(data stored in ACNUC30567 zone)

HOGENOM: AEDAE_1225_PE27

ID   AEDAE_1225_PE27                      STANDARD;      PRT;   471 AA.
AC   AEDAE_1225_PE27; P42660; Q175U2;
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=Vitellogenic carboxypeptidase; EC=3.4.16 -;Flags:
DE   Precursor; (AEDAE_1225.PE27).
GN   Name=VCP; ORFNames=AAEL006563;
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_1225.PE27.
CC       Aedes aegypti supercontig supercont1.210 AaegL1  sequence 1..2048554
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:VCP_AEDAE
CC   -!- FUNCTION: May play a role in activating hydrolytic enzymes that
CC       are involved in the degradation of yolk proteins in developing
CC       embryos or may function as an exopeptidase in the degradation of
CC       vitellogenin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Synthesized in the fat body of vitellogenic
CC       females, secreted into the hemolymph and accumulates in yolk
CC       bodies of developing oocytes.
CC   -!- DEVELOPMENTAL STAGE: Maximally present at the middle of embryonic
CC       development and disappears by the end.
CC   -!- INDUCTION: By 20-hydroxyecdysone.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17682.1; Type=Frameshift; Positions=426; Note=Lacks the last active site residue;
CC   -!- GENE_FAMILY: HOG000252949 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Aedes_aegypti;AAEL006563;AAEL006563-RA;AAEL006563-PA.
DR   EMBL; CH477395; - ;
DR   EMBL; L46594; - ;
DR   EMBL; M79452; - ;
DR   UniProtKB/Swiss-Prot; P42660; Q175U2; -.
DR   EMBL; M79452; AAA17682.1; ALT_FRAME; mRNA.
DR   EMBL; L46594; AAC41580.1; -; Genomic_DNA.
DR   EMBL; CH477395; EAT41863.1; -; Genomic_DNA.
DR   PIR; A41612; A41612.
DR   RefSeq; XP_001652056.1; XM_001652006.1.
DR   UniGene; Aae.26090; -.
DR   UniGene; Aae.5325; -.
DR   ProteinModelPortal; P42660; -.
DR   MEROPS; S10.003; -.
DR   EnsemblMetazoa; AAEL006563-RA; AAEL006563-PA; AAEL006563.
DR   GeneID; 5568117; -.
DR   KEGG; aag:AaeL_AAEL006563; -.
DR   eggNOG; meNOG06562; -.
DR   GeneTree; EMGT00050000002403; -.
DR   InParanoid; P42660; -.
DR   OMA; TESEEGY; -.
DR   OrthoDB; EOG4RN8SH; -.
DR   PhylomeDB; P42660; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Peptidase_S10_AS.
DR   PANTHER; PTHR11802; Peptidase_S10; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
DR   HOGENOMDNA; AEDAE_1225.PE27; -.
KW   AAEL0065633; AAEL006563-PA ; P42660; CH477395; L46594; M79452;
KW   Carboxypeptidase; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Signal.
SQ   SEQUENCE   471 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVKFHLLVLI AFTCYTCSDA TLWNPYKKLM RGSASPRRPG ESGEPLFLTP LLQDGKIEEA
     RNKARVNHPM LSSVESYSGF MTVDAKHNSN LFFWYVPAKN NREQAPILVW LQGGPGASSL
     FGMFEENGPF HIHRNKSVKQ REYSWHQNHH MIYIDNPVGT GFSFTDSDEG YSTNEEHVGE
     NLMKFIQQFF VLFPNLLKHP FYISGESYGG KFVPAFGYAI HNSQSQPKIN LQGLAIGDGY
     TDPLNQLNYG EYLYELGLID LNGRKKFDED TAAAIACAER KDMKCANRLI QGLFDGLDGQ
     ESYFKKVTGF SSYYNFIKGD EESKQDSVLM EFLSNPEVRK GIHVGELPFH DSDGHNKVAE
     MLSEDTLDTV APWVSKLLSH YRVLFYNGQL DIICAYPMTV DFLMKMPFDG DSEYKRANRE
     IYRVDGEIAG YKKRAGRLQE VLIRNAGHMV PRDQPKWAFD MITSFTHKNY L
//

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