TRY6_ANOGA
ID TRY6_ANOGA Reviewed; 273 AA.
AC P35040; Q7Q492;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Trypsin-6;
DE EC=3.4.21.4;
DE Flags: Precursor;
GN Name=TRYP6; ORFNames=AGAP008290;
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 -!- CAUTION: As this protein has Gly-222 in the position that determines
CC the specificity of the enzyme instead of the Asp found in trypsins, it
CC could have a chymotrypsin-like activity. {ECO:0000305}.
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DR EMBL; Z22930; CAA80513.1; -; Genomic_DNA.
DR EMBL; AAAB01008964; EAA12587.2; -; Genomic_DNA.
DR PIR; S40003; S40003.
DR RefSeq; XP_317175.2; XM_317175.2.
DR AlphaFoldDB; P35040; -.
DR SMR; P35040; -.
DR STRING; 7165.AGAP008290-PA; -.
DR MEROPS; S01.130; -.
DR PaxDb; P35040; -.
DR GeneID; 1277692; -.
DR KEGG; aga:AgaP_AGAP008290; -.
DR CTD; 1277692; -.
DR VEuPathDB; VectorBase:AGAP008290; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; P35040; -.
DR OMA; DAPYQIF; -.
DR OrthoDB; 594175at2759; -.
DR PhylomeDB; P35040; -.
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..22
FT /evidence="ECO:0000255"
FT PROPEP 23..46
FT /note="Activation peptide"
FT /id="PRO_0000028253"
FT CHAIN 47..273
FT /note="Trypsin-6"
FT /id="PRO_0000028254"
FT DOMAIN 47..272
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 87
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 228
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 222
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 72..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 197..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 224..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 13
FT /note="H -> L (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="K -> R (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="S -> A (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="E -> Q (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="L -> V (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 127..128
FT /note="GG -> SA (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 140..142
FT /note="CEL -> SEI (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="V -> L (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="Q -> S (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="D -> E (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="L -> S (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 207..208
FT /note="VA -> IT (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="A -> E (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="D -> E (in Ref. 1; CAA80513)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 29295 MW; 4A485528B7D679D1 CRC64;
MLSKFTAILL AVHIALFACA LTQAEKRHKL TRPAFHPNAP YLAGKRIVGG FVIDISDAPY
QISLQYNGKH HCGGSILNSK WILTAAHCID LYSEVKPTVR VGSSEHAAGG TVLHLLRIVP
HPGHSSGGNN YDIALLELEC ELTFNDNVQP VQLPEQDDPI DEGTMGIVSG WGMTMSAADL
NAILRATNVP TVNQQECNQA YQSYGGVAEQ MFCAGYKQGG TGTCRNDSGG PFVAEGKLIG
VVSWSHECAL AGYPGVYARV ASVRDWIRET SGV
