ALLS_DROME
ID ALLS_DROME Reviewed; 151 AA.
AC Q9VC44; Q9NB67;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Allatostatin-A;
DE AltName: Full=Allatostatins Ast;
DE Contains:
DE RecName: Full=Drostatin-1;
DE AltName: Full=AST-A1 {ECO:0000303|PubMed:21214272};
DE Contains:
DE RecName: Full=Drostatin-2;
DE AltName: Full=AST-A2(14-21) {ECO:0000303|PubMed:21214272};
DE Contains:
DE RecName: Full=Drostatin-3;
DE AltName: Full=AST-A3 {ECO:0000303|PubMed:21214272};
DE Contains:
DE RecName: Full=Drostatin-4;
DE AltName: Full=AST-A4 {ECO:0000303|PubMed:21214272};
DE Contains:
DE RecName: Full=Drostatin-5;
DE AltName: Full=AST-A2(1-11) {ECO:0000303|PubMed:21214272};
DE Flags: Precursor;
GN Name=AstA; Synonyms=Ast; ORFNames=CG13633;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S;
RX PubMed=10891383; DOI=10.1006/bbrc.2000.3062;
RA Lenz C., Williamson M., Grimmelikhuijzen C.J.P.;
RT "Molecular cloning and genomic organization of an Allatostatin
RT preprohormone from Drosophila melanogaster.";
RL Biochem. Biophys. Res. Commun. 273:1126-1131(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PROTEIN SEQUENCE OF 57-64; 68-78; 81-88; 92-99 AND 138-148, IDENTIFICATION
RP BY MASS SPECTROMETRY, MASS SPECTROMETRY, AND AMIDATION AT LEU-64; LEU-88;
RP LEU-99 AND LEU-148.
RC TISSUE=Midgut {ECO:0000303|PubMed:21214272};
RX PubMed=21214272; DOI=10.1021/pr101116g;
RA Reiher W., Shirras C., Kahnt J., Baumeister S., Isaac R.E., Wegener C.;
RT "Peptidomics and peptide hormone processing in the Drosophila midgut.";
RL J. Proteome Res. 10:1881-1892(2011).
RN [6]
RP PROTEIN SEQUENCE OF 68-78; 92-99 AND 138-148, AND AMIDATION.
RC TISSUE=Larva;
RX PubMed=12171930; DOI=10.1074/jbc.m206257200;
RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.;
RT "Peptidomics of the larval Drosophila melanogaster central nervous
RT system.";
RL J. Biol. Chem. 277:40368-40374(2002).
CC -!- FUNCTION: May act as a neurotransmitter or neuromodulator.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- MASS SPECTROMETRY: [Drostatin-1]: Mass=953.52; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [Drostatin-5]: Mass=1161.47; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [Drostatin-2]: Mass=921.52; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [Drostatin-3]: Mass=925.49; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [Drostatin-4]: Mass=1276.68; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21214272};
CC -!- SIMILARITY: Belongs to the allatostatin family. {ECO:0000305}.
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DR EMBL; AF263923; AAF97792.1; -; mRNA.
DR EMBL; AE014297; AAF56331.1; -; Genomic_DNA.
DR EMBL; AY071110; AAL48732.1; -; mRNA.
DR PIR; JC7325; JC7325.
DR RefSeq; NP_001287511.1; NM_001300582.1.
DR RefSeq; NP_524489.2; NM_079765.3.
DR AlphaFoldDB; Q9VC44; -.
DR STRING; 7227.FBpp0084119; -.
DR PaxDb; Q9VC44; -.
DR PRIDE; Q9VC44; -.
DR DNASU; 42947; -.
DR EnsemblMetazoa; FBtr0084744; FBpp0084119; FBgn0015591.
DR EnsemblMetazoa; FBtr0346367; FBpp0312068; FBgn0015591.
DR GeneID; 42947; -.
DR KEGG; dme:Dmel_CG13633; -.
DR UCSC; CG13633-RA; d. melanogaster.
DR CTD; 42947; -.
DR FlyBase; FBgn0015591; AstA.
DR VEuPathDB; VectorBase:FBgn0015591; -.
DR eggNOG; ENOG502SDVK; Eukaryota.
DR HOGENOM; CLU_1715176_0_0_1; -.
DR InParanoid; Q9VC44; -.
DR OMA; RMERYAF; -.
DR OrthoDB; 1309198at2759; -.
DR PhylomeDB; Q9VC44; -.
DR BioGRID-ORCS; 42947; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42947; -.
DR PRO; PR:Q9VC44; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0015591; Expressed in adult hindgut (Drosophila) and 20 other tissues.
DR ExpressionAtlas; Q9VC44; baseline and differential.
DR Genevisible; Q9VC44; DM.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0005179; F:hormone activity; NAS:FlyBase.
DR GO; GO:0005184; F:neuropeptide hormone activity; NAS:FlyBase.
DR GO; GO:0071855; F:neuropeptide receptor binding; IPI:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; NAS:UniProtKB.
DR GO; GO:0045968; P:negative regulation of juvenile hormone biosynthetic process; NAS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR InterPro; IPR010276; Allatostatin.
DR Pfam; PF05953; Allatostatin; 4.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..54
FT /id="PRO_0000001147"
FT PEPTIDE 57..64
FT /note="Drostatin-1"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000001148"
FT PEPTIDE 68..78
FT /note="Drostatin-5"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000001149"
FT PEPTIDE 81..88
FT /note="Drostatin-2"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000001150"
FT PEPTIDE 92..99
FT /note="Drostatin-3"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000001151"
FT PROPEP 103..135
FT /id="PRO_0000001152"
FT PEPTIDE 138..148
FT /note="Drostatin-4"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000001153"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:21214272"
FT MOD_RES 88
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:21214272"
FT MOD_RES 99
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:12171930,
FT ECO:0000269|PubMed:21214272"
FT MOD_RES 148
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:12171930,
FT ECO:0000269|PubMed:21214272"
FT CONFLICT 9
FT /note="L -> I (in Ref. 1; AAF97792)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="C -> G (in Ref. 1; AAF97792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 151 AA; 16852 MW; 1EC8A90494184C96 CRC64;
MNSLHAHLLL LAVCCVGYIA SSPVIGQDQR SGDSDADVLL AADEMADNGG DNIDKRVERY
AFGLGRRAYM YTNGGPGMKR LPVYNFGLGK RSRPYSFGLG KRSDYDYDQD NEIDYRVPPA
NYLAAERAVR PGRQNKRTTR PQPFNFGLGR R
