ID   TRY7_ANOGA              Reviewed;         267 AA.
AC   P35041; Q7PNF6;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Trypsin-7;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
GN   Name=TRYP7; ORFNames=AGAP008293;
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; CAA80516.1; -; Genomic_DNA.
DR   EMBL; AAAB01008964; EAA12262.3; -; Genomic_DNA.
DR   PIR; S40006; S40006.
DR   RefSeq; XP_317172.2; XM_317172.4.
DR   AlphaFoldDB; P35041; -.
DR   SMR; P35041; -.
DR   MEROPS; S01.130; -.
DR   PaxDb; 7165-AGAP008293-PA; -.
DR   EnsemblMetazoa; AGAP008293-RA; AGAP008293-PA; AGAP008293.
DR   GeneID; 1277689; -.
DR   KEGG; aga:AgaP_AGAP008293; -.
DR   CTD; 1277689; -.
DR   VEuPathDB; VectorBase:AGAP008293; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   InParanoid; P35041; -.
DR   OMA; YINSHRC; -.
DR   OrthoDB; 2910936at2759; -.
DR   PhylomeDB; P35041; -.
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..41
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028255"
FT   CHAIN           42..267
FT                   /note="Trypsin-7"
FT                   /id="PRO_0000028256"
FT   DOMAIN          42..266
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        82
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        127
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        222
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            216
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        192..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        218..242
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        118..124
FT                   /note="KYNEYNT -> NYDDSTI (in Ref. 1; CAA80516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170..173
FT                   /note="KSAT -> HNAA (in Ref. 1; CAA80516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="D -> E (in Ref. 1; CAA80516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="S -> A (in Ref. 1; CAA80516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256
FT                   /note="V -> I (in Ref. 1; CAA80516)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   267 AA;  28542 MW;  2C7FF0650E7E0F58 CRC64;
     MSNKIAILLT VLIAVVACAR AQPSRRHPLV QPRSPHGSGH RIVGGFEINV SDTPYQVSLQ
     YINSHRCGGS VLNSKWVLTA AHCTDGLQAF TLTVRLGSSR HASSGTVVNV ARIVEHPKYN
     EYNTDYDYAL LELESELTFS DVVQPVALPE QDEAVDAGTM TIVSGWGSTK SATESNAILR
     AANVPTVDQE ECREAYSHDA ITDRMLCAGY QQGGKDACQG DSGGPLVADG KLIGVVSWGS
     GCAQPGYPGV YARVAVVRNW VREISGV
//