CTR1_ANOGA
ID CTR1_ANOGA Reviewed; 259 AA.
AC Q27289; Q7PF17;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Chymotrypsin-1;
DE EC=3.4.21.1;
DE AltName: Full=AnChym1;
DE Flags: Precursor;
GN Name=CHYM1; ORFNames=AGAP006709;
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], PROTEIN SEQUENCE OF 33-42,
RP SUBCELLULAR LOCATION, AND TISSUE 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; Z18887; CAA79325.1; -; mRNA.
DR EMBL; Z32645; CAA83568.1; -; Genomic_DNA.
DR EMBL; AAAB01008807; EAA45497.2; -; Genomic_DNA.
DR PIR; S49129; S49129.
DR RefSeq; XP_309033.2; XM_309033.4.
DR AlphaFoldDB; Q27289; -.
DR SMR; Q27289; -.
DR STRING; 7165.AGAP006709-PA; -.
DR MEROPS; S01.166; -.
DR PaxDb; Q27289; -.
DR GeneID; 1270348; -.
DR KEGG; aga:AgaP_AGAP006709; -.
DR CTD; 1270348; -.
DR VEuPathDB; VectorBase:AGAP006709; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_4_1; -.
DR InParanoid; Q27289; -.
DR OMA; ISNDECK; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q27289; -.
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 1: Evidence at protein level;
KW Digestion; Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..32
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:11453997"
FT /id="PRO_0000027654"
FT CHAIN 33..259
FT /note="Chymotrypsin-1"
FT /id="PRO_0000027655"
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 9..11
FT /note="VSV -> ASI (in Ref. 1; CAA79325/CAA83568)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="T -> P (in Ref. 1; CAA79325/CAA83568)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="N -> H (in Ref. 1; CAA79325/CAA83568)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="R -> Q (in Ref. 1; CAA79325/CAA83568)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="H -> R (in Ref. 1; CAA79325/CAA83568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 27722 MW; 3EF7D6F19EAAED23 CRC64;
MLRKVFAVVS VLLVVSAAKV TKLVLDDNYV NRVVGGEVAK NGSAPYQVSL QVPGWGHNCG
GSLLNDRWVL TAAHCLVGHA PGDLMVLVGT NSLKEGGELL KVDKLLYHSR YNLPRFHNDI
GLVRLEQPVR FSELVQSVEY SEKAVPANAT VRLTGWGHTS ANGPSPTLLQ SLNVVTLSNE
DCNKKGGDPG YTDVGHLCTL TKTGEGACNG DSGGPLVYEG KLVGVVNFGV PCALGYPDGF
ARVSYYHDWV RTTMANNSK
