TRY5_AEDAE
ID TRY5_AEDAE Reviewed; 266 AA.
AC P29787; Q16ID7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Trypsin 5G1;
DE EC=3.4.21.4;
DE Flags: Precursor;
GN ORFNames=AAEL013712;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-266.
RX PubMed=9087545; DOI=10.1111/j.1365-2583.1993.tb00127.x;
RA Kalhok S., Tabak L.M., Prosser D.E., Brook W., Downer A.E.R., White B.N.;
RT "Isolation, sequencing and characterization of two cDNA clones coding for
RT trypsin-like enzymes from the midgut of Aedes aegypti.";
RL Insect Mol. Biol. 2:71-79(1993).
CC -!- FUNCTION: Major function may be to aid in digestion of the blood meal.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Midgut.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA45715.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CH478086; EAT34029.1; -; Genomic_DNA.
DR EMBL; X64363; CAA45715.1; ALT_FRAME; mRNA.
DR PIR; S19891; TRWV5Y.
DR RefSeq; XP_001663895.1; XM_001663845.1.
DR AlphaFoldDB; P29787; -.
DR SMR; P29787; -.
DR STRING; 7159.AAEL013712-PA; -.
DR MEROPS; S01.130; -.
DR GeneID; 5578510; -.
DR KEGG; aag:5578510; -.
DR VEuPathDB; VectorBase:AAEL010196; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; P29787; -.
DR OMA; NWNDIAL; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P29787; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; 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; -; 1.
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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..39
FT /note="Activation peptide"
FT /id="PRO_0000028241"
FT CHAIN 40..266
FT /note="Trypsin 5G1"
FT /id="PRO_0000028242"
FT DOMAIN 40..265
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 81
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 125
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 215
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 66..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 190..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 217..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 151
FT /note="A -> T (in Ref. 2; CAA45715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 266 AA; 28246 MW; 63CB0B37F1B022C6 CRC64;
MTRIILILTA TFFACALGAS TGGSHPLRPW WNALRSSGRI VGGFEVPVEE VPFQVSLSGV
GSSHFCGGSL LSERWVMTAG HCAASGQTNL QVRIGSSQHA SGGQLIKVKK VNRHPKYDEV
TTDYDFALLE LEETVTFSDS CAPVKLPQKD APVNEGTCLQ VSGWGNTQNP SESSEVLRAA
YVPAVSQKEC HKAYLSFGGV TDRMVCAGFK EGGKDSCQGD SGGPLVHDNT LVGVVSWGYG
CAQAGYPGVY ARVASVRDWV KEVSGL
