TRY1_ANOGA
ID TRY1_ANOGA Reviewed; 274 AA.
AC P35035; Q7PN85;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Trypsin-1;
DE EC=3.4.21.4;
DE AltName: Full=Antryp1;
DE Flags: Precursor;
GN Name=TRYP1; ORFNames=AGAP008296;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=Suakoko; TISSUE=Midgut;
RX PubMed=8335004; DOI=10.1002/j.1460-2075.1993.tb05951.x;
RA Mueller H.-M., Crampton J.M., della Torre A., Sinden R., Crisanti A.;
RT "Members of a trypsin gene family in Anopheles gambiae are induced in the
RT gut by blood meal.";
RL EMBO J. 12:2891-2900(1993).
RN [2]
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 [3]
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: Major function may be to aid in digestion of the blood meal.
CC {ECO:0000269|PubMed:7498434, ECO:0000269|PubMed:8335004}.
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 ECO:0000269|PubMed:8335004}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed at low level in the gut of
CC adult females. Also expressed in the gut of male and female pupae.
CC {ECO:0000269|PubMed:7498434, ECO:0000269|PubMed:8335004}.
CC -!- INDUCTION: By blood meal. {ECO:0000269|PubMed:8335004}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; Z18889; CAA79327.1; -; mRNA.
DR EMBL; Z22930; CAA80512.1; -; Genomic_DNA.
DR EMBL; AAAB01008964; EAA12590.3; -; Genomic_DNA.
DR PIR; S35339; S35339.
DR RefSeq; XP_317170.2; XM_317170.2.
DR AlphaFoldDB; P35035; -.
DR SMR; P35035; -.
DR MEROPS; S01.130; -.
DR PaxDb; P35035; -.
DR GeneID; 1277688; -.
DR KEGG; aga:AgaP_AGAP008296; -.
DR CTD; 1277688; -.
DR VEuPathDB; VectorBase:AGAP008296; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; P35035; -.
DR OMA; GGKGACH; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P35035; -.
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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..47
FT /note="Activation peptide"
FT /id="PRO_0000028243"
FT CHAIN 48..274
FT /note="Trypsin-1"
FT /id="PRO_0000028244"
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 133
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 198..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 225..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 93
FT /note="A -> R (in Ref. 1; CAA79327)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="P -> T (in Ref. 1; CAA79327 and 2; CAA80512)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="R -> P (in Ref. 1; CAA79327)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="S -> A (in Ref. 2; CAA80512)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="E -> D (in Ref. 1; CAA79327 and 2; CAA80512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 29057 MW; 7055CA51C6CEF3F8 CRC64;
MSNKIAILLA VLVAVVACAE AQANQRHRLV RPSPSFSPRP RYAVGQRIVG GFEIDVSDAP
YQVSLQYNKR HNCGGSVLSS KWVLTAAHCT AGASPSSLTV RLGTSRHASG GTVVRVARVV
QHPKYDSSSI DFDYSLLELE DELTFSDSVQ PVGLPKQDET VKDGTMTTVS GWGNTQSAAE
SNAVLRAANV PTVNQKECNK AYSEFGGVTD RMLCAGYQQG GKDACQGDSG GPLVADGKLV
GVVSWGYGCA QAGYPGVYSR VAVVRDWVRE NSGV
