CTR2_ANOGA
ID CTR2_ANOGA Reviewed; 258 AA.
AC Q17025; Q17026; Q7PT16;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Chymotrypsin-2;
DE EC=3.4.21.1;
DE AltName: Full=AnChym2;
DE Flags: Precursor;
GN Name=CHYM2; ORFNames=AGAP006711;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Suakoko; TISSUE=Midgut;
RX PubMed=11453997; DOI=10.1046/j.1432-1327.2001.02315.x;
RA Vizioli J., Catteruccia F., della Torre A., Reckmann I., Mueller H.M.;
RT "Blood digestion in the malaria mosquito Anopheles gambiae: molecular
RT cloning and biochemical characterization of two inducible chymotrypsins.";
RL Eur. J. Biochem. 268:4027-4035(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-
CC Xaa.; EC=3.4.21.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10078,
CC ECO:0000255|PROSITE-ProRule:PRU10079};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11453997}.
CC -!- TISSUE SPECIFICITY: After blood feeding, expression is induced in the
CC midgut epithelium, followed by secretion into the midgut lumen.
CC {ECO:0000269|PubMed:11453997}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; Z18888; CAA79326.1; -; mRNA.
DR EMBL; Z32645; CAA83567.1; -; Genomic_DNA.
DR EMBL; AAAB01008807; EAA04684.3; -; Genomic_DNA.
DR PIR; S44184; S44184.
DR RefSeq; XP_309032.2; XM_309032.3.
DR AlphaFoldDB; Q17025; -.
DR SMR; Q17025; -.
DR STRING; 7165.AGAP006711-PA; -.
DR MEROPS; S01.166; -.
DR PaxDb; Q17025; -.
DR GeneID; 1270347; -.
DR KEGG; aga:AgaP_AGAP006711; -.
DR CTD; 1270347; -.
DR VEuPathDB; VectorBase:AGAP006711; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_4_1; -.
DR InParanoid; Q17025; -.
DR OMA; SGQHSCG; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q17025; -.
DR Proteomes; UP000007062; Chromosome 2L.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Digestion; Disulfide bond; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..32
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027656"
FT CHAIN 33..258
FT /note="Chymotrypsin-2"
FT /id="PRO_0000027657"
FT DOMAIN 33..255
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 74
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 206
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 59..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 182..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 208..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 21
FT /note="T -> P (in Ref. 1; CAA79326/CAA83567)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="H -> N (in Ref. 1; CAA79326/CAA83567)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="E -> V (in Ref. 1; CAA79326/CAA83567)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="G -> C (in Ref. 1; CAA79326/CAA83567)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="N -> D (in Ref. 1; CAA79326/CAA83567)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="P -> R (in Ref. 1; CAA79326)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="K -> E (in Ref. 1; CAA79326/CAA83567)"
FT /evidence="ECO:0000305"
FT CONFLICT 194..196
FT /note="LGH -> FPD (in Ref. 1; CAA79326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 27928 MW; 8C82E91B5C790EB8 CRC64;
MLRKVFAVVS VLLVVSAAKV TKLVLDDHYV NRVVGGEVAK NGSAPYQVSL QVPGWGHNCG
GSLLNNRWVL TAAHCLVGYE PSDLMVLVGT NSLKEGGELL KVDKLLYHSR YNRPQFHNDI
GLMRLEQPVQ FSELVQSVEY LEKAVPVNAT VRLTGWGRTS TNGNVPTLLQ SLNVVTLSNE
DCKAKMGNPK NVDLGHVCTL TKAGEGACNG DSGGPLVYEG KLVGVVNFGV PCGRGFPDGF
ARVSYYHEWV RTTMANNS
