ID   TRY5_ANOGA              Reviewed;         274 AA.
AC   P35039; Q7Q493;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Trypsin-5;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
GN   Name=TRYP5; ORFNames=AGAP008291;
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Suakoko; TISSUE=Midgut;
RX   PubMed=7498434; DOI=10.1006/expr.1995.1128;
RA   Mueller H.-M., Catteruccia F., Vizioli J., della Torre A., Crisanti A.;
RT   "Constitutive and blood meal-induced trypsin genes in Anopheles gambiae.";
RL   Exp. Parasitol. 81:371-385(1995).
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   -!- FUNCTION: Constitutive trypsin that is expressed 2 days after
CC       emergence, coinciding with host seeking behavior of the female.
CC       {ECO:0000269|PubMed:7498434}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7498434}.
CC   -!- TISSUE SPECIFICITY: Expressed in the midgut. Expression levels drop a
CC       few hours after blood feeding and pick up again 28 hours later.
CC       {ECO:0000269|PubMed:7498434}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; Z22930; CAA80514.1; -; Genomic_DNA.
DR   EMBL; AAAB01008964; EAA12584.2; -; Genomic_DNA.
DR   PIR; S40004; S40004.
DR   RefSeq; XP_317174.2; XM_317174.3.
DR   AlphaFoldDB; P35039; -.
DR   SMR; P35039; -.
DR   MEROPS; S01.130; -.
DR   PaxDb; 7165-AGAP008291-PA; -.
DR   EnsemblMetazoa; AGAP008291-RA; AGAP008291-PA; AGAP008291.
DR   GeneID; 1277691; -.
DR   KEGG; aga:AgaP_AGAP008291; -.
DR   CTD; 1277691; -.
DR   VEuPathDB; VectorBase:AGAP008291; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   InParanoid; P35039; -.
DR   OMA; CINDNAP; -.
DR   OrthoDB; 2910936at2759; -.
DR   PhylomeDB; P35039; -.
DR   Proteomes; UP000007062; Chromosome 3R.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
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; Trypsin-like serine proteases; 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   PANTHER; PTHR24276:SF100; AT20289P-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Digestion; Disulfide bond; Hydrolase;
KW   Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..47
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028251"
FT   CHAIN           48..274
FT                   /note="Trypsin-5"
FT                   /id="PRO_0000028252"
FT   DOMAIN          48..273
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        88
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        132
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        229
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            223
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        197..214
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        225..249
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        13
FT                   /note="F -> I (in Ref. 1; CAA80514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        18
FT                   /note="Y -> C (in Ref. 1; CAA80514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="N -> D (in Ref. 1; CAA80514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="K -> E (in Ref. 1; CAA80514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114
FT                   /note="I -> V (in Ref. 1; CAA80514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="S -> T (in Ref. 1; CAA80514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        211
FT                   /note="Q -> E (in Ref. 1; CAA80514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="K -> E (in Ref. 1; CAA80514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259
FT                   /note="A -> P (in Ref. 1; CAA80514)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   274 AA;  29815 MW;  468AB656797AED8E CRC64;
     MSIKFTTLLA VLFALLAYAR AQAERRHKLT RPVHRFAPNR PYLAGKRIVG GFVINISDAP
     YQISLQYDDD HNCGGSILSS KWILTAAHCI NDNAPSKPTV RVGSSKHASG GTVIRVARIV
     PHPMHGSKNN YDIALLELKN ELTFSEKVQP IALPEQDEPI EEGTMGIVSG WGLTLSEADS
     NDVLRATNVP TVNQQECNKA YQSRYGGITD QMFCAGYKQG GQDTCRQDSG GPFVAKGKLI
     GVISWGHECA LAGYPGVYAR VASVRDWIRT TSGV
//