PF01147

Crustacean CHH/MIH/GIH neurohormone family

Pfam entry
Member databasePfam
Pfam typefamily
Short nameCrust_neurohorm
Author Finn RD;0000-0001-8626-2148 Bateman A;0000-0002-6982-4660
Sequence Ontology0100021

Description
Imported from IPR031098

Arthropod express a family of neuropeptides
[1]
which so far consist of the following types of neurohormones:
 * Crustacean hyperglycemic hormone (CHH). CHH is primarily involved in blood sugar regulation, but also plays a role in the control of molting and reproduction.
 * Molt-inhibiting hormone (MIH). MIH inhibits Y-organs where molting hormone (ecdysteroid) is secreted. A molting cycle is initiated when MIH secretion diminishes or stops.
 * Gonad-inhibiting hormone (GIH), also known as vitellogenesis-inhibiting hormone (VIH) because of its role in inhibiting vitellogenesis in female animals.
 * Mandibular organ-inhibiting hormone (MOIH). MOIH represses the synthesis of methyl farnesoate, the precursor of insect juvenile hormone III in the mandibular organ.
 * Ion transport peptide (ITP) from locust. ITP stimulates salt and water reabsorption and inhibits acid secretion in the ileum of the locust.

These neurohormones are peptides of 70 to 80 residues which are processed from larger size precursors. They contain six conserved cysteines that are involved in disulphide bonds, as shown in the following schematic representation.

Alpha-latrotoxin associated low molecular weight proteins (LMWPs) are a family of uncharacterised venom peptides associated with alpha-latrotoxin, a black widow spider neurotoxin, which are probably also expressed in the venoms of other Latrodectus and Steatoda species
[4, 3, 2]
.

This entry also includes proteins from Nematoda, such as Caenorhabditis elegans hypothetical protein ZC168.2.

References
Imported from IPR031098

1.Molecular biology of neurohormone precursors in the eyestalk of Crustacea. De Kleijn DP, Van Herp F. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 112, 573-9, (1995). View articlePMID: 8590372

2.Recruitment and diversification of an ecdysozoan family of neuropeptide hormones for black widow spider venom expression. McCowan C, Garb JE. Gene 536, 366-75, (2014). View articlePMID: 24316130

3.The cloning of a cDNA encoding a protein (latrodectin) which co-purifies with the alpha-latrotoxin from the black widow spider Latrodectus tredecimguttatus (Theridiidae). Pescatori M, Bradbury A, Bouet F, Gargano N, Mastrogiacomo A, Grasso A. Eur. J. Biochem. 230, 322-8, (1995). View articlePMID: 7601118

4.Structure of the low molecular weight protein copurified with alpha-latrotoxin. Kiyatkin N, Dulubova I, Chekhovskaya I, Lipkin A, Grishin E. Toxicon 30, 771-4, (1992). View articlePMID: 1509496

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