OR11H7

Model summary

A human seven-helix membrane receptor that belongs to the olfactory class of G protein–coupled receptors. It resides at the cell surface as a multi-pass protein and initiates signaling by binding a small, likely hydrophobic ligand within the membrane, thereby activating heterotrimeric G proteins. The ensuing second-messenger cascades that modulate cAMP and Ca2+ provide a route to enhance the terminal steps of cell division, aligning with a role in promoting cytokinesis. Its signaling depends on dynamic protein–protein interactions that couple extracellular cue detection to intracellular effector pathways at the plasma membrane.

Predicted Gene Ontology terms

1. 01

   I begin with the InterPro architecture.

   The core transmembrane engine is IPR017452 (GPCR, rhodopsin-like, 7TM domain, residues 41–290), which encodes the canonical seven-helix bundle that transduces extracellular ligand binding into intracellular G-protein activation. This structural core is embedded within multiple olfactory/rhodopsin-like GPCR family signatures that collectively define both fold and lineage: IPR050939 (Olfactory G-protein coupled receptor 1 family, residues 2–303) and IPR000725 (Olfactory receptor family, residues 33–306) specify an olfactory-class GPCR scaffold; IPR000276 (G protein-coupled receptor, rhodopsin-like family, residues 26–50) and IPR000276 (rhodopsin-like family, residues 104–126) plus IPR000276 (rhodopsin-like family, residues 272–298) mark conserved substructures that stabilize the inactive and active states and couple to heterotrimeric G proteins. The ordered layout—N-terminal extracellular region, seven transmembranes, and intracellular C-terminal loops—creates a receptor that binds small hydrophobic ligands in the membrane plane and signals through G proteins.

2. 02

   This architecture causes a molecular function centered on receptor-mediated signal initiation.

   The rhodopsin-like 7TM fold and olfactory-family signatures together define a G protein-coupled receptor that binds intracellular partners and extracellular cues; thus protein binding (GO:0005515) is intrinsic, encompassing ligand capture and Gα/βγ engagement. The absence of catalytic motifs and the presence of multiple GPCR family signatures reinforce that signaling occurs via conformational switching and effector recruitment rather than enzymatic chemistry.

3. 03

   From this molecular function, I infer the biological process.

   GPCR signaling can modulate cell-cycle machinery by controlling second messengers (cAMP, Ca2+) and kinase cascades that feed into cytokinesis checkpoints. An olfactory-class GPCR situated at the cell surface can elevate cAMP/PKA or Ca2+-dependent pathways that enhance contractile ring dynamics and abscission efficiency; this provides a mechanistic route to positive regulation of cytokinesis (GO:0032467). In this model, receptor activation biases cytoskeletal and membrane-trafficking modules that drive the terminal steps of cell division.

4. 04

   The cellular component follows directly from the seven-helix transmembrane core and the olfactory-family identity: the protein is an integral, multi-pass membrane receptor embedded in the plasma membrane (GO:0005886).

   The N-terminal extracellular region and the intracellular C-terminal tail position the receptor to sense the extracellular milieu and couple to cytosolic G proteins at the membrane interface.

5. 05

   Mechanistically, I hypothesize that the receptor binds a small, likely hydrophobic odorant or endogenous pheromone-like cue within the membrane, stabilizing an active state that recruits and activates a heterotrimeric G protein.

   The ensuing Gα exchange and Gβγ release modulate adenylyl cyclase and phosphodiesterase pathways, tuning cAMP and Ca2+ signals that secondarily enhance cytokinesis efficiency. Consistent with this, the receptor likely forms transient complexes with Gα subunits (e.g., Golf/Gs), Gβγ dimers, GPCR kinases, and arrestins, and may interface with membrane-associated scaffolds that coordinate actomyosin and membrane remodeling during cell division.