ASPP_AEDAE
ID ASPP_AEDAE Reviewed; 387 AA.
AC Q03168; Q177E0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Lysosomal aspartic protease;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN ORFNames=AAEL006169;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 54-71.
RX PubMed=1400492; DOI=10.1016/s0021-9258(19)36686-4;
RA Cho W.L., Raikhel A.S.;
RT "Cloning of cDNA for mosquito lysosomal aspartic protease. Sequence
RT analysis of an insect lysosomal enzyme similar to cathepsins D and E.";
RL J. Biol. Chem. 267:21823-21829(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RA Cho W.-L., Dhadialla T.S., Raikhel A.S.;
RT "Purification and characterization of a lysosomal aspartic protease with
RT cathepsin D activity from the mosquito.";
RL Insect Biochem. 21:165-176(1991).
CC -!- FUNCTION: May degrade organelles involved in the biosynthesis and
CC secretion of vitellogenin. {ECO:0000269|Ref.3}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M95187; AAA29350.1; -; mRNA.
DR EMBL; CH477377; EAT42285.1; -; Genomic_DNA.
DR PIR; A45117; A45117.
DR RefSeq; XP_001657556.1; XM_001657506.1.
DR AlphaFoldDB; Q03168; -.
DR SMR; Q03168; -.
DR STRING; 7159.AAEL006169-PA; -.
DR Allergome; 11917; Aed a 11.
DR Allergome; 11918; Aed a 11.0101.
DR MEROPS; A01.009; -.
DR GeneID; 5567565; -.
DR KEGG; aag:5567565; -.
DR VEuPathDB; VectorBase:AAEL006169; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_3_1; -.
DR InParanoid; Q03168; -.
DR OMA; YLYILGQ; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; Q03168; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05485; Cathepsin_D_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR034129; Cathepsin_D-like.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lysosome; Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..18
FT PROPEP 19..53
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:1400492"
FT /id="PRO_0000025933"
FT CHAIN 54..387
FT /note="Lysosomal aspartic protease"
FT /id="PRO_0000025934"
FT DOMAIN 68..384
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..106
FT /evidence="ECO:0000250"
FT DISULFID 263..267
FT /evidence="ECO:0000250"
FT DISULFID 306..343
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="A -> S (in Ref. 1; AAA29350)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 41790 MW; B9AD73E444167EEB CRC64;
MLIKSIIALV CLAVLAQADF VRVQLHKTES ARQHFRNVDT EIKQLRLKYN AVSGPVPEPL
SNYLDAQYYG AITIGTPPQS FKVVFDTGSS NLWVPSKECS FTNIACLMHN KYNAKKSSTF
EKNGTAFHIQ YGSGSLSGYL STDTVGLGGV SVTKQTFAEA INEPGLVFVA AKFDGILGLG
YSSISVDGVV PVFYNMFNQG LIDAPVFSFY LNRDPSAAEG GEIIFGGSDS NKYTGDFTYL
SVDRKAYWQF KMDSVKVGDT EFCNNGCEAI ADTGTSLIAG PVSEVTAINK AIGGTPIMNG
EYMVDCSLIP KLPKISFVLG GKSFDLEGAD YVLRVAQMGK TICLSGFMGI DIPPPNGPLW
ILGDVFIGKY YTEFDMGNDR VGFATAV
