ALLS_DIPPU
ID ALLS_DIPPU Reviewed; 370 AA.
AC P12764; P12765; P12766; P12767; P22410;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Allatostatins;
DE Contains:
DE RecName: Full=Allatostatin-1;
DE Short=AST1;
DE Contains:
DE RecName: Full=Allatostatin-2;
DE Short=AST2;
DE AltName: Full=ASA5;
DE AltName: Full=ASB2;
DE Contains:
DE RecName: Full=Allatostatin-3;
DE Short=AST3;
DE Contains:
DE RecName: Full=Allatostatin-4;
DE Short=AST4;
DE AltName: Full=ASA7;
DE Contains:
DE RecName: Full=Allatostatin-5;
DE Short=AST5;
DE AltName: Full=ASA4;
DE Contains:
DE RecName: Full=Allatostatin-6;
DE Short=AST6;
DE Contains:
DE RecName: Full=Allatostatin-7;
DE Short=AST7;
DE AltName: Full=ASA1;
DE Contains:
DE RecName: Full=Allatostatin-8;
DE Short=AST8;
DE AltName: Full=ASA3;
DE Contains:
DE RecName: Full=Allatostatin-9;
DE Short=AST9;
DE AltName: Full=ASA2;
DE Contains:
DE RecName: Full=Allatostatin-10;
DE Short=AST10;
DE Contains:
DE RecName: Full=Allatostatin-11;
DE Short=AST11;
DE AltName: Full=ASA6;
DE Contains:
DE RecName: Full=Allatostatin-12;
DE Short=AST12;
DE Contains:
DE RecName: Full=Allatostatin-13;
DE Short=AST13;
DE Flags: Precursor;
OS Diploptera punctata (Pacific beetle cockroach).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blaberidae;
OC Diplopterinae; Diploptera.
OX NCBI_TaxID=6984;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT LEU-73; LEU-94; LEU-105;
RP LEU-117; LEU-161; LEU-172; LEU-188; LEU-200; LEU-213; LEU-232; LEU-264;
RP LEU-353 AND ILE-364.
RC TISSUE=Brain;
RX PubMed=8415611; DOI=10.1073/pnas.90.19.8807;
RA Donly B.C., Ding Q., Tobe S.S., Bendena W.G.;
RT "Molecular cloning of the gene for the allatostatin family of neuropeptides
RT from the cockroach Diploptera punctata.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8807-8811(1993).
RN [2]
RP PROTEIN SEQUENCE OF 154-161; 176-188; 192-200 AND 204-213.
RC TISSUE=Brain;
RX PubMed=2762309; DOI=10.1073/pnas.86.15.5997;
RA Woodhead A.P., Stay B., Seidel S.L., Khan M.A., Tobe S.S.;
RT "Primary structure of four allatostatins: neuropeptide inhibitors of
RT juvenile hormone synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5997-6001(1989).
RN [3]
RP PROTEIN SEQUENCE OF 77-94.
RC TISSUE=Brain;
RX PubMed=2006179; DOI=10.1073/pnas.88.6.2412;
RA Pratt G.E., Farnsworth D.E., Fok K.F., Siegel N.R., McCormack A.L.,
RA Shabanowitz J., Hunt D.F., Feyereisen R.;
RT "Identity of a second type of allatostatin from cockroach brains: an
RT octadecapeptide amide with a tyrosine-rich address sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2412-2416(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 77-189.
RX PubMed=7991553; DOI=10.1073/pnas.91.25.11894;
RA Reichwald K., Unnithan G.C., Davis N.T., Agricola H., Feyereisen R.;
RT "Expression of the allatostatin gene in endocrine cells of the cockroach
RT midgut.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11894-11898(1994).
RN [5]
RP PROTEIN SEQUENCE OF 176-188 (AST7), AND AMIDATION AT LEU-188.
RC TISSUE=Brain;
RX PubMed=2783135; DOI=10.1016/0006-291x(89)91111-x;
RA Pratt G.E., Farnsworth D.E., Siegel N.R., Fok K.F., Feyereisen R.;
RT "Identification of an allatostatin from adult Diploptera punctata.";
RL Biochem. Biophys. Res. Commun. 163:1243-1247(1989).
RN [6]
RP STRUCTURE BY NMR OF 154-161 AND 192-200, FUNCTION, AND AMIDATION AT LEU-161
RP AND LEU-200.
RX PubMed=18191874; DOI=10.1016/j.peptides.2007.11.016;
RA Banerjee M., Meyerowitz E., Huang C., Mohanty S.;
RT "Probing the conformation and dynamics of allatostatin neuropeptides: a
RT structural model for functional differences.";
RL Peptides 29:375-385(2008).
CC -!- FUNCTION: Neuropeptide inhibitors of juvenile hormone synthesis and gut
CC muscle contraction. {ECO:0000269|PubMed:18191874}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Brain, subesophageal ganglion and corpus allatum.
CC -!- SIMILARITY: Belongs to the allatostatin family. {ECO:0000305}.
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DR EMBL; U00444; AAA18260.1; -; mRNA.
DR EMBL; S74578; AAB32720.2; -; mRNA.
DR PIR; A48252; A48252.
DR PDB; 2JQS; NMR; -; A=154-161.
DR PDB; 2JQU; NMR; -; A=192-200.
DR PDBsum; 2JQS; -.
DR PDBsum; 2JQU; -.
DR AlphaFoldDB; P12764; -.
DR SMR; P12764; -.
DR EvolutionaryTrace; P12764; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR010276; Allatostatin.
DR Pfam; PF05953; Allatostatin; 13.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Neuropeptide; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..65
FT /id="PRO_0000001129"
FT PEPTIDE 68..73
FT /note="Allatostatin-1"
FT /id="PRO_0000001130"
FT PEPTIDE 77..94
FT /note="Allatostatin-2"
FT /id="PRO_0000001131"
FT PEPTIDE 98..105
FT /note="Allatostatin-3"
FT /id="PRO_0000001132"
FT PEPTIDE 109..117
FT /note="Allatostatin-4"
FT /id="PRO_0000001133"
FT PROPEP 121..151
FT /id="PRO_0000001134"
FT PEPTIDE 154..161
FT /note="Allatostatin-5"
FT /id="PRO_0000001135"
FT PEPTIDE 165..172
FT /note="Allatostatin-6"
FT /id="PRO_0000001136"
FT PEPTIDE 176..188
FT /note="Allatostatin-7"
FT /id="PRO_0000001137"
FT PEPTIDE 192..200
FT /note="Allatostatin-8"
FT /id="PRO_0000001138"
FT PEPTIDE 204..213
FT /note="Allatostatin-9"
FT /id="PRO_0000001139"
FT PEPTIDE 217..232
FT /note="Allatostatin-10"
FT /id="PRO_0000001140"
FT PROPEP 236..251
FT /id="PRO_0000001141"
FT PEPTIDE 254..264
FT /note="Allatostatin-11"
FT /id="PRO_0000001142"
FT PROPEP 268..345
FT /id="PRO_0000001143"
FT PEPTIDE 348..353
FT /note="Allatostatin-12"
FT /id="PRO_0000001144"
FT PEPTIDE 357..364
FT /note="Allatostatin-13"
FT /id="PRO_0000001145"
FT PROPEP 368..370
FT /id="PRO_0000001146"
FT REGION 29..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8415611"
FT MOD_RES 94
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8415611"
FT MOD_RES 105
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8415611"
FT MOD_RES 117
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8415611"
FT MOD_RES 161
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:18191874,
FT ECO:0000269|PubMed:8415611"
FT MOD_RES 172
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8415611"
FT MOD_RES 188
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:2783135,
FT ECO:0000269|PubMed:8415611"
FT MOD_RES 200
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:18191874,
FT ECO:0000269|PubMed:8415611"
FT MOD_RES 213
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8415611"
FT MOD_RES 232
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8415611"
FT MOD_RES 264
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8415611"
FT MOD_RES 353
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8415611"
FT MOD_RES 364
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:8415611"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2JQS"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:2JQU"
SQ SEQUENCE 370 AA; 41562 MW; A5AA8E7C13DE8ED9 CRC64;
MSGPRTCFCL PSALVLVLLS LSTSALGTAP EPSGVHEESP AGGGTDLLPH PEDLSASDNP
DLEFVKRLYD FGLGKRAYSY VSEYKRLPVY NFGLGKRSKM YGFGLGKRDG RMYSFGLGKR
DYDYYGEEDE DDQQAIGDED IEESDVGDLM DKRDRLYSFG LGKRARPYSF GLGKRAPSGA
QRLYGFGLGK RGGSLYSFGL GKRGDGRLYA FGLGKRPVNS GRSSGSRFNF GLGKRSDDID
FRELEEKFAE DKRYPQEHRF SFGLGKREVE PSELEAVRNE EKDNSSVHDK KNNTNDMHSG
ERIKRSLHYP FGIRKLESSY DLNSASSLNS EENDDITPEE FSRMVRRPFN FGLGKRIPMY
DFGIGKRSER
