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O60895 (RAMP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor activity-modifying protein 2
Alternative name(s):
Calcitonin-receptor-like receptor activity-modifying protein 2
Short name=CRLR activity-modifying protein 2
Gene names
Name:RAMP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL. Ref.1 Ref.5

Subunit structure

Heterodimer of CALCRL and RAMP2 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Strongly expressed in lung, breast, immune system and fetal tissues. Ref.1

Sequence similarities

Belongs to the RAMP family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

adherens junction assembly

Inferred from direct assay PubMed 18097473. Source: UniProtKB

angiogenesis

Inferred from direct assay PubMed 20596610. Source: UniProtKB

basement membrane assembly

Inferred from sequence or structural similarity. Source: UniProtKB

cAMP biosynthetic process

Inferred from direct assay PubMed 20074556. Source: UniProtKB

calcium ion transport

Inferred from direct assay PubMed 10882736. Source: UniProtKB

cellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to vascular endothelial growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

female pregnancy

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

negative regulation of endothelial cell apoptotic process

Inferred from direct assay PubMed 18097473. Source: UniProtKB

negative regulation of vascular permeability

Inferred from direct assay PubMed 18097473. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cAMP biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of gene expression

Inferred from direct assay PubMed 18097473. Source: UniProtKB

positive regulation of vasculogenesis

Inferred from electronic annotation. Source: Ensembl

protein localization to plasma membrane

Inferred from direct assay PubMed 10882736. Source: UniProtKB

protein transport

Inferred from direct assay PubMed 10882736Ref.1. Source: UniProtKB

receptor internalization

Inferred from direct assay PubMed 10882736PubMed 15613468PubMed 20074556. Source: UniProtKB

regulation of G-protein coupled receptor protein signaling pathway

Inferred from electronic annotation. Source: InterPro

regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

sprouting angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

tight junction assembly

Inferred from direct assay PubMed 18097473. Source: UniProtKB

vascular smooth muscle cell development

Inferred from sequence or structural similarity. Source: UniProtKB

vasculogenesis

Inferred from mutant phenotype PubMed 16964401. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay PubMed 14722252. Source: UniProtKB

coated pit

Traceable author statement PubMed 10882736. Source: ProtInc

cytoplasm

Inferred from direct assay PubMed 10882736. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

lysosome

Traceable author statement PubMed 10882736. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 15613468. Source: UniProtKB

   Molecular_functioncoreceptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20596610Ref.1. Source: UniProtKB

protein transporter activity

Inferred from direct assay PubMed 10882736Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242 Potential
Chain43 – 175133Receptor activity-modifying protein 2
PRO_0000030172

Regions

Topological domain43 – 145103Extracellular Potential
Transmembrane146 – 16621Helical; Potential
Topological domain167 – 1759Cytoplasmic Potential

Amino acid modifications

Glycosylation1301N-linked (GlcNAc...) Potential
Disulfide bond68 ↔ 99 Ref.4 Ref.5
Disulfide bond84 ↔ 131 Ref.4 Ref.5

Experimental info

Sequence conflict251L → V in CAA04473. Ref.1

Secondary structure

......... 175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O60895 [UniParc].

Last modified January 10, 2003. Version 2.
Checksum: AF69A9A461EFFCA3

FASTA17519,608
        10         20         30         40         50         60 
MASLRVERAG GPRLPRTRVG RPAALRLLLL LGAVLNPHEA LAQPLPTTGT PGSEGGTVKN 

        70         80         90        100        110        120 
YETAVQFCWN HYKDQMDPIE KDWCDWAMIS RPYSTLRDCL EHFAELFDLG FPNPLAERII 

       130        140        150        160        170 
FETHQIHFAN CSLVQPTFSD PPEDVLLAMI IAPICLIPFL ITLVVWRSKD SEAQA 

« Hide

References

« Hide 'large scale' references
[1]"RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor."
McLatchie L.M., Fraser N.J., Main M.J., Wise A., Brown J., Thompson N., Solari R., Lee M.G., Foord S.M.
Nature 393:333-339(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Neuroblastoma.
[2]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Kopatz S.A., Aronstam R.S., Sharma S.V.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[4]"Structure of the extracellular domain of human RAMP2."
Structural genomics consortium (SGC)
Submitted (DEC-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 48-139, DISULFIDE BONDS.
[5]"Structural basis for extracellular interactions between calcitonin receptor-like receptor and receptor activity-modifying protein 2 for adrenomedullin-specific binding."
Kusano S., Kukimoto-Niino M., Hino N., Ohsawa N., Okuda K., Sakamoto K., Shirouzu M., Shindo T., Yokoyama S.
Protein Sci. 21:199-210(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 52-139 IN COMPLEX WITH CALCRL, FUNCTION, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001015 mRNA. Translation: CAA04473.1.
AY265458 mRNA. Translation: AAP23299.1.
BC027975 mRNA. Translation: AAH27975.1.
CCDSCCDS11437.1.
RefSeqNP_005845.2. NM_005854.2.
UniGeneHs.514193.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XVTX-ray2.05A/B/C/D/E/F48-139[»]
3AQEX-ray2.00A/B/C/D/E/F56-139[»]
3AQFX-ray2.60A56-139[»]
ProteinModelPortalO60895.
SMRO60895. Positions 60-135.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115557. 1 interaction.
STRING9606.ENSP00000253796.

Chemistry

ChEMBLCHEMBL2364173.
DrugBankDB01278. Pramlintide.

PTM databases

PhosphoSiteO60895.

Proteomic databases

PaxDbO60895.
PRIDEO60895.

Protocols and materials databases

DNASU10266.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253796; ENSP00000253796; ENSG00000131477.
GeneID10266.
KEGGhsa:10266.
UCSCuc002ibg.3. human.

Organism-specific databases

CTD10266.
GeneCardsGC17P040913.
HGNCHGNC:9844. RAMP2.
MIM605154. gene.
neXtProtNX_O60895.
PharmGKBPA34203.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42995.
HOGENOMHOG000230963.
HOVERGENHBG067366.
InParanoidO60895.
KOK08448.
PhylomeDBO60895.
TreeFamTF333286.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressO60895.
BgeeO60895.
CleanExHS_RAMP2.
GenevestigatorO60895.

Family and domain databases

InterProIPR006985. RAMP.
[Graphical view]
PANTHERPTHR14076. PTHR14076. 1 hit.
PfamPF04901. RAMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAMP2.
GenomeRNAi10266.
NextBio38894.
PROO60895.
SOURCESearch...

Entry information

Entry nameRAMP2_HUMAN
AccessionPrimary (citable) accession number: O60895
Secondary accession number(s): Q8N1F2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 10, 2003
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM