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Protein

Chymotrypsin-2

Gene

CHYM2

Organism
Anopheles gambiae (African malaria mosquito)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei74 – 741Charge relay systemBy similarity
Active sitei119 – 1191Charge relay systemBy similarity
Sitei206 – 2061Required for specificityBy similarity
Active sitei212 – 2121Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Protein family/group databases

MEROPSiS01.166.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsin-2 (EC:3.4.21.1)
Alternative name(s):
AnChym2
Gene namesi
Name:CHYM2
ORF Names:AGAP006711
OrganismiAnopheles gambiae (African malaria mosquito)
Taxonomic identifieri7165 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
ProteomesiUP000007062 Componenti: Chromosome 2L

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 3215Activation peptideSequence AnalysisPRO_0000027656Add
BLAST
Chaini33 – 258226Chymotrypsin-2PRO_0000027657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi59 ↔ 75PROSITE-ProRule annotation
Disulfide bondi182 ↔ 198PROSITE-ProRule annotation
Disulfide bondi208 ↔ 232PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Expressioni

Tissue specificityi

After blood feeding, expression is induced in the midgut epithelium, followed by secretion into the midgut lumen.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ17025.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 255223Peptidase 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.
HOGENOMiHOG000251820.
InParanoidiQ17025.
OMAiKGYGHIC.
OrthoDBiEOG7MKW6Q.
PhylomeDBiQ17025.

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.

Q17025-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRKVFAVVS VLLVVSAAKV TKLVLDDHYV NRVVGGEVAK NGSAPYQVSL
60 70 80 90 100
QVPGWGHNCG GSLLNNRWVL TAAHCLVGYE PSDLMVLVGT NSLKEGGELL
110 120 130 140 150
KVDKLLYHSR YNRPQFHNDI GLMRLEQPVQ FSELVQSVEY LEKAVPVNAT
160 170 180 190 200
VRLTGWGRTS TNGNVPTLLQ SLNVVTLSNE DCKAKMGNPK NVDLGHVCTL
210 220 230 240 250
TKAGEGACNG DSGGPLVYEG KLVGVVNFGV PCGRGFPDGF ARVSYYHEWV

RTTMANNS
Length:258
Mass (Da):27,928
Last modified:May 16, 2006 - v3
Checksum:i8C82E91B5C790EB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211T → P in CAA79326 (PubMed:11453997).Curated
Sequence conflicti21 – 211T → P in CAA83567 (PubMed:11453997).Curated
Sequence conflicti28 – 281H → N in CAA79326 (PubMed:11453997).Curated
Sequence conflicti28 – 281H → N in CAA83567 (PubMed:11453997).Curated
Sequence conflicti37 – 371E → V in CAA79326 (PubMed:11453997).Curated
Sequence conflicti37 – 371E → V in CAA83567 (PubMed:11453997).Curated
Sequence conflicti42 – 421G → C in CAA79326 (PubMed:11453997).Curated
Sequence conflicti42 – 421G → C in CAA83567 (PubMed:11453997).Curated
Sequence conflicti66 – 661N → D in CAA79326 (PubMed:11453997).Curated
Sequence conflicti66 – 661N → D in CAA83567 (PubMed:11453997).Curated
Sequence conflicti166 – 1661P → R in CAA79326 (PubMed:11453997).Curated
Sequence conflicti190 – 1901K → E in CAA79326 (PubMed:11453997).Curated
Sequence conflicti190 – 1901K → E in CAA83567 (PubMed:11453997).Curated
Sequence conflicti194 – 1963LGH → FPD in CAA79326 (PubMed:11453997).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18888 mRNA. Translation: CAA79326.1.
Z32645 Genomic DNA. Translation: CAA83567.1.
AAAB01008807 Genomic DNA. Translation: EAA04684.3.
PIRiS44184.
RefSeqiXP_309032.2. XM_309032.3.

Genome annotation databases

EnsemblMetazoaiAGAP006711-RA; AGAP006711-PA; AGAP006711.
GeneIDi1270347.
KEGGiaga:AgaP_AGAP006711.
VectorBaseiAGAP006711. Anopheles gambiae.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18888 mRNA. Translation: CAA79326.1.
Z32645 Genomic DNA. Translation: CAA83567.1.
AAAB01008807 Genomic DNA. Translation: EAA04684.3.
PIRiS44184.
RefSeqiXP_309032.2. XM_309032.3.

3D structure databases

ProteinModelPortaliQ17025.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiAGAP006711-RA; AGAP006711-PA; AGAP006711.
GeneIDi1270347.
KEGGiaga:AgaP_AGAP006711.
VectorBaseiAGAP006711. Anopheles gambiae.

Organism-specific databases

CTDi1270347.

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
InParanoidiQ17025.
OMAiKGYGHIC.
OrthoDBiEOG7MKW6Q.
PhylomeDBiQ17025.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCTR2_ANOGA
AccessioniPrimary (citable) accession number: Q17025
Secondary accession number(s): Q17026, Q7PT16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 16, 2006
Last modified: January 7, 2015
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.