ID   ITP_SCHGR               Reviewed;         130 AA.
AC   Q26491;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Ion transport peptide;
DE            Short=ITP;
DE   Flags: Precursor;
OS   Schistocerca gregaria (Desert locust) (Gryllus gregarius).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX   NCBI_TaxID=7010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8786332; DOI=10.1242/jeb.199.5.1053;
RA   Meredith J., Ring M., Macins A., Marschall J., Cheng N.N., Theilmann D.,
RA   Brock H.W., Phillips J.E.;
RT   "Locust ion transport peptide (ITP): primary structure, cDNA and expression
RT   in a baculovirus system.";
RL   J. Exp. Biol. 199:1053-1061(1996).
CC   -!- FUNCTION: Stimulates salt and water reabsorption and inhibits acid
CC       secretion in the ileum of S.gregaria.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Brain and corpus cardiacum.
CC   -!- SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U36919; AAB16822.1; -; mRNA.
DR   AlphaFoldDB; Q26491; -.
DR   SMR; Q26491; -.
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   Gene3D; 1.10.2010.10; -; 1.
DR   InterPro; IPR018251; Crust_neurhormone_CS.
DR   InterPro; IPR031098; Crust_neurohorm.
DR   InterPro; IPR035957; Crust_neurohorm_sf.
DR   InterPro; IPR001166; Hyperglycemic.
DR   InterPro; IPR000346; Hyperglycemic1.
DR   PANTHER; PTHR35981; PTHR35981; 1.
DR   Pfam; PF01147; Crust_neurohorm; 1.
DR   PRINTS; PR00548; HYPRGLYCEMC1.
DR   PRINTS; PR00550; HYPRGLYCEMIC.
DR   SUPFAM; SSF81778; SSF81778; 1.
DR   PROSITE; PS01250; CHH_MIH_GIH; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW   Neuropeptide; Secreted; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..55
FT                   /id="PRO_0000019086"
FT   PEPTIDE         56..127
FT                   /note="Ion transport peptide"
FT                   /id="PRO_0000019087"
FT   MOD_RES         127
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..94
FT                   /evidence="ECO:0000250"
FT   DISULFID        81..107
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   130 AA;  15022 MW;  9499D8C1B0A93896 CRC64;
     MHHQKQQQQQ KQQGEAPCRH LQWRLSGVVL CVLVVASLVS TAASSPLDPH HLAKRSFFDI
     QCKGVYDKSI FARLDRICED CYNLFREPQL HSLCRSDCFK SPYFKGCLQA LLLIDEEEKF
     NQMVEILGKK