TRY5_ANOGA
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 03-AUG-2022, entry version 138.
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; P35039; -.
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; 1314811at2759; -.
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; -; 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 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.
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
