Family

Anti-muellerian hormone receptor, type II (IPR015771)

Short name: Anti-muellerian_hrmn_rcpt_II

Overlapping homologous superfamilies

None.

Family relationships

Description

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [PMID: 3291115]:

  • Serine/threonine-protein kinases
  • Tyrosine-protein kinases
  • Dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)

Protein kinase function is evolutionarily conserved from Escherichia coli to human [PMID: 12471243]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [PMID: 12368087]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [PMID: 15078142], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [PMID: 15320712].

Protein kinases are a group of enzymes that possess a catalytic subunit, which transfers the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues (such as serine, threonine, or tyrosine) in a substrate protein's side chain, resulting in a conformational change affecting protein function. Protein kinase function has been evolutionarily conserved from Escherichia coli to Homo sapiens (Human), where they play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [PMID: 12368087].

The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [PMID: 15078142], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [PMID: 15320712].

Anti-Mullerian hormone (AMH), also called Mullerian inhibiting substance, is a member of the transforming growth factor beta (TGF-beta) family that represses the development and function of reproductive organs [PMID: 14656470]. Anti-Mullerian hormone is thought to exert its effects through two membrane-bound serine/threonine kinase receptors, type 2 and type 1. Upon ligand binding, these drive receptor-specific cytoplasmic substrates, the Smad molecules, into the nucleus where they act as transcription factors. A type 2 receptor specific for AMH was cloned through its homology with receptors of TGF-beta family members. Components of the AMH signalling pathway have been identified in gonads and gonadal cell lines. The AMH type II receptor is highly specific. In contrast, the identity of the AMH type I receptor is not clear.

GO terms

Biological Process

GO:0006468 protein phosphorylation

Molecular Function

GO:0005524 ATP binding
GO:0004675 transmembrane receptor protein serine/threonine kinase activity

Cellular Component

GO:0016020 membrane

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PIRSF