(data stored in ACNUC30567 zone)

HOGENOM: AEDAE_1024_PE9

ID   AEDAE_1024_PE9                       STANDARD;      PRT;   387 AA.
AC   AEDAE_1024_PE9; Q03168; Q177E0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Lysosomal aspartic protease; EC=3.4.23 -;Flags: Precursor;
DE   (AEDAE_1024.PE9).
GN   ORFNames=AAEL006169;
OS   AEDES AEGYPTI.
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera;
OC   Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Culicinae;
OC   Culicini; Aedes.
OX   NCBI_TaxID=7159;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AEDAE_1024.PE9.
CC       Aedes aegypti supercontig supercont1.192 AaegL1  sequence 1..1864021
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:ASPP_AEDAE
CC   -!- FUNCTION: May degrade organelles involved in the biosynthesis and
CC       secretion of vitellogenin.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC   -!- GENE_FAMILY: HOG000197681 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Aedes_aegypti;AAEL006169;AAEL006169-RA;AAEL006169-PA.
DR   EMBL; CH477377; - ;
DR   EMBL; M95187; - ;
DR   UniProtKB/Swiss-Prot; Q03168; Q177E0; -.
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   UniGene; Aae.18587; -.
DR   ProteinModelPortal; Q03168; -.
DR   SMR; Q03168; 54-386.
DR   STRING; Q03168; -.
DR   MEROPS; A01.009; -.
DR   Siena-2DPAGE; Q03168; -.
DR   EnsemblMetazoa; AAEL006169-RA; AAEL006169-PA; AAEL006169.
DR   GeneID; 5567565; -.
DR   KEGG; aag:AaeL_AAEL006169; -.
DR   eggNOG; inNOG06901; -.
DR   GeneTree; EMGT00050000005383; -.
DR   InParanoid; Q03168; -.
DR   OMA; SGFMGID; -.
DR   OrthoDB; EOG4573P1; -.
DR   PhylomeDB; Q03168; -.
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:InterPro.
DR   InterPro; IPR001461; Peptidase_A1.
DR   InterPro; IPR021109; Peptidase_aspartic.
DR   InterPro; IPR001969; Peptidase_aspartic_AS.
DR   InterPro; IPR009007; Peptidase_aspartic_catalytic.
DR   InterPro; IPR012848; Propep_A1.
DR   Gene3D; G3DSA:2.40.70.10; Pept_Aspartc_cat; 2.
DR   PANTHER; PTHR13683; Peptidase_A1; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Pept_Aspartic; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   HOGENOMDNA; AEDAE_1024.PE9; -.
KW   AAEL0061693; AAEL006169-PA ; Q03168; CH477377; M95187;
KW   Aspartyl protease; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hydrolase; Lysosome; Protease; Signal; Zymogen.
SQ   SEQUENCE   387 AA;  UNKNOWN MW;  UNKNOWN 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
//

If you have problems or comments...

PBIL Back to PBIL home page