V15A2_AEDAE
ID V15A2_AEDAE Reviewed; 97 AA.
AC P19425; Q26291; Q7JPT3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Vitelline membrane protein 15a-2;
DE Contains:
DE RecName: Full=Trypsin-modulating oostatic factor;
DE Short=TMOF;
DE AltName: Full=OOSH;
DE Flags: Precursor;
GN Name=15a-2;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Rockefeller;
RX PubMed=9887508; DOI=10.1016/s0965-1748(98)00083-6;
RA Edwards M.J., Severson D.W., Hagedorn H.H.;
RT "Vitelline envelope genes of the yellow fever mosquito, Aedes aegypti.";
RL Insect Biochem. Mol. Biol. 28:915-925(1998).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 6-97, AND DEVELOPMENTAL STAGE.
RX PubMed=8432405; DOI=10.1006/dbio.1993.1052;
RA Lin Y., Hamblin M.T., Edwards M.J., Barillas-Mury C., Kanost M.R.,
RA Knipple D.C., Wolfner M.F., Hagedorn H.H.;
RT "Structure, expression, and hormonal control of genes from the mosquito,
RT Aedes aegypti, which encode proteins similar to the vitelline membrane
RT proteins of Drosophila melanogaster.";
RL Dev. Biol. 155:558-568(1993).
RN [4]
RP PROTEIN SEQUENCE OF 20-29, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND MASS SPECTROMETRY.
RC STRAIN=Vero beach; TISSUE=Ovary;
RX PubMed=2394318; DOI=10.1096/fasebj.4.12.2394318;
RA Borovsky D., Carlson D.A., Griffin P.R., Shabanowitz J., Hunt D.F.;
RT "Mosquito oostatic factor: a novel decapeptide modulating trypsin-like
RT enzyme biosynthesis in the midgut.";
RL FASEB J. 4:3015-3020(1990).
RN [5]
RP PROTEIN SEQUENCE OF 20-29, FUNCTION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Vero beach; TISSUE=Ovary;
RX PubMed=8353526; DOI=10.1016/0965-1748(93)90044-s;
RA Borovsky D., Carlson D.A., Griffin P.R., Shabanowitz J., Hunt D.F.;
RT "Mass spectrometry and characterization of Aedes aegypti trypsin modulating
RT oostatic factor (TMOF) and its analogs.";
RL Insect Biochem. Mol. Biol. 23:703-712(1993).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 20-ASP--TYR-21.
RX PubMed=14506222; DOI=10.1242/jeb.00602;
RA Borovsky D.;
RT "Trypsin-modulating oostatic factor: a potential new larvicide for mosquito
RT control.";
RL J. Exp. Biol. 206:3869-3875(2003).
RN [7]
RP STRUCTURE BY NMR OF 20-29.
RX PubMed=8512567; DOI=10.1006/bbrc.1993.1679;
RA Curto E.V., Jarpe M.A., Blalock J.E., Borovsky D., Krishna N.R.;
RT "Solution structure of trypsin modulating oostatic factor is a left-handed
RT helix.";
RL Biochem. Biophys. Res. Commun. 193:688-693(1993).
CC -!- FUNCTION: Has an oostatic activity. Inhibits trypsin biosynthesis in
CC the midgut epithelial cells which indirectly reduces the vitellogenin
CC concentration in the hemolymph resulting in inhibition of oocyte
CC development. {ECO:0000269|PubMed:14506222, ECO:0000269|PubMed:2394318,
CC ECO:0000269|PubMed:8353526}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14506222,
CC ECO:0000269|PubMed:2394318}. Note=Secreted from the ovary, starting 18
CC hours after a blood meal, circulates in the hemolymph.
CC -!- TISSUE SPECIFICITY: Expressed in the anterior region of the follicle
CC cells. {ECO:0000269|PubMed:9887508}.
CC -!- DEVELOPMENTAL STAGE: Synthesized and released from follicular
CC epithelium 18-24 hours after a blood meal. Synthesis peaks at 36 hours
CC and stops at 56 hours. {ECO:0000269|PubMed:14506222,
CC ECO:0000269|PubMed:2394318, ECO:0000269|PubMed:8432405,
CC ECO:0000269|PubMed:9887508}.
CC -!- MASS SPECTROMETRY: [Trypsin-modulating oostatic factor]: Mass=1047.6;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:2394318};
CC -!- MISCELLANEOUS: Can potentially be used as a larvicide. The stable
CC three-dimensional conformation of the decapeptide means it is not
CC degraded by gut proteolytic enzymes and can traverse the gut epithelial
CC cells into the hemolymph of adults and larvae. Hormone fed to different
CC species of mosquito larvae stops food digestion and causes larval
CC mortality. The tetrapeptide (DYPA) is as effective as the decapeptide.
CC -!- SIMILARITY: Belongs to the vitelline membrane protein family.
CC {ECO:0000305}.
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DR EMBL; U91681; AAB51283.1; -; Genomic_DNA.
DR EMBL; CH477949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S54556; AAB25307.1; -; mRNA.
DR PIR; A36454; A36454.
DR PIR; B48831; B48831.
DR RefSeq; XP_011493693.1; XM_011495391.1.
DR AlphaFoldDB; P19425; -.
DR STRING; 7159.AAEL017403-PA; -.
DR GeneID; 23687823; -.
DR KEGG; aag:23687823; -.
DR VEuPathDB; VectorBase:AAEL017403; -.
DR HOGENOM; CLU_2348359_0_0_1; -.
DR Proteomes; UP000008820; Chromosome 2.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IMP:UniProtKB.
DR GO; GO:0048599; P:oocyte development; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2394318,
FT ECO:0000269|PubMed:8353526"
FT CHAIN 20..97
FT /note="Vitelline membrane protein 15a-2"
FT /id="PRO_0000343657"
FT PEPTIDE 20..29
FT /note="Trypsin-modulating oostatic factor"
FT /id="PRO_0000044226"
FT DOMAIN 61..97
FT /note="VM"
FT REGION 20..23
FT /note="Required for binding to the gut receptor"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 20..21
FT /note="DY->YD: In TMOF(A); increased hormone activity."
FT /evidence="ECO:0000269|PubMed:14506222"
FT CONFLICT 78
FT /note="S -> A (in Ref. 3; AAB25307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 97 AA; 10047 MW; 49F9C51A7B56BD29 CRC64;
MNKIIAALVL FTAVIGALAD YPAPPPPPPK PYHAPPPPPY HAPPHHAPAP LHPVVHTYPV
KAPAAKCGAN LLVGCAPSVA HVPCVPVHPH PPPPAHY
