TRY3_AEDAE
ID TRY3_AEDAE Reviewed; 254 AA.
AC P29786; Q170R6; Q8MMK9; Q8T637;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Trypsin 3A1;
DE EC=3.4.21.4;
DE Flags: Precursor;
GN ORFNames=AAEL007818;
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 [MRNA] (ISOFORM B).
RC TISSUE=Larval gut;
RA Borovsky D., Matthys V.S.;
RT "Cloning and sequencing of early trypsin mRNA from Aedes aegypti 4th instar
RT larval gut.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM B).
RC TISSUE=Gut;
RA Borovsky D., Peeters T.;
RT "Cloning, sequencing and characterization of Aedes aegypti early trypsin
RT pre-mRNA.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Midgut;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
CC -!- FUNCTION: Major function may be to aid in digestion of the blood meal.
CC {ECO:0000269|PubMed:9087545}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:9087545}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=P29786-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P29786-2; Sequence=VSP_035031;
CC -!- TISSUE SPECIFICITY: Midgut. {ECO:0000269|PubMed:9087545}.
CC -!- INDUCTION: By blood feed. {ECO:0000269|PubMed:9087545}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF487426; AAL93209.1; -; mRNA.
DR EMBL; AF508783; AAM34268.1; -; Transcribed_RNA.
DR EMBL; X64362; CAA45714.1; -; mRNA.
DR EMBL; CH477469; EAT40452.1; -; Genomic_DNA.
DR EMBL; CH477469; EAT40453.1; -; Genomic_DNA.
DR PIR; S19890; TRWV3Y.
DR RefSeq; XP_001652943.1; XM_001652893.1. [P29786-1]
DR RefSeq; XP_001652944.1; XM_001652894.1. [P29786-2]
DR AlphaFoldDB; P29786; -.
DR SMR; P29786; -.
DR MEROPS; S01.130; -.
DR GeneID; 5569681; -.
DR KEGG; aag:5569681; -.
DR VEuPathDB; VectorBase:AAEL007818; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P29786; -.
DR OMA; VNRTECA; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P29786; -.
DR BRENDA; 3.4.21.4; 149.
DR Proteomes; UP000008820; Chromosome 2.
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 Alternative splicing; Digestion; Disulfide bond; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..27
FT /note="Activation peptide"
FT /id="PRO_0000028239"
FT CHAIN 28..254
FT /note="Trypsin 3A1"
FT /id="PRO_0000028240"
FT DOMAIN 28..253
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 68
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 113
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 203
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 53..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 178..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 205..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 18..19
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_035031"
FT CONFLICT 14..17
FT /note="GLSQ -> DSAK (in Ref. 3; CAA45714)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="A -> R (in Ref. 3; CAA45714)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="E -> D (in Ref. 3; CAA45714)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="S -> F (in Ref. 2; AAM34268)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="K -> E (in Ref. 2; AAM34268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 26852 MW; 8127EBC9C523FAFE CRC64;
MNQFLFVSFC ALLGLSQVSA ATLSSGRIVG GFQIDIAEVP HQVSLQRSGR HFCGGSIISP
RWVLTAAHCT TNTDPAAYTI RAGSTDRTNG GIIVKVKSVI PHPQYNGDTY NYDFSLLELD
ESIGFSRSIE AIALPEASET VADGAMCTVS GWGDTKNVFE MNTLLRAVNV PSYNQAECAA
ALVNVVPVTE QMICAGYAAG GKDSCQGDSG GPLVSGDKLV GVVSWGKGCA LPNLPGVYAR
VSTVRQWIRE VSEV
