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Domain

The transmembrane domain is composed of seven transmembrane helices that are arranged in V-shape. Transmembrane helix 7 assumes a sharply kinked structure (By similarity).

The uncleaved pseudo signal peptide prevents receptor's oligomerization and coupling to G(i) subunits. It is also responsible for the rather low receptor localization at the plasma membrane (PubMed:22689579).

Function

G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels.

Post-translational modifications

A N-glycosylation site within the signal peptide impedes its proper cleavage and function.

Sequence similarities

Belongs to the G-protein coupled receptor 2 family.

Cellular localization

  • Cell membrane
  • Multi-pass membrane protein

Alternative names

CRF2R, CRH2R, CRHR2, Corticotropin-releasing factor receptor 2, CRF-R-2, CRF-R2, CRFR-2, Corticotropin-releasing hormone receptor 2, CRH-R-2, CRH-R2

Target type

Proteins

Primary research area

Metabolism

Molecular weight

47688Da

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Primary Antibodies

Target

Application

Reactive species

Search our catalogue for 'CRHR2' (2)

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