DIAP_GASAT
ID DIAP_GASAT Reviewed; 65 AA.
AC Q8T0W8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Diapause-specific peptide;
DE Short=DSP;
DE AltName: Full=Diapausin;
DE Flags: Precursor;
OS Gastrophysa atrocyanea (Leaf beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Gastrophysa.
OX NCBI_TaxID=169758;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-65, FUNCTION,
RP DEVELOPMENTAL STAGE, AND DISULFIDE BOND.
RX PubMed=14706547; DOI=10.1016/j.peptides.2003.07.021;
RA Tanaka H., Sato K., Saito Y., Yamashita T., Agoh M., Okunishi J.,
RA Tachikawa E., Suzuki K.;
RT "Insect diapause-specific peptide from the leaf beetle has consensus with a
RT putative iridovirus peptide.";
RL Peptides 24:1327-1333(2003).
RN [2]
RP PROTEIN SEQUENCE OF 25-60, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MASS SPECTROMETRY.
RA Tanaka H., Sudo C., An Y., Yamashita T., Sato K., Kurihara M., Suzuki K.;
RT "Relationship between the introduced and indigenous parasitoids Torymus
RT sinensis and T. beneficus (Hymenoptera: Torymidae), as inferred from mt-DNA
RT (COI) sequences.";
RL Appl. Entomol. Zool. (Jpn.) 33:535-543(1998).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=15936770; DOI=10.1016/j.jinsphys.2005.03.018;
RA Tanaka H., Suzuki K.;
RT "Expression profiling of a diapause-specific peptide (DSP) of the leaf
RT beetle Gastrophysa atrocyanea and silencing of DSP by double-strand RNA.";
RL J. Insect Physiol. 51:701-707(2005).
RN [4]
RP STRUCTURE BY NMR OF 25-65, AND DISULFIDE BONDS.
RX PubMed=17994764; DOI=10.1021/bi701319t;
RA Kouno T., Mizuguchi M., Tanaka H., Yang P., Mori Y., Shinoda H., Unoki K.,
RA Aizawa T., Demura M., Suzuki K., Kawano K.;
RT "The structure of a novel insect peptide explains its Ca(2+) channel
RT blocking and antifungal activities.";
RL Biochemistry 46:13733-13741(2007).
CC -!- FUNCTION: Has antifungal activity against T.rubrum. Blocks voltage-
CC dependent N-type calcium channels (Cav2.2 / CACNA1B).
CC {ECO:0000269|PubMed:14706547}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the fat body.
CC {ECO:0000269|Ref.2}.
CC -!- DEVELOPMENTAL STAGE: Produced throughout adult diapause, and to a minor
CC extent in pupae, but not in eggs, larvae, or post-diapausing adults.
CC Inhibition of DSP expression does not affect the onset or maintenance
CC of diapause, indicating that the expression of DSP accompanies but does
CC not play a direct role in the induction or maintenance of diapause.
CC {ECO:0000269|PubMed:14706547, ECO:0000269|PubMed:15936770}.
CC -!- MASS SPECTROMETRY: Mass=4466.3; Method=MALDI;
CC Evidence={ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the diapausin family. {ECO:0000305}.
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DR EMBL; AB070558; BAB88222.1; -; mRNA.
DR PDB; 2CDX; NMR; -; A=25-65.
DR PDB; 2E2F; NMR; -; A=25-65.
DR PDBsum; 2CDX; -.
DR PDBsum; 2E2F; -.
DR AlphaFoldDB; Q8T0W8; -.
DR BMRB; Q8T0W8; -.
DR SMR; Q8T0W8; -.
DR EvolutionaryTrace; Q8T0W8; -.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.120; -; 1.
DR InterPro; IPR038203; Diapausin_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Calcium channel impairing toxin;
KW Direct protein sequencing; Disulfide bond; Fungicide;
KW Ion channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:14706547, ECO:0000269|Ref.2"
FT CHAIN 25..65
FT /note="Diapause-specific peptide"
FT /id="PRO_0000007217"
FT DISULFID 31..45
FT /evidence="ECO:0000269|PubMed:17994764"
FT DISULFID 35..57
FT /evidence="ECO:0000269|PubMed:17994764"
FT DISULFID 46..64
FT /evidence="ECO:0000269|PubMed:17994764"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:2E2F"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2E2F"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:2E2F"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2E2F"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2E2F"
SQ SEQUENCE 65 AA; 6939 MW; 72BC929D4AA31A42 CRC64;
MGAALKMTIF LLIVACAMIA TTEAAVRIGP CDQVCPRIVP ERHECCRAHG RSGYAYCSGG
GMYCN
