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Database: UniProt/SWISS-PROT
Entry: TRY7_ANOGA
LinkDB: TRY7_ANOGA
Original site: TRY7_ANOGA 
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   05-JUL-2017, entry version 118.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; 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.,
RA   Crisanti A.;
RT   "Constitutive and blood meal-induced trypsin genes in Anopheles
RT   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.,
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: 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: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7498434}.
CC   -!- TISSUE SPECIFICITY: Expressed in the midgut. Expression levels
CC       drop a few hours after blood feeding and pick up again 28 hours
CC       later. {ECO:0000269|PubMed:7498434}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   ProteinModelPortal; P35041; -.
DR   SMR; P35041; -.
DR   STRING; 7165.AGAP008293-PA; -.
DR   MEROPS; S01.130; -.
DR   PaxDb; P35041; -.
DR   EnsemblMetazoa; AGAP008293-RA; AGAP008293-PA; AGAP008293.
DR   GeneID; 1277689; -.
DR   KEGG; aga:AgaP_AGAP008293; -.
DR   VectorBase; AGAP008293-RA; AGAP008293-PA; AGAP008293.
DR   CTD; 1277689; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251820; -.
DR   InParanoid; P35041; -.
DR   KO; K01312; -.
DR   OMA; KYKQYGG; -.
DR   OrthoDB; EOG091G0DF7; -.
DR   PhylomeDB; P35041; -.
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     41       Activation peptide.
FT                                /FTId=PRO_0000028255.
FT   CHAIN        42    267       Trypsin-7.
FT                                /FTId=PRO_0000028256.
FT   DOMAIN       42    266       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     82     82       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    127    127       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    222    222       Charge relay system. {ECO:0000250}.
FT   SITE        216    216       Required for specificity. {ECO:0000250}.
FT   DISULFID     67     83       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    192    207       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    218    242       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   CONFLICT    118    124       KYNEYNT -> NYDDSTI (in Ref. 1; CAA80516).
FT                                {ECO:0000305}.
FT   CONFLICT    170    173       KSAT -> HNAA (in Ref. 1; CAA80516).
FT                                {ECO:0000305}.
FT   CONFLICT    199    199       D -> E (in Ref. 1; CAA80516).
FT                                {ECO:0000305}.
FT   CONFLICT    240    240       S -> A (in Ref. 1; CAA80516).
FT                                {ECO:0000305}.
FT   CONFLICT    256    256       V -> I (in Ref. 1; CAA80516).
FT                                {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
//
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