GHSR is a seven-transmembrane ghrelin receptor that couples to heterotrimeric G proteins. Binding of acylated ghrelin activates pathways regulating growth-hormone release and energy balance, and the receptor also has substantial constitutive activity. In mammalian neurons it can participate in receptor heteromers, while peripheral immune and reproductive effects depend on tissue context. Ghrelin is distinct from growth-hormone-releasing hormone and oxytocin.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001616 growth hormone secretagogue receptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: Ghrelin/growth-hormone-secretagogue receptor activity is the core molecular function. Reason: Receptor cloning, endogenous ligand identification and modern ghrelin-bound receptor structures establish this specific function. The full-length horse receptor retains the seven-transmembrane architecture and 95.1% identity, supporting transfer of ligand class and receptor mechanism; the equine expression paper verifies GHSR1a transcripts but is not a ligand-binding assay. Supporting Evidence: PMID:10604470 an endogenous ligand specific for GHS-R. PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0001616 growth hormone secretagogue receptor activity | IDA PMID:11322507 Growth hormone secretagogue receptor family members and liga... | ACCEPT | Summary: Ghrelin/growth-hormone-secretagogue receptor activity is the core molecular function. Reason: Receptor cloning, endogenous ligand identification and modern ghrelin-bound receptor structures establish this specific function. The full-length horse receptor retains the seven-transmembrane architecture and 95.1% identity, supporting transfer of ligand class and receptor mechanism; the equine expression paper verifies GHSR1a transcripts but is not a ligand-binding assay. Supporting Evidence: PMID:10604470 an endogenous ligand specific for GHS-R. PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0001616 growth hormone secretagogue receptor activity | IDA PMID:8688086 A receptor in pituitary and hypothalamus that functions in g... | ACCEPT | Summary: Ghrelin/growth-hormone-secretagogue receptor activity is the core molecular function. Reason: Receptor cloning, endogenous ligand identification and modern ghrelin-bound receptor structures establish this specific function. The full-length horse receptor retains the seven-transmembrane architecture and 95.1% identity, supporting transfer of ligand class and receptor mechanism; the equine expression paper verifies GHSR1a transcripts but is not a ligand-binding assay. Supporting Evidence: PMID:10604470 an endogenous ligand specific for GHS-R. PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0001616 growth hormone secretagogue receptor activity | IEA GO_REF:0000107 | ACCEPT | Summary: Ghrelin/growth-hormone-secretagogue receptor activity is the core molecular function. Reason: Receptor cloning, endogenous ligand identification and modern ghrelin-bound receptor structures establish this specific function. The full-length horse receptor retains the seven-transmembrane architecture and 95.1% identity, supporting transfer of ligand class and receptor mechanism; the equine expression paper verifies GHSR1a transcripts but is not a ligand-binding assay. Supporting Evidence: PMID:10604470 an endogenous ligand specific for GHS-R. PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0004930 G protein-coupled receptor activity | IDA PMID:8688086 A receptor in pituitary and hypothalamus that functions in g... | MODIFY | Summary: The ghrelin receptor term captures the experimentally established specificity. Reason: GHSR is a peptide-hormone-binding GPCR, but the specific ghrelin/growth-hormone-secretagogue receptor activity is more informative than generic receptor or peptide-binding terms. Proposed replacements: growth hormone secretagogue receptor activity Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0004930 G protein-coupled receptor activity | IEA GO_REF:0000002 | MODIFY | Summary: The ghrelin receptor term captures the experimentally established specificity. Reason: GHSR is a peptide-hormone-binding GPCR, but the specific ghrelin/growth-hormone-secretagogue receptor activity is more informative than generic receptor or peptide-binding terms. Proposed replacements: growth hormone secretagogue receptor activity Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: The seven-transmembrane receptor functions at the cell surface. Reason: Cloned GHSR has membrane receptor pharmacology, and the active receptor structures show the transmembrane signaling architecture. A preserved full-length horse receptor supports the same membrane compartment. Supporting Evidence: PMID:8688086 A heterotrimeric GTP-binding protein (G protein)-coupled receptor (GPC-R) |
| GO:0005886 plasma membrane | IDA PMID:15232612 Ghrelin inhibits leptin- and activation-induced proinflammat... | ACCEPT | Summary: The seven-transmembrane receptor functions at the cell surface. Reason: Cloned GHSR has membrane receptor pharmacology, and the active receptor structures show the transmembrane signaling architecture. A preserved full-length horse receptor supports the same membrane compartment. Supporting Evidence: PMID:8688086 A heterotrimeric GTP-binding protein (G protein)-coupled receptor (GPC-R) |
| GO:0005886 plasma membrane | IDA PMID:35027551 Molecular mechanism of agonism and inverse agonism in ghreli... | ACCEPT | Summary: The seven-transmembrane receptor functions at the cell surface. Reason: Cloned GHSR has membrane receptor pharmacology, and the active receptor structures show the transmembrane signaling architecture. A preserved full-length horse receptor supports the same membrane compartment. Supporting Evidence: PMID:8688086 A heterotrimeric GTP-binding protein (G protein)-coupled receptor (GPC-R) |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: The seven-transmembrane receptor functions at the cell surface. Reason: Cloned GHSR has membrane receptor pharmacology, and the active receptor structures show the transmembrane signaling architecture. A preserved full-length horse receptor supports the same membrane compartment. Supporting Evidence: PMID:8688086 A heterotrimeric GTP-binding protein (G protein)-coupled receptor (GPC-R) |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-379048 | ACCEPT | Summary: The seven-transmembrane receptor functions at the cell surface. Reason: Cloned GHSR has membrane receptor pharmacology, and the active receptor structures show the transmembrane signaling architecture. A preserved full-length horse receptor supports the same membrane compartment. Supporting Evidence: PMID:8688086 A heterotrimeric GTP-binding protein (G protein)-coupled receptor (GPC-R) |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-749448 | ACCEPT | Summary: The seven-transmembrane receptor functions at the cell surface. Reason: Cloned GHSR has membrane receptor pharmacology, and the active receptor structures show the transmembrane signaling architecture. A preserved full-length horse receptor supports the same membrane compartment. Supporting Evidence: PMID:8688086 A heterotrimeric GTP-binding protein (G protein)-coupled receptor (GPC-R) |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-749452 | ACCEPT | Summary: The seven-transmembrane receptor functions at the cell surface. Reason: Cloned GHSR has membrane receptor pharmacology, and the active receptor structures show the transmembrane signaling architecture. A preserved full-length horse receptor supports the same membrane compartment. Supporting Evidence: PMID:8688086 A heterotrimeric GTP-binding protein (G protein)-coupled receptor (GPC-R) |
| GO:0007154 cell communication | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Ghrelin activates G-protein-dependent receptor signaling. Reason: GHSR ligand recognition activates heterotrimeric G proteins and downstream second messengers. The specific receptor-signaling process is core; generic signaling/communication or hormone-response terms are compatible but less informative. Shared GPCR coupling does not imply oxytocin specificity. Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0007186 G protein-coupled receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: Ghrelin activates G-protein-dependent receptor signaling. Reason: GHSR ligand recognition activates heterotrimeric G proteins and downstream second messengers. The specific receptor-signaling process is core; generic signaling/communication or hormone-response terms are compatible but less informative. Shared GPCR coupling does not imply oxytocin specificity. Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0007186 G protein-coupled receptor signaling pathway | IDA PMID:8688086 A receptor in pituitary and hypothalamus that functions in g... | ACCEPT | Summary: Ghrelin activates G-protein-dependent receptor signaling. Reason: GHSR ligand recognition activates heterotrimeric G proteins and downstream second messengers. The specific receptor-signaling process is core; generic signaling/communication or hormone-response terms are compatible but less informative. Shared GPCR coupling does not imply oxytocin specificity. Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0007186 G protein-coupled receptor signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: Ghrelin activates G-protein-dependent receptor signaling. Reason: GHSR ligand recognition activates heterotrimeric G proteins and downstream second messengers. The specific receptor-signaling process is core; generic signaling/communication or hormone-response terms are compatible but less informative. Shared GPCR coupling does not imply oxytocin specificity. Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: Ghrelin activates G-protein-dependent receptor signaling. Reason: GHSR ligand recognition activates heterotrimeric G proteins and downstream second messengers. The specific receptor-signaling process is core; generic signaling/communication or hormone-response terms are compatible but less informative. Shared GPCR coupling does not imply oxytocin specificity. Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway | ISS GO_REF:0000024 | ACCEPT | Summary: Ghrelin activates G-protein-dependent receptor signaling. Reason: GHSR ligand recognition activates heterotrimeric G proteins and downstream second messengers. The specific receptor-signaling process is core; generic signaling/communication or hormone-response terms are compatible but less informative. Shared GPCR coupling does not imply oxytocin specificity. Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0007283 spermatogenesis | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific spermatogenesis assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0007565 female pregnancy | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific female pregnancy assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0007611 learning or memory | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0007612 learning | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0007612 learning | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0007613 memory | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0007613 memory | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0008154 actin polymerization or depolymerization | IDA PMID:15232612 Ghrelin inhibits leptin- and activation-induced proinflammat... | KEEP AS NON CORE | Summary: Immune-cell membrane organization/cytoskeletal effects require the stated tissue context. Reason: The human primary GHSR immune-cell study supplies these IDA observations. Retain the human observation as non-core; the corresponding horse annotation lacks a verified horse cellular context, and receptor conservation alone does not establish membrane-raft partitioning or actin remodeling in that tissue. Supporting Evidence: PMID:15232612 GHS-R and ghrelin are expressed in human T lymphocytes and monocytes |
| GO:0008343 adult feeding behavior | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Feeding/appetite regulation is a supported physiological context of ghrelin signaling. Reason: Ghrelin/GHSR signaling promotes appetite in mammalian pharmacological studies. This is a plausible conserved physiological effect, but the equine hormone concentration study does not directly demonstrate that receptor activity causes feeding behavior. Supporting Evidence: PMID:16511605 its endogenous ligand--ghrelin--stimulates, through the GHSR, GH secretion and appetite |
| GO:0008343 adult feeding behavior | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Feeding/appetite regulation is a supported physiological context of ghrelin signaling. Reason: Ghrelin/GHSR signaling promotes appetite in mammalian pharmacological studies. This is a plausible conserved physiological effect, but the equine hormone concentration study does not directly demonstrate that receptor activity causes feeding behavior. Supporting Evidence: PMID:16511605 its endogenous ligand--ghrelin--stimulates, through the GHSR, GH secretion and appetite |
| GO:0009725 response to hormone | IDA PMID:15232612 Ghrelin inhibits leptin- and activation-induced proinflammat... | KEEP AS NON CORE | Summary: Ghrelin activates G-protein-dependent receptor signaling. Reason: GHSR ligand recognition activates heterotrimeric G proteins and downstream second messengers. The specific receptor-signaling process is core; generic signaling/communication or hormone-response terms are compatible but less informative. Shared GPCR coupling does not imply oxytocin specificity. Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0009755 hormone-mediated signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: Ghrelin activates G-protein-dependent receptor signaling. Reason: GHSR ligand recognition activates heterotrimeric G proteins and downstream second messengers. The specific receptor-signaling process is core; generic signaling/communication or hormone-response terms are compatible but less informative. Shared GPCR coupling does not imply oxytocin specificity. Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0009755 hormone-mediated signaling pathway | IDA PMID:8688086 A receptor in pituitary and hypothalamus that functions in g... | ACCEPT | Summary: Ghrelin activates G-protein-dependent receptor signaling. Reason: GHSR ligand recognition activates heterotrimeric G proteins and downstream second messengers. The specific receptor-signaling process is core; generic signaling/communication or hormone-response terms are compatible but less informative. Shared GPCR coupling does not imply oxytocin specificity. Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0009986 cell surface | IDA PMID:8688086 A receptor in pituitary and hypothalamus that functions in g... | ACCEPT | Summary: The seven-transmembrane receptor functions at the cell surface. Reason: Cloned GHSR has membrane receptor pharmacology, and the active receptor structures show the transmembrane signaling architecture. A preserved full-length horse receptor supports the same membrane compartment. Supporting Evidence: PMID:8688086 A heterotrimeric GTP-binding protein (G protein)-coupled receptor (GPC-R) |
| GO:0010700 negative regulation of norepinephrine secretion | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific negative regulation of norepinephrine secretion assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0015026 coreceptor activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0015026 coreceptor activity | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: The seven-transmembrane receptor functions at the cell surface. Reason: Cloned GHSR has membrane receptor pharmacology, and the active receptor structures show the transmembrane signaling architecture. A preserved full-length horse receptor supports the same membrane compartment. Proposed replacements: plasma membrane Supporting Evidence: PMID:8688086 A heterotrimeric GTP-binding protein (G protein)-coupled receptor (GPC-R) |
| GO:0016520 growth hormone-releasing hormone receptor activity | IDA PMID:10604470 Ghrelin is a growth-hormone-releasing acylated peptide from ... | MODIFY | Summary: The cited ligand is ghrelin, not growth-hormone-releasing hormone. Reason: QuickGO defines GO:0016520 as binding growth-hormone-releasing hormone, whereas GO:0001616 binds ghrelin. The discovery paper explicitly distinguishes the ghrelin/GHSR pathway from hypothalamic GHRH. Human IDA rows cite ghrelin/secretagogue studies, and the horse Ensembl transfer names human Q92847 as donor. Replace the ligand-confused term with the ghrelin receptor term; no claim of a wrong experimental organism or missing assay is needed. Proposed replacements: growth hormone secretagogue receptor activity Supporting Evidence: PMID:10604470 there is a mechanism for regulating GH release that is distinct from its regulation by hypothalamic growth-hormone-releasing hormone (GHRH). |
| GO:0016520 growth hormone-releasing hormone receptor activity | IDA PMID:8688086 A receptor in pituitary and hypothalamus that functions in g... | MODIFY | Summary: The cited ligand is ghrelin, not growth-hormone-releasing hormone. Reason: QuickGO defines GO:0016520 as binding growth-hormone-releasing hormone, whereas GO:0001616 binds ghrelin. The discovery paper explicitly distinguishes the ghrelin/GHSR pathway from hypothalamic GHRH. Human IDA rows cite ghrelin/secretagogue studies, and the horse Ensembl transfer names human Q92847 as donor. Replace the ligand-confused term with the ghrelin receptor term; no claim of a wrong experimental organism or missing assay is needed. Proposed replacements: growth hormone secretagogue receptor activity Supporting Evidence: PMID:10604470 there is a mechanism for regulating GH release that is distinct from its regulation by hypothalamic growth-hormone-releasing hormone (GHRH). |
| GO:0016520 growth hormone-releasing hormone receptor activity | IEA GO_REF:0000107 | MODIFY | Summary: The cited ligand is ghrelin, not growth-hormone-releasing hormone. Reason: QuickGO defines GO:0016520 as binding growth-hormone-releasing hormone, whereas GO:0001616 binds ghrelin. The discovery paper explicitly distinguishes the ghrelin/GHSR pathway from hypothalamic GHRH. Human IDA rows cite ghrelin/secretagogue studies, and the horse Ensembl transfer names human Q92847 as donor. Replace the ligand-confused term with the ghrelin receptor term; no claim of a wrong experimental organism or missing assay is needed. Proposed replacements: growth hormone secretagogue receptor activity Supporting Evidence: PMID:10604470 there is a mechanism for regulating GH release that is distinct from its regulation by hypothalamic growth-hormone-releasing hormone (GHRH). |
| GO:0017046 peptide hormone binding | IEA GO_REF:0000107 | MODIFY | Summary: The ghrelin receptor term captures the experimentally established specificity. Reason: GHSR is a peptide-hormone-binding GPCR, but the specific ghrelin/growth-hormone-secretagogue receptor activity is more informative than generic receptor or peptide-binding terms. Proposed replacements: growth hormone secretagogue receptor activity Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0023052 signaling | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Ghrelin activates G-protein-dependent receptor signaling. Reason: GHSR ligand recognition activates heterotrimeric G proteins and downstream second messengers. The specific receptor-signaling process is core; generic signaling/communication or hormone-response terms are compatible but less informative. Shared GPCR coupling does not imply oxytocin specificity. Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0030252 growth hormone secretion | TAS PMID:16511605 Loss of constitutive activity of the growth hormone secretag... | ACCEPT | Summary: GHSR signaling regulates growth-hormone release and contributes to growth. Reason: Secretagogue receptor pharmacology and human loss-of-constitutive-activity variants support this endocrine role. The horse pituitary GHSR1a transcript and conserved receptor support the general mechanism, but do not establish the magnitude of growth effects in horse. Supporting Evidence: PMID:16511605 selectively impairs the constitutive activity of the GHSR, while preserving its ability to respond to ghrelin. |
| GO:0032099 negative regulation of appetite | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific negative regulation of appetite assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0032100 positive regulation of appetite | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Feeding/appetite regulation is a supported physiological context of ghrelin signaling. Reason: Ghrelin/GHSR signaling promotes appetite in mammalian pharmacological studies. This is a plausible conserved physiological effect, but the equine hormone concentration study does not directly demonstrate that receptor activity causes feeding behavior. Supporting Evidence: PMID:16511605 its endogenous ligand--ghrelin--stimulates, through the GHSR, GH secretion and appetite |
| GO:0032100 positive regulation of appetite | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Feeding/appetite regulation is a supported physiological context of ghrelin signaling. Reason: Ghrelin/GHSR signaling promotes appetite in mammalian pharmacological studies. This is a plausible conserved physiological effect, but the equine hormone concentration study does not directly demonstrate that receptor activity causes feeding behavior. Supporting Evidence: PMID:16511605 its endogenous ligand--ghrelin--stimulates, through the GHSR, GH secretion and appetite |
| GO:0032354 response to follicle-stimulating hormone | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific response to follicle-stimulating hormone assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0032355 response to estradiol | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific response to estradiol assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0032691 negative regulation of interleukin-1 beta production | IDA PMID:15232612 Ghrelin inhibits leptin- and activation-induced proinflammat... | KEEP AS NON CORE | Summary: GHSR-dependent cytokine inhibition is supported in human immune cells. Reason: Human monocyte/T-cell experiments demonstrate suppression of IL-1beta, IL-6 and TNF-alpha expression through GHSR. This is a tissue-specific signaling consequence, not the defining receptor function; conservation makes horse transfer plausible but direct horse immune-cell assays are absent. Supporting Evidence: PMID:15232612 ghrelin acts via GHS-R to specifically inhibit the expression of proinflammatory anorectic cytokines such as IL-1beta, IL-6, and TNF-alpha. |
| GO:0032715 negative regulation of interleukin-6 production | IDA PMID:15232612 Ghrelin inhibits leptin- and activation-induced proinflammat... | KEEP AS NON CORE | Summary: GHSR-dependent cytokine inhibition is supported in human immune cells. Reason: Human monocyte/T-cell experiments demonstrate suppression of IL-1beta, IL-6 and TNF-alpha expression through GHSR. This is a tissue-specific signaling consequence, not the defining receptor function; conservation makes horse transfer plausible but direct horse immune-cell assays are absent. Supporting Evidence: PMID:15232612 ghrelin acts via GHS-R to specifically inhibit the expression of proinflammatory anorectic cytokines such as IL-1beta, IL-6, and TNF-alpha. |
| GO:0032720 negative regulation of tumor necrosis factor production | IDA PMID:15232612 Ghrelin inhibits leptin- and activation-induced proinflammat... | KEEP AS NON CORE | Summary: GHSR-dependent cytokine inhibition is supported in human immune cells. Reason: Human monocyte/T-cell experiments demonstrate suppression of IL-1beta, IL-6 and TNF-alpha expression through GHSR. This is a tissue-specific signaling consequence, not the defining receptor function; conservation makes horse transfer plausible but direct horse immune-cell assays are absent. Supporting Evidence: PMID:15232612 ghrelin acts via GHS-R to specifically inhibit the expression of proinflammatory anorectic cytokines such as IL-1beta, IL-6, and TNF-alpha. |
| GO:0032720 negative regulation of tumor necrosis factor production | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GHSR-dependent cytokine inhibition is supported in human immune cells. Reason: Human monocyte/T-cell experiments demonstrate suppression of IL-1beta, IL-6 and TNF-alpha expression through GHSR. This is a tissue-specific signaling consequence, not the defining receptor function; conservation makes horse transfer plausible but direct horse immune-cell assays are absent. Supporting Evidence: PMID:15232612 ghrelin acts via GHS-R to specifically inhibit the expression of proinflammatory anorectic cytokines such as IL-1beta, IL-6, and TNF-alpha. |
| GO:0036321 ghrelin secretion | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific ghrelin secretion assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0038023 signaling receptor activity | IEA GO_REF:0000117 | MODIFY | Summary: The ghrelin receptor term captures the experimentally established specificity. Reason: GHSR is a peptide-hormone-binding GPCR, but the specific ghrelin/growth-hormone-secretagogue receptor activity is more informative than generic receptor or peptide-binding terms. Proposed replacements: growth hormone secretagogue receptor activity Supporting Evidence: PMID:35027551 active ghrelin receptor-Go complex bound to the endogenous agonist ghrelin. |
| GO:0040018 positive regulation of multicellular organism growth | IMP PMID:16511605 Loss of constitutive activity of the growth hormone secretag... | KEEP AS NON CORE | Summary: GHSR signaling regulates growth-hormone release and contributes to growth. Reason: Secretagogue receptor pharmacology and human loss-of-constitutive-activity variants support this endocrine role. The horse pituitary GHSR1a transcript and conserved receptor support the general mechanism, but do not establish the magnitude of growth effects in horse. Supporting Evidence: PMID:16511605 selectively impairs the constitutive activity of the GHSR, while preserving its ability to respond to ghrelin. |
| GO:0043005 neuron projection | IDA PMID:12890514 Growth hormone secretagogue receptors in rat and human gastr... | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0043134 regulation of hindgut contraction | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific regulation of hindgut contraction assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0045121 membrane raft | IDA PMID:15232612 Ghrelin inhibits leptin- and activation-induced proinflammat... | KEEP AS NON CORE | Summary: Immune-cell membrane organization/cytoskeletal effects require the stated tissue context. Reason: The human primary GHSR immune-cell study supplies these IDA observations. Retain the human observation as non-core; the corresponding horse annotation lacks a verified horse cellular context, and receptor conservation alone does not establish membrane-raft partitioning or actin remodeling in that tissue. Supporting Evidence: PMID:15232612 GHS-R and ghrelin are expressed in human T lymphocytes and monocytes |
| GO:0045923 positive regulation of fatty acid metabolic process | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific positive regulation of fatty acid metabolic process assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0045927 positive regulation of growth | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GHSR signaling regulates growth-hormone release and contributes to growth. Reason: Secretagogue receptor pharmacology and human loss-of-constitutive-activity variants support this endocrine role. The horse pituitary GHSR1a transcript and conserved receptor support the general mechanism, but do not establish the magnitude of growth effects in horse. Supporting Evidence: PMID:16511605 selectively impairs the constitutive activity of the GHSR, while preserving its ability to respond to ghrelin. |
| GO:0046697 decidualization | IDA PMID:17494105 Facilitation of decidualization by locally produced ghrelin ... | KEEP AS NON CORE | Summary: The decidualization evidence is from human endometrial stromal cells. Reason: The primary study adds ghrelin to human stromal-cell decidualization cultures and detects receptor expression. This supports a human reproductive context; placentation and decidual responses differ among mammals, so this precise process is not transferred confidently to horse without relevant uterine evidence. Supporting Evidence: PMID:17494105 Ghrelin administered in combination with sex steroids to HESC, resulted in an increase in PRL and IGFBP-1 production |
| GO:0048167 regulation of synaptic plasticity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0048167 regulation of synaptic plasticity | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0050728 negative regulation of inflammatory response | IDA PMID:15232612 Ghrelin inhibits leptin- and activation-induced proinflammat... | KEEP AS NON CORE | Summary: GHSR-dependent cytokine inhibition is supported in human immune cells. Reason: Human monocyte/T-cell experiments demonstrate suppression of IL-1beta, IL-6 and TNF-alpha expression through GHSR. This is a tissue-specific signaling consequence, not the defining receptor function; conservation makes horse transfer plausible but direct horse immune-cell assays are absent. Supporting Evidence: PMID:15232612 ghrelin acts via GHS-R to specifically inhibit the expression of proinflammatory anorectic cytokines such as IL-1beta, IL-6, and TNF-alpha. |
| GO:0051969 regulation of transmission of nerve impulse | IEA GO_REF:0000107 | UNDECIDED | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0060123 regulation of growth hormone secretion | IEA GO_REF:0000107 | ACCEPT | Summary: GHSR signaling regulates growth-hormone release and contributes to growth. Reason: Secretagogue receptor pharmacology and human loss-of-constitutive-activity variants support this endocrine role. The horse pituitary GHSR1a transcript and conserved receptor support the general mechanism, but do not establish the magnitude of growth effects in horse. Supporting Evidence: PMID:16511605 selectively impairs the constitutive activity of the GHSR, while preserving its ability to respond to ghrelin. |
| GO:0060259 regulation of feeding behavior | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Feeding/appetite regulation is a supported physiological context of ghrelin signaling. Reason: Ghrelin/GHSR signaling promotes appetite in mammalian pharmacological studies. This is a plausible conserved physiological effect, but the equine hormone concentration study does not directly demonstrate that receptor activity causes feeding behavior. Supporting Evidence: PMID:16511605 its endogenous ligand--ghrelin--stimulates, through the GHSR, GH secretion and appetite |
| GO:0060416 response to growth hormone | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific response to growth hormone assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0071222 cellular response to lipopolysaccharide | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific cellular response to lipopolysaccharide assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0071548 response to dexamethasone | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific response to dexamethasone assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0090327 negative regulation of locomotion involved in locomotory behavior | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific negative regulation of locomotion involved in locomotory behavior assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0097060 synaptic membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0097067 cellular response to thyroid hormone stimulus | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific cellular response to thyroid hormone stimulus assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:0098685 Schaffer collateral - CA1 synapse | IEA GO_REF:0000107 | UNDECIDED | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0098696 regulation of neurotransmitter receptor localization to postsynaptic specialization membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0098794 postsynapse | IEA GO_REF:0000108 | UNDECIDED | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | UNDECIDED | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0099170 postsynaptic modulation of chemical synaptic transmission | IEA GO_REF:0000107 | UNDECIDED | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0099175 regulation of postsynapse organization | IEA GO_REF:0000107 | UNDECIDED | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:0120058 positive regulation of small intestinal transit | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific positive regulation of small intestinal transit assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:1902065 response to L-glutamate | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific response to L-glutamate assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:1903672 positive regulation of sprouting angiogenesis | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific positive regulation of sprouting angiogenesis assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:1904000 positive regulation of eating behavior | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Feeding/appetite regulation is a supported physiological context of ghrelin signaling. Reason: Ghrelin/GHSR signaling promotes appetite in mammalian pharmacological studies. This is a plausible conserved physiological effect, but the equine hormone concentration study does not directly demonstrate that receptor activity causes feeding behavior. Supporting Evidence: PMID:16511605 its endogenous ligand--ghrelin--stimulates, through the GHSR, GH secretion and appetite |
| GO:1904349 positive regulation of small intestine smooth muscle contraction | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific positive regulation of small intestine smooth muscle contraction assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:1905333 regulation of gastric motility | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific regulation of gastric motility assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:1905564 positive regulation of vascular endothelial cell proliferation | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific positive regulation of vascular endothelial cell proliferation assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:1990314 cellular response to insulin-like growth factor stimulus | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific cellular response to insulin-like growth factor stimulus assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:2000110 negative regulation of macrophage apoptotic process | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific negative regulation of macrophage apoptotic process assignment requires donor-specific physiological evidence. Reason: This electronic transfer concerns a specialized physiological response rather than the established receptor mechanism. Ghrelin receptor conservation and endocrine expression do not by themselves validate the direction, tissue, developmental state or stimulus named by this term. The relevant donor experiment has not been resolved, so the annotation is not accepted or rejected solely from general ghrelin biology. |
| GO:2000292 regulation of defecation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
| GO:2000292 regulation of defecation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Neuronal receptor-heteromer roles are context-specific and distinct from ghrelin ligand recognition. Reason: The curated mammalian synthesis describes GHSR/DRD1 or GHSR/DRD2 heteromers in synaptic plasticity and defecation. Broad neuronal/coreceptor effects are retained as non-core evolutionary inferences; precise synapse subdivisions and postsynaptic organization require inspection of the donor experiment. No heteromer claim establishes oxytocin receptor activity. Supporting Evidence: file:human/GHSR/GHSR-uniprot.txt by forming CC a heteromer with the dopamine receptors DRD1 and DRD2 in neurons |
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