VCP_AEDAE
ID VCP_AEDAE Reviewed; 471 AA.
AC P42660; Q175U2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Vitellogenic carboxypeptidase;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=VCP; ORFNames=AAEL006563;
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], PROTEIN SEQUENCE OF 20-36, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC TISSUE=Fat body;
RX PubMed=1961751; DOI=10.1073/pnas.88.23.10821;
RA Cho W.-L., Deitsch K.W., Raikhel A.S.;
RT "An extraovarian protein accumulated in mosquito oocytes is a
RT carboxypeptidase activated in embryos.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10821-10824(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ugals;
RX PubMed=9087558; DOI=10.1111/j.1365-2583.1994.tb00140.x;
RA Deitsch K.W., Raikhel A.S.;
RT "Cloning and analysis of the locus for mosquito vitellogenic
RT carboxypeptidase.";
RL Insect Mol. Biol. 2:205-213(1993).
RN [3]
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).
CC -!- FUNCTION: May play a role in activating hydrolytic enzymes that are
CC involved in the degradation of yolk proteins in developing embryos or
CC may function as an exopeptidase in the degradation of vitellogenin.
CC {ECO:0000269|PubMed:1961751}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1961751}.
CC -!- TISSUE SPECIFICITY: Synthesized in the fat body of vitellogenic
CC females, secreted into the hemolymph and accumulates in yolk bodies of
CC developing oocytes. {ECO:0000269|PubMed:1961751}.
CC -!- DEVELOPMENTAL STAGE: Maximally present at the middle of embryonic
CC development and disappears by the end. {ECO:0000269|PubMed:1961751}.
CC -!- INDUCTION: By 20-hydroxyecdysone. {ECO:0000269|PubMed:1961751}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17682.1; Type=Frameshift; Note=Lacks the last active site residue.; Evidence={ECO:0000305};
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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 AlphaFoldDB; P42660; -.
DR SMR; P42660; -.
DR STRING; 7159.AAEL006563-PA; -.
DR ESTHER; aedae-vcp; Carboxypeptidase_S10.
DR MEROPS; S10.003; -.
DR GeneID; 5568117; -.
DR KEGG; aag:5568117; -.
DR VEuPathDB; VectorBase:AAEL006563; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_1_1; -.
DR InParanoid; P42660; -.
DR OMA; NCYVEMD; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; P42660; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
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:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1961751"
FT CHAIN 20..471
FT /note="Vitellogenic carboxypeptidase"
FT /id="PRO_0000004336"
FT ACT_SITE 207
FT /evidence="ECO:0000250"
FT ACT_SITE 391
FT /evidence="ECO:0000250"
FT ACT_SITE 448
FT /evidence="ECO:0000250"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="R -> P (in Ref. 2; AAC41580)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="K -> N (in Ref. 1; AAA17682)"
FT /evidence="ECO:0000305"
FT CONFLICT 284..285
FT /note="KC -> NS (in Ref. 2; AAC41580)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 53766 MW; 91FD6331DD156472 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
