].

Last modified May 16, 2006. Version 3.
Checksum: 8C82E91B5C790EB8

FASTA25827,928
        10         20         30         40         50         60 
MLRKVFAVVS VLLVVSAAKV TKLVLDDHYV NRVVGGEVAK NGSAPYQVSL QVPGWGHNCG 

        70         80         90        100        110        120 
GSLLNNRWVL TAAHCLVGYE PSDLMVLVGT NSLKEGGELL KVDKLLYHSR YNRPQFHNDI 

       130        140        150        160        170        180 
GLMRLEQPVQ FSELVQSVEY LEKAVPVNAT VRLTGWGRTS TNGNVPTLLQ SLNVVTLSNE 

       190        200        210        220        230        240 
DCKAKMGNPK NVDLGHVCTL TKAGEGACNG DSGGPLVYEG KLVGVVNFGV PCGRGFPDGF 

       250 
ARVSYYHEWV RTTMANNS 

« Hide

References

« Hide 'large scale' references
[1]"Blood digestion in the malaria mosquito Anopheles gambiae: molecular cloning and biochemical characterization of two inducible chymotrypsins."
Vizioli J., Catteruccia F., della Torre A., Reckmann I., Mueller H.M.
Eur. J. Biochem. 268:4027-4035(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: Suakoko.
Tissue: Midgut.
[2]"The genome sequence of the malaria mosquito Anopheles gambiae."
Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. expand/collapse author list , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.
Science 298:129-149(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PEST.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z18888 mRNA. Translation: CAA79326.1.
Z32645 Genomic DNA. Translation: CAA83567.1.
AAAB01008807 Genomic DNA. Translation: EAA04684.3.
PIRS44184.

3D structure databases

ProteinModelPortalQ17025.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.166.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAGAP006711-RA; AGAP006711-PA; AGAP006711.
KEGGaga:AgaP_AGAP006711.
VectorBaseAGAP006711. Anopheles gambiae.

Organism-specific databases

CTD1270347.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
InParanoidQ17025.
OMAKGYGHIC.
OrthoDBEOG7MKW6Q.
PhylomeDBQ17025.

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 nameCTR2_ANOGA
AccessionPrimary (citable) accession number: Q17025
Secondary accession number(s): Q17026, Q7PT16
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 94 of the entry and version 3 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