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 03-AUG-2022, entry version 134.
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; 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; CAA80516.1; -; Genomic_DNA.
DR EMBL; AAAB01008964; EAA12262.3; -; Genomic_DNA.
DR PIR; S40006; S40006.
DR RefSeq; XP_317172.2; XM_317172.4.
DR AlphaFoldDB; P35041; -.
DR SMR; P35041; -.
DR STRING; 7165.AGAP008293-PA; -.
DR MEROPS; S01.130; -.
DR PaxDb; P35041; -.
DR GeneID; 1277689; -.
DR KEGG; aga:AgaP_AGAP008293; -.
DR CTD; 1277689; -.
DR VEuPathDB; VectorBase:AGAP008293; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; P35041; -.
DR OMA; KYKQYGG; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P35041; -.
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..41
FT /note="Activation peptide"
FT /id="PRO_0000028255"
FT CHAIN 42..267
FT /note="Trypsin-7"
FT /id="PRO_0000028256"
FT DOMAIN 42..266
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 82
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 216
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 67..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 192..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 218..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 118..124
FT /note="KYNEYNT -> NYDDSTI (in Ref. 1; CAA80516)"
FT /evidence="ECO:0000305"
FT CONFLICT 170..173
FT /note="KSAT -> HNAA (in Ref. 1; CAA80516)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="D -> E (in Ref. 1; CAA80516)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="S -> A (in Ref. 1; CAA80516)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="V -> I (in Ref. 1; CAA80516)"
FT /evidence="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
