TRY3_ANOGA
ID TRY3_ANOGA Reviewed; 275 AA.
AC P35037; Q7PNF7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 5.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Trypsin-3;
DE EC=3.4.21.4;
DE Flags: Precursor;
GN Name=TRYP3; ORFNames=AGAP008294;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA12261.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z22930; CAA80517.1; -; Genomic_DNA.
DR EMBL; AAAB01008964; EAA12261.3; ALT_SEQ; Genomic_DNA.
DR PIR; S40007; S40007.
DR RefSeq; XP_317171.2; XM_317171.3.
DR AlphaFoldDB; P35037; -.
DR SMR; P35037; -.
DR MEROPS; S01.130; -.
DR PaxDb; P35037; -.
DR GeneID; 3291693; -.
DR KEGG; aga:AgaP_AGAP008294; -.
DR CTD; 3291693; -.
DR VEuPathDB; VectorBase:AGAP008294; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; P35037; -.
DR OrthoDB; 1314811at2759; -.
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; -; 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..22
FT /evidence="ECO:0000255"
FT PROPEP 23..48
FT /note="Activation peptide"
FT /id="PRO_0000028247"
FT CHAIN 49..275
FT /note="Trypsin-3"
FT /id="PRO_0000028248"
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 42
FT /note="K -> Q (in Ref. 1; CAA80517)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="S -> T (in Ref. 1; CAA80517)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="D -> E (in Ref. 1; CAA80517)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="I -> T (in Ref. 1; CAA80517)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="V -> I (in Ref. 1; CAA80517)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="D -> N (in Ref. 1; CAA80517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 29374 MW; 93D27A26AF4C5458 CRC64;
MISNKIAILL AVLVVAVACA QARVALKHRS VQALPRFLPR PKYDVGHRIV GGFEIDVSET
PYQVSLQYFN SHRCGGSVLN SKWILTAAHC TVNLQPSSLA VRLGSSRHAS GGTVVRVARV
LEHPNYDDST IDYDFSLMEL ESELTFSDVV QPVSLPDQDE AVEDGTMTIV SGWGNTQSAA
ESNAILRAAN VPTVNQKECT IAYSSSGGIT DRMLCAGYKR GGKDACQGDS GGPLVVDGKL
VGVVSWGFGC AMPGYPGVYA RVAVVRDWVR ENSGA
