SP24D_ANOGA
ID SP24D_ANOGA Reviewed; 271 AA.
AC Q17004; Q7PIA2; Q7Q5I5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 3.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Serine protease SP24D;
DE EC=3.4.21.-;
DE AltName: Full=AgSp24D;
DE Flags: Precursor;
GN Name=Sp24D; ORFNames=AGAP006416;
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=G3;
RX PubMed=9359580; DOI=10.1046/j.1365-2583.1997.00193.x;
RA Han Y.S., Salazar C.E., Reese-Stardy S.R., Cornel A., Gorman M.J.,
RA Collins F.H., Paskewitz S.M.;
RT "Cloning and characterization of a serine protease from the human malaria
RT vector, Anopheles gambiae.";
RL Insect Mol. Biol. 6:385-395(1997).
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 -!- TISSUE SPECIFICITY: Highest level of adult expression is in the thorax.
CC {ECO:0000269|PubMed:9359580}.
CC -!- DEVELOPMENTAL STAGE: Low expression levels are seen in larvae and
CC pupae. Expressed at higher levels in adult males than females.
CC Plasmodium-refractory mosquitoes have higher levels of expression than
CC susceptible mosquitoes. {ECO:0000269|PubMed:9359580}.
CC -!- INDUCTION: Expression levels are not increased after blood feeding or
CC cold shock, septic wounding, bacterial injection, laminarin injection
CC or CM-Sephadex bead injection. {ECO:0000269|PubMed:9359580}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA73920.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U21917; AAA73920.1; ALT_FRAME; mRNA.
DR EMBL; AAAB01008960; EAA44223.1; -; Genomic_DNA.
DR RefSeq; XP_316450.1; XM_316450.1.
DR AlphaFoldDB; Q17004; -.
DR SMR; Q17004; -.
DR STRING; 7165.AGAP006416-PA; -.
DR PaxDb; Q17004; -.
DR GeneID; 1277027; -.
DR KEGG; aga:AgaP_AGAP006416; -.
DR CTD; 1277027; -.
DR VEuPathDB; VectorBase:AGAP006416; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_4_1; -.
DR InParanoid; Q17004; -.
DR OMA; RYLQWNT; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q17004; -.
DR Proteomes; UP000007062; Chromosome 2L.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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 Disulfide bond; Hydrolase; Protease; Reference proteome; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..49
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028151"
FT CHAIN 50..271
FT /note="Serine protease SP24D"
FT /id="PRO_0000028152"
FT DOMAIN 50..269
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 90
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 75..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 199..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 221..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 126
FT /note="P -> T (in Ref. 1; AAA73920)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="T -> S (in Ref. 1; AAA73920)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..202
FT /note="MA -> DP (in Ref. 1; AAA73920)"
FT /evidence="ECO:0000305"
FT CONFLICT 238..239
FT /note="VA -> RP (in Ref. 1; AAA73920)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="R -> K (in Ref. 1; AAA73920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 28655 MW; C83F3372622ECFD1 CRC64;
MTLADRVPLA LAALAYLALV SGVRFHLSEQ NDVLPGGSQA RRPFFQGARI VGGSVASEGQ
FPHQVALLRG NALTCGGSLI ESRWVLTAAH CVYNGALVVP ASSIVVVAGS VSLSNGVRRA
VARVIPHERY GNFKNDVALL QLQLSLPSSA YIRPIALRTT SVPAGSEVVI SGWGRMYQGG
PVSNMLRYNR ATVVADQQCR MATGISTGLI CFTSPVNNGA CNGDSGGPAI LNNQLVGVAN
FIINYCGSAS PDGYARVSDF VTWIQTTMRR Y
