ID   TRY4_ANOGA              Reviewed;         275 AA.
AC   P35038; Q7Q494;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Trypsin-4;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
GN   Name=TRYP4; ORFNames=AGAP008292;
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; CAA80515.1; -; Genomic_DNA.
DR   EMBL; AAAB01008964; EAA12264.2; -; Genomic_DNA.
DR   PIR; S40005; S40005.
DR   RefSeq; XP_317173.2; XM_317173.3.
DR   AlphaFoldDB; P35038; -.
DR   SMR; P35038; -.
DR   MEROPS; S01.130; -.
DR   PaxDb; 7165-AGAP008292-PA; -.
DR   EnsemblMetazoa; AGAP008292-RA; AGAP008292-PA; AGAP008292.
DR   GeneID; 1277690; -.
DR   KEGG; aga:AgaP_AGAP008292; -.
DR   CTD; 1277690; -.
DR   VEuPathDB; VectorBase:AGAP008292; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   InParanoid; P35038; -.
DR   OMA; GFQIDIA; -.
DR   OrthoDB; 2910936at2759; -.
DR   PhylomeDB; P35038; -.
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   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24264:SF65; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24264; TRYPSIN-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.
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..48
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028249"
FT   CHAIN           49..275
FT                   /note="Trypsin-4"
FT                   /id="PRO_0000028250"
FT   DOMAIN          49..274
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        89
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        134
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        230
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            224
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        74..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        199..215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        226..250
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        97
FT                   /note="A -> E (in Ref. 1; CAA80515)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="A -> T (in Ref. 1; CAA80515)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   275 AA;  29608 MW;  AEFFEDA9F24F71C8 CRC64;
     MSNKITILLA VLLAVVACAQ AHASHQRRVP YPLPRFLPRP HHTVSNHRIV GGFEIDVAET
     PYQVSLQRSK RHICGGSVLS GKWILTAAHC TDGSQPASLT VRLGSSRHAS GGSVIHVARI
     VQHPDYDQET IDYDYSLLEL ESVLTFSNKV QPIALPEQDE AVEDGIMTIV SGWGSTKSAI
     ESNAILRAAN VPTVNQDECN QAYHKSEGIT ERMLCAGYQQ GGKDACQGDS GGPLVAEDKL
     IGVVSWGAGC AQPGYPGVYA RVAVVRDWIR ETCGV
//