TRY4_ANOGA
ID TRY4_ANOGA Reviewed; 275 AA.
AC P35038; Q7Q494;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Trypsin-4;
DE EC=3.4.21.4;
DE Flags: Precursor;
GN Name=TRYP4; ORFNames=AGAP008292;
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; CAA80515.1; -; Genomic_DNA.
DR EMBL; AAAB01008964; EAA12264.2; -; Genomic_DNA.
DR PIR; S40005; S40005.
DR RefSeq; XP_317173.2; XM_317173.3.
DR AlphaFoldDB; P35038; -.
DR SMR; P35038; -.
DR MEROPS; S01.130; -.
DR PaxDb; P35038; -.
DR GeneID; 1277690; -.
DR KEGG; aga:AgaP_AGAP008292; -.
DR CTD; 1277690; -.
DR VEuPathDB; VectorBase:AGAP008292; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; P35038; -.
DR OMA; HCTELAS; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P35038; -.
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..48
FT /note="Activation peptide"
FT /id="PRO_0000028249"
FT CHAIN 49..275
FT /note="Trypsin-4"
FT /id="PRO_0000028250"
FT DOMAIN 49..274
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 89
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 224
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 74..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 199..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 226..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 97
FT /note="A -> E (in Ref. 1; CAA80515)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="A -> T (in Ref. 1; CAA80515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 29608 MW; AEFFEDA9F24F71C8 CRC64;
MSNKITILLA VLLAVVACAQ AHASHQRRVP YPLPRFLPRP HHTVSNHRIV GGFEIDVAET
PYQVSLQRSK RHICGGSVLS GKWILTAAHC TDGSQPASLT VRLGSSRHAS GGSVIHVARI
VQHPDYDQET IDYDYSLLEL ESVLTFSNKV QPIALPEQDE AVEDGIMTIV SGWGSTKSAI
ESNAILRAAN VPTVNQDECN QAYHKSEGIT ERMLCAGYQQ GGKDACQGDS GGPLVAEDKL
IGVVSWGAGC AQPGYPGVYA RVAVVRDWIR ETCGV
