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 16-JUN-2009, entry version 67. 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; 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 RT chymotrypsins."; RL Eur. J. Biochem. 268:4027-4035(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEST; RX MEDLINE=22251359; 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., RA Lai Z., Kraft C.L., Abril J.F., Anthouard V., Arensburger P., RA Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., RA Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., RA Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., RA Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., RA Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., RA Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., RA Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., RA Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., RA Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., RA Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., RA Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., RA Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., RA Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., RA Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., RA 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., RA Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., RA Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., RA Weissenbach J., Kafatos F.C., 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: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, CC Phe-|-Xaa, Leu-|-Xaa. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: After blood feeding, expression is induced in CC the midgut epithelium, followed by secretion into the midgut CC lumen. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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; -. DR HSSP; P00746; 1FDP. DR MEROPS; S01.166; -. DR Ensembl; AGAP006709; Anopheles gambiae. DR GeneID; 1270348; -. DR KEGG; aga:AgaP_AGAP006709; -. DR VectorBase; AGAP006709; Anopheles gambiae. DR HOGENOM; Q27289; -. DR OMA; Q27289; GHTSANG. DR BRENDA; 3.4.21.1; 165157. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR018114; Peptidase_S1/S6_AS. DR InterPro; IPR001254; Peptidase_S1_S6. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 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 Complete proteome; Digestion; Direct protein sequencing; KW Disulfide bond; Hydrolase; Protease; Secreted; Serine protease; KW Signal; Zymogen. FT SIGNAL 1 17 Potential. FT PROPEP 18 32 Activation peptide. FT /FTId=PRO_0000027654. FT CHAIN 33 259 Chymotrypsin-1. FT /FTId=PRO_0000027655. FT DOMAIN 33 255 Peptidase S1. FT ACT_SITE 74 74 Charge relay system (By similarity). FT ACT_SITE 119 119 Charge relay system (By similarity). FT ACT_SITE 212 212 Charge relay system (By similarity). FT SITE 206 206 Required for specificity (By similarity). FT DISULFID 59 75 By similarity. FT DISULFID 182 198 By similarity. FT DISULFID 208 232 By similarity. FT CONFLICT 9 11 VSV -> ASI (in Ref. 1; CAA79325/ FT CAA83568). FT CONFLICT 21 21 T -> P (in Ref. 1; CAA79325/CAA83568). FT CONFLICT 28 28 N -> H (in Ref. 1; CAA79325/CAA83568). FT CONFLICT 130 130 R -> Q (in Ref. 1; CAA79325/CAA83568). FT CONFLICT 158 158 H -> R (in Ref. 1; CAA79325/CAA83568). 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 //