RAMP2 receptor activity modifying protein 2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: RAMP2provided by HGNC
Official Full Name: receptor activity modifying protein 2provided by HGNC
Primary source: HGNC:HGNC:9844
See related: Ensembl:ENSG00000131477 MIM:605154; AllianceGenome:HGNC:9844
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Summary: The protein encoded by this gene is a member of the RAMP family of single-transmembrane-domain proteins, called receptor (calcitonin) activity modifying proteins (RAMPs). RAMPs are type I transmembrane proteins with an extracellular N terminus and a cytoplasmic C terminus. RAMPs are required to transport calcitonin-receptor-like receptor (CRLR) to the plasma membrane. CRLR, a receptor with seven transmembrane domains, can function as either a calcitonin-gene-related peptide (CGRP) receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. In the presence of this (RAMP2) protein, CRLR functions as an adrenomedullin receptor. The RAMP2 protein is involved in core glycosylation and transportation of adrenomedullin receptor to the cell surface. [provided by RefSeq, Jul 2008]
Expression: Broad expression in lung (RPKM 58.9), fat (RPKM 57.7) and 22 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 17q21.2

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	17	NC_000017.11 (42761227..42763041)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	17	NC_060941.1 (43618368..43620182)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	17	NC_000017.10 (40913245..40915059)

Chromosome 17 - NC_000017.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

RAMP2-AS1 stabilized RAPM2 mRNA through TIA1 to inhibit the progression of non-small cell lung cancer.
Title: RAMP2-AS1 stabilized RAPM2 mRNA through TIA1 to inhibit the progression of non-small cell lung cancer.
Receptor Activity-Modifying Protein 2 (RAMP2) alters glucagon receptor trafficking in hepatocytes with functional effects on receptor signalling.
Title: Receptor Activity-Modifying Protein 2 (RAMP2) alters glucagon receptor trafficking in hepatocytes with functional effects on receptor signalling.
Adrenomedullin-Receptor Activity-Modifying Protein 2 System Ameliorates Subretinal Fibrosis by Suppressing Epithelial-Mesenchymal Transition in Age-Related Macular Degeneration.
Title: Adrenomedullin-Receptor Activity-Modifying Protein 2 System Ameliorates Subretinal Fibrosis by Suppressing Epithelial-Mesenchymal Transition in Age-Related Macular Degeneration.
Based on the finding that an acylated chimeric ADM/ADM2 analog potently stimulates CLR/RAMP1 and 2 signaling, we hypothesized that the binding domain of this analog could have potent inhibitory activity on CLR/RAMP receptors.
Title: Development of chimeric and bifunctional antagonists for CLR/RAMP receptors.
Interactions between RAMP2 and CRF receptors: The effect of receptor subtypes, splice variants and cell context
Title: Interactions between RAMP2 and CRF receptors: The effect of receptor subtypes, splice variants and cell context.
Single nucleotide polymorphism of RAMP2 is associated with Stroke.
Title: Genetic Variants of RAMP2 and CLR are Associated with Stroke.
This work suggests that RAMP2 may modify the agonist activity and trafficking of the GCGR, with potential relevance to production of new peptide analogs with selective agonist activities.
Title: RAMP2 Influences Glucagon Receptor Pharmacology via Trafficking and Signaling.
Data suggest that a single GlcNAc residue at CTR N130 (asparagine 130) is responsible for enhanced affinity of calcitonin for CTR ECD; the same appears to apply for enhanced affinity of amylin for RAMP2-CTR ECD. [GlcNAc = N-acetylglucosamine; CTR = calcitonin receptor; ECD = extracellular domain; RAMP2 = receptor (calcitonin) activity modifying protein 2].
Title: N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity.
interaction of RAMP2 or RAMP3 with CLR induces conformational variation in the juxtamembrane region, yielding distinct binding pockets, probably via an allosteric mechanism.
Title: Receptor Activity-modifying Proteins 2 and 3 Generate Adrenomedullin Receptor Subtypes with Distinct Molecular Properties.
This study reveals the glucagon receptor as a previously unidentified target for GLP-1 receptor agonists and highlights a role for RAMP2 in regulating its pharmacology.
Title: Modulation of Glucagon Receptor Pharmacology by Receptor Activity-modifying Protein-2 (RAMP2).

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Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Variation

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables adrenomedullin binding	IPI Inferred from Physical Interaction more info	PubMed
enables adrenomedullin receptor activity	IPI Inferred from Physical Interaction more info	PubMed
enables coreceptor activity	IBA Inferred from Biological aspect of Ancestor more info
enables coreceptor activity	ISS Inferred from Sequence or Structural Similarity more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in G protein-coupled receptor signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in adenylate cyclase-activating G protein-coupled receptor signaling pathway	IPI Inferred from Physical Interaction more info	PubMed
involved_in adherens junction assembly	IDA Inferred from Direct Assay more info	PubMed
involved_in adrenomedullin receptor signaling pathway	IPI Inferred from Physical Interaction more info	PubMed
involved_in angiogenesis	IBA Inferred from Biological aspect of Ancestor more info
involved_in angiogenesis	IDA Inferred from Direct Assay more info	PubMed
involved_in basement membrane assembly	ISS Inferred from Sequence or Structural Similarity more info
involved_in bicellular tight junction assembly	IDA Inferred from Direct Assay more info	PubMed
involved_in calcium ion transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in calcium ion transport	IDA Inferred from Direct Assay more info	PubMed
involved_in cellular response to hormone stimulus	IBA Inferred from Biological aspect of Ancestor more info
involved_in cellular response to vascular endothelial growth factor stimulus	ISS Inferred from Sequence or Structural Similarity more info
involved_in heart development	ISS Inferred from Sequence or Structural Similarity more info
involved_in intracellular protein transport	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of endothelial cell apoptotic process	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of vascular permeability	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of angiogenesis	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of gene expression	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of vasculogenesis	IEA Inferred from Electronic Annotation more info
involved_in protein localization to plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein localization to plasma membrane	IDA Inferred from Direct Assay more info	PubMed
involved_in protein transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein transport	IDA Inferred from Direct Assay more info	PubMed
involved_in receptor internalization	IBA Inferred from Biological aspect of Ancestor more info
involved_in receptor internalization	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of G protein-coupled receptor signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in regulation of blood pressure	ISS Inferred from Sequence or Structural Similarity more info
involved_in sprouting angiogenesis	ISS Inferred from Sequence or Structural Similarity more info
involved_in vascular associated smooth muscle cell development	ISS Inferred from Sequence or Structural Similarity more info
involved_in vasculogenesis	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of adrenomedullin receptor complex	IDA Inferred from Direct Assay more info	PubMed
is_active_in cell surface	IBA Inferred from Biological aspect of Ancestor more info
located_in cell surface	IDA Inferred from Direct Assay more info	PubMed
located_in clathrin-coated pit	TAS Traceable Author Statement more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in lysosome	TAS Traceable Author Statement more info	PubMed
colocalizes_with plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	TAS Traceable Author Statement more info
part_of receptor complex	IBA Inferred from Biological aspect of Ancestor more info
part_of receptor complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: receptor activity-modifying protein 2

Names: CRLR activity-modifying protein 2; calcitonin receptor-like receptor activity modifying protein 2; receptor (G protein-coupled) activity modifying protein 2; receptor (calcitonin) activity modifying protein 2

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.