GBP_MYTSE
ID GBP_MYTSE Reviewed; 145 AA.
AC Q27913; Q9TWE7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Growth-blocking peptide, long form;
DE Short=GBP;
DE Contains:
DE RecName: Full=Growth-blocking peptide, short form;
DE Flags: Precursor;
OS Mythimna separata (Oriental armyworm) (Pseudaletia separata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Hadeninae; Mythimna.
OX NCBI_TaxID=271217;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (SHORT FORM), AND TISSUE SPECIFICITY.
RX PubMed=7498538; DOI=10.1016/0014-5793(95)01273-7;
RA Hayakawa Y., Ohnishi A., Yamanaka A., Izumi S., Tomino S.;
RT "Molecular cloning and characterization of cDNA for insect biogenic
RT peptide, growth-blocking peptide.";
RL FEBS Lett. 376:185-189(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (SHORT FORM).
RX PubMed=9654083; DOI=10.1046/j.1432-1327.1998.2530810.x;
RA Hayakawa Y., Noguchi H.;
RT "Growth-blocking peptide expressed in the insect nervous system -- cloning
RT and functional characterization.";
RL Eur. J. Biochem. 253:810-816(1998).
RN [3]
RP PROTEIN SEQUENCE OF 121-145.
RX PubMed=2022627; DOI=10.1016/s0021-9258(18)92927-3;
RA Hayakawa Y.;
RT "Structure of a growth-blocking peptide present in parasitized insect
RT hemolymph.";
RL J. Biol. Chem. 266:7982-7984(1991).
RN [4]
RP PROTEIN SEQUENCE OF 121-145, AND SYNTHESIS.
RX PubMed=12182821; DOI=10.1016/s1046-5928(02)00036-0;
RA Koganesawa N., Aizawa T., Shimojo H., Miura K., Ohnishi A., Demura M.,
RA Hayakawa Y., Nitta K., Kawano K.;
RT "Expression and purification of a small cytokine growth-blocking peptide
RT from armyworm Pseudaletia separata by an optimized fermentation method
RT using the methylotrophic yeast Pichia pastoris.";
RL Protein Expr. Purif. 25:416-425(2002).
RN [5]
RP PROTEIN SEQUENCE OF 121-143, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=8580912; DOI=10.1016/0965-1748(95)00054-2;
RA Ohnishi A., Hayakawa Y., Matsuda Y., Kwon K.-W., Takahashi T.A.,
RA Sekiguchi S.;
RT "Growth-blocking peptide titer during larval development of parasitized and
RT cold-stressed armyworm.";
RL Insect Biochem. Mol. Biol. 25:1121-1127(1995).
RN [6]
RP FUNCTION.
RX PubMed=9753606; DOI=10.1006/bbrc.1998.8959;
RA Hayakawa Y., Ohnishi A.;
RT "Cell growth activity of growth-blocking peptide.";
RL Biochem. Biophys. Res. Commun. 250:194-199(1998).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10928276; DOI=10.1007/s004419900152;
RA Hayakawa Y., Ohnishi A., Mizoguchi A., Yamashika C.;
RT "Distribution of growth-blocking peptide in the insect central nervous
RT tissue.";
RL Cell Tissue Res. 300:459-464(2000).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLU-121; ASP-136; THR-142 AND PHE-143.
RX PubMed=11429413; DOI=10.1074/jbc.m105251200;
RA Aizawa T., Hayakawa Y., Ohnishi A., Fujitani N., Clark K.D., Strand M.R.,
RA Miura K., Koganesawa N., Kumaki Y., Demura M., Nitta K., Kawano K.;
RT "Structure and activity of the insect cytokine growth-blocking peptide.
RT Essential regions for mitogenic and hemocyte-stimulating activities are
RT separate.";
RL J. Biol. Chem. 276:31813-31818(2001).
RN [9]
RP MUTAGENESIS OF GLY-125 AND GLY-126.
RX PubMed=15385535; DOI=10.1074/jbc.m409382200;
RA Yoshida M., Aizawa T., Nakamura T., Shitara K., Hayakawa Y., Matsubara K.,
RA Miura K., Kouno T., Clark K.D., Strand M.R., Mizuguchi M., Demura M.,
RA Nitta K., Kawano K.;
RT "The Gly-Gly linker region of the insect cytokine growth-blocking peptide
RT is essential for activity.";
RL J. Biol. Chem. 279:51331-51337(2004).
RN [10]
RP STRUCTURE BY NMR OF 121-145.
RC TISSUE=Hemolymph;
RX PubMed=9890941; DOI=10.1074/jbc.274.4.1887;
RA Aizawa T., Fujitani N., Hayakawa Y., Ohnishi A., Ohkubo T., Kumaki Y.,
RA Kawano K., Hikichi K., Nitta K.;
RT "Solution structure of an insect growth factor, growth-blocking peptide.";
RL J. Biol. Chem. 274:1887-1890(1999).
CC -!- FUNCTION: Biogenic peptide that prevents the onset of metamorphosis
CC from larva to pupa. Has repressive activity against juvenile hormone
CC esterase. Induces cell proliferation at low concentrations and inhibits
CC it at high concentrations. Mediates the spreading of plasmatocytes to
CC foreign surfaces. May have a role in the regulation of dopamine
CC concentrations. {ECO:0000269|PubMed:10928276,
CC ECO:0000269|PubMed:11429413, ECO:0000269|PubMed:9753606}.
CC -!- TISSUE SPECIFICITY: Expressed in the hemolymph, perineural cells and
CC neuroglia of larval brain. {ECO:0000269|PubMed:10928276,
CC ECO:0000269|PubMed:7498538}.
CC -!- DEVELOPMENTAL STAGE: Levels are highest on day 0 of penultimate instar
CC larvae and then decrease throughout larval growth with a temporary
CC increase on day 0 of the last larval instar. In parasitized larvae,
CC expression increases within one day of parasitization with elevated
CC levels persisting for one day, declining gradually, rising and then
CC declining again. {ECO:0000269|PubMed:8580912}.
CC -!- INDUCTION: By parasitization and low temperatures.
CC {ECO:0000269|PubMed:10928276, ECO:0000269|PubMed:8580912}.
CC -!- PTM: Growth-blocking peptide appears to exist in two different forms, a
CC long form which has been isolated from parasitized larvae and a short
CC form which is found in non-parasitized larvae. The stop codon of the
CC short form may be read as a Tyr to synthesize the long form.
CC -!- SIMILARITY: Belongs to the GBP/PSP1/paralytic peptide family.
CC {ECO:0000305}.
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DR EMBL; S80564; AAB35742.1; -; mRNA.
DR EMBL; AB012294; BAA32793.1; -; Genomic_DNA.
DR PIR; S68226; S68226.
DR PDB; 1BQF; NMR; -; A=121-145.
DR PDB; 2EQH; NMR; -; A=121-143.
DR PDB; 2EQQ; NMR; -; A=121-145.
DR PDB; 2EQT; NMR; -; A=121-145.
DR PDBsum; 1BQF; -.
DR PDBsum; 2EQH; -.
DR PDBsum; 2EQQ; -.
DR PDBsum; 2EQT; -.
DR AlphaFoldDB; Q27913; -.
DR SMR; Q27913; -.
DR EvolutionaryTrace; Q27913; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
DR GO; GO:0035099; P:hemocyte migration; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; TAS:UniProtKB.
DR InterPro; IPR003463; GBP_PSP.
DR Pfam; PF02425; GBP_PSP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Cytokine; Direct protein sequencing;
KW Disulfide bond; Mitogen; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..120
FT /evidence="ECO:0000269|PubMed:12182821,
FT ECO:0000269|PubMed:2022627, ECO:0000269|PubMed:8580912"
FT /id="PRO_0000010714"
FT PEPTIDE 121..145
FT /note="Growth-blocking peptide, long form"
FT /id="PRO_0000263063"
FT PEPTIDE 121..143
FT /note="Growth-blocking peptide, short form"
FT /id="PRO_0000010715"
FT REGION 46..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 145
FT /note="Glutamine amide"
FT /evidence="ECO:0000250"
FT DISULFID 127..139
FT MUTAGEN 121
FT /note="Missing: Abolishes plasmatocyte spreading activity."
FT /evidence="ECO:0000269|PubMed:11429413"
FT MUTAGEN 125
FT /note="G->A: No effect on plasmatocyte spreading activity."
FT /evidence="ECO:0000269|PubMed:15385535"
FT MUTAGEN 125
FT /note="G->F: Significantly reduces plasmatocyte spreading
FT activity."
FT /evidence="ECO:0000269|PubMed:15385535"
FT MUTAGEN 126
FT /note="G->A: No effect on plasmatocyte spreading activity."
FT /evidence="ECO:0000269|PubMed:15385535"
FT MUTAGEN 126
FT /note="G->F: Significantly reduces plasmatocyte spreading
FT activity."
FT /evidence="ECO:0000269|PubMed:15385535"
FT MUTAGEN 136
FT /note="D->E,L,N: Abolishes mitogenic activity and reduces
FT plasmatocyte spreading activity."
FT /evidence="ECO:0000269|PubMed:11429413"
FT MUTAGEN 142
FT /note="Missing: Reduces mitogenic activity and slightly
FT reduces plasmatocyte spreading activity."
FT /evidence="ECO:0000269|PubMed:11429413"
FT MUTAGEN 143
FT /note="Missing: Reduces mitogenic activity and slightly
FT reduces plasmatocyte spreading activity."
FT /evidence="ECO:0000269|PubMed:11429413"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1BQF"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1BQF"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1BQF"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1BQF"
SQ SEQUENCE 145 AA; 15547 MW; 1A46BEBFB5279568 CRC64;
MKLTISILFC VILTLQYNGA DGKLKDLFGK IHDSVHGTAD KVKEDLNSLF HPNDKNQQGN
NDASSNIHFA DSEENTDAAK KPDEVTPATT TTTTAAPAVP NAPSDNPTTL APSTTTKDGR
ENFSGGCVAG YMRTPDGRCK PTFYQ
