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Database: UniProt/SWISS-PROT
Entry: TRY1_ANOGA
LinkDB: TRY1_ANOGA
Original site: 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   23-MAY-2018, entry version 120.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; 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;
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
RT   the 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.,
RA   Crisanti A.;
RT   "Constitutive and blood meal-induced trypsin genes in Anopheles
RT   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.,
RA   Lai Z., Kraft C.L., Abril J.F., Anthouard V., Arensburger P.,
RA   Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V.,
RA   Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S.,
RA   Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M.,
RA   Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I.,
RA   Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z.,
RA   Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R.,
RA   Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E.,
RA   Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F.,
RA   Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R.,
RA   Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C.,
RA   Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V.,
RA   Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D.,
RA   Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H.,
RA   Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A.,
RA   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.,
RA   Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S.,
RA   Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C.,
RA   Weissenbach J., Kafatos F.C., 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
CC       meal. {ECO:0000269|PubMed:7498434, ECO:0000269|PubMed:8335004}.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7498434,
CC       ECO:0000269|PubMed:8335004}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed at low level in the
CC       gut of adult females. Also expressed in the gut of male and female
CC       pupae. {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.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   ProteinModelPortal; P35035; -.
DR   SMR; P35035; -.
DR   STRING; 7165.AGAP008296-PA; -.
DR   MEROPS; S01.130; -.
DR   PaxDb; P35035; -.
DR   PRIDE; P35035; -.
DR   EnsemblMetazoa; AGAP008296-RA; AGAP008296-PA; AGAP008296.
DR   GeneID; 1277688; -.
DR   KEGG; aga:AgaP_AGAP008296; -.
DR   VectorBase; AGAP008296-RA; AGAP008296-PA; AGAP008296.
DR   CTD; 1277688; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251820; -.
DR   InParanoid; P35035; -.
DR   KO; K01312; -.
DR   OMA; SNESDEW; -.
DR   OrthoDB; EOG091G0DF7; -.
DR   PhylomeDB; P35035; -.
DR   Proteomes; UP000007062; Chromosome 3R.
DR   Proteomes; UP000007062; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   Complete proteome; Digestion; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   PROPEP       19     47       Activation peptide.
FT                                /FTId=PRO_0000028243.
FT   CHAIN        48    274       Trypsin-1.
FT                                /FTId=PRO_0000028244.
FT   DOMAIN       48    273       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     88     88       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    133    133       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    229    229       Charge relay system. {ECO:0000250}.
FT   SITE        223    223       Required for specificity. {ECO:0000250}.
FT   DISULFID     73     89       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    198    214       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    225    249       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   CONFLICT     93     93       A -> R (in Ref. 1; CAA79327).
FT                                {ECO:0000305}.
FT   CONFLICT     95     95       P -> T (in Ref. 1; CAA79327 and 2;
FT                                CAA80512). {ECO:0000305}.
FT   CONFLICT    101    101       R -> P (in Ref. 1; CAA79327).
FT                                {ECO:0000305}.
FT   CONFLICT    148    148       S -> A (in Ref. 2; CAA80512).
FT                                {ECO:0000305}.
FT   CONFLICT    204    204       E -> D (in Ref. 1; CAA79327 and 2;
FT                                CAA80512). {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
//
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