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O60894 (RAMP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. 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 1
Alternative name(s):
Calcitonin-receptor-like receptor activity-modifying protein 1
Short name=CRLR activity-modifying protein 1
Gene names
Name:RAMP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length148 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 calcitonin-gene-related peptide (CGRP) together with CALCRL. Ref.1

Subunit structure

Heterodimer of CALCRL and RAMP1. Ref.6 Ref.7

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in many tissues including the uterus, bladder, brain, pancreas and gastro-intestinal tract. Ref.1

Sequence similarities

Belongs to the RAMP family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from direct assay PubMed 20596610. Source: UniProtKB

calcium ion transport

Inferred from direct assay PubMed 10882736. Source: UniProtKB

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

positive regulation of cAMP biosynthetic process

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

positive regulation of protein glycosylation

Inferred from direct assay Ref.1. Source: UniProtKB

protein localization to plasma membrane

Inferred from direct assay PubMed 10882736. Source: UniProtKB

protein transport

Inferred from direct assay PubMed 10882736. Source: UniProtKB

receptor internalization

Inferred from direct assay PubMed 15613468. Source: UniProtKB

regulation of G-protein coupled receptor protein signaling pathway

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay PubMed 14722252. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Inferred from direct assay PubMed 18039931. Source: BHF-UCL

receptor complex

Inferred from direct assay PubMed 15613468. Source: UniProtKB

   Molecular_functioncalcitonin receptor activity

Inferred from direct assay Ref.1. Source: UniProtKB

calcitonin receptor binding

Inferred from physical interaction Ref.1. Source: UniProtKB

coreceptor activity

Inferred from electronic annotation. Source: Ensembl

protein transporter activity

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

receptor activity

Inferred from direct assay PubMed 10882736PubMed 14722252. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 148122Receptor activity-modifying protein 1
PRO_0000030168

Regions

Topological domain27 – 11791Extracellular Potential
Transmembrane118 – 13821Helical; Potential
Topological domain139 – 14810Cytoplasmic Potential

Amino acid modifications

Disulfide bond27 ↔ 82 Ref.6 Ref.7
Disulfide bond40 ↔ 72 Ref.6 Ref.7
Disulfide bond57 ↔ 104 Ref.6 Ref.7

Secondary structure

.............. 148
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O60894 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 8530DD590BAEBE5C

FASTA14816,988
        10         20         30         40         50         60 
MARALCRLPR RGLWLLLAHH LFMTTACQEA NYGALLRELC LTQFQVDMEA VGETLWCDWG 

        70         80         90        100        110        120 
RTIRSYRELA DCTWHMAEKL GCFWPNAEVD RFFLAVHGRY FRSCPISGRA VRDPPGSILY 

       130        140 
PFIVVPITVT LLVTALVVWQ SKRTEGIV 

« 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, TOPOLOGY.
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: Lung.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Brain.
[6]"Crystal structure of the human receptor activity-modifying protein 1 extracellular domain."
Kusano S., Kukimoto-Niino M., Akasaka R., Toyama M., Terada T., Shirouzu M., Shindo T., Yokoyama S.
Protein Sci. 17:1907-1914(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-112, SUBUNIT, DISULFIDE BONDS.
[7]"Crystal structure of the ectodomain complex of the CGRP receptor, a class-B GPCR, reveals the site of drug antagonism."
ter Haar E., Koth C.M., Abdul-Manan N., Swenson L., Coll J.T., Lippke J.A., Lepre C.A., Garcia-Guzman M., Moore J.M.
Structure 18:1083-1093(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 26-117 IN COMPLEX WITH CALRL AND ANTAGONIST, SUBUNIT, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001014 mRNA. Translation: CAA04472.1.
AY265457 mRNA. Translation: AAP23298.1.
CR542032 mRNA. Translation: CAG46829.1.
CR542044 mRNA. Translation: CAG46841.1.
CH471063 Genomic DNA. Translation: EAW71127.1.
BC000548 mRNA. Translation: AAH00548.1.
RefSeqNP_005846.1. NM_005855.2.
UniGeneHs.471783.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YX8X-ray2.40A27-112[»]
3N7PX-ray2.80D/E/F/R26-117[»]
3N7RX-ray2.90C/D26-117[»]
3N7SX-ray2.10C/D26-117[»]
ProteinModelPortalO60894.
SMRO60894. Positions 26-116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115558. 3 interactions.
DIPDIP-37675N.
IntActO60894. 1 interaction.
STRING9606.ENSP00000254661.

Chemistry

BindingDBO60894.
ChEMBLCHEMBL2107838.
DrugBankDB01278. Pramlintide.

Proteomic databases

PaxDbO60894.
PRIDEO60894.

Protocols and materials databases

DNASU10267.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254661; ENSP00000254661; ENSG00000132329.
GeneID10267.
KEGGhsa:10267.
UCSCuc002vxj.3. human.

Organism-specific databases

CTD10267.
GeneCardsGC02P238767.
HGNCHGNC:9843. RAMP1.
HPAHPA057814.
MIM605153. gene.
neXtProtNX_O60894.
PharmGKBPA34202.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41532.
HOGENOMHOG000253018.
HOVERGENHBG061268.
InParanoidO60894.
KOK08447.
OMAWRSKRPE.
OrthoDBEOG7ZKSD3.
PhylomeDBO60894.
TreeFamTF333286.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressO60894.
BgeeO60894.
CleanExHS_RAMP1.
GenevestigatorO60894.

Family and domain databases

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

Other

ChiTaRSRAMP1. human.
EvolutionaryTraceO60894.
GeneWikiRAMP1.
GenomeRNAi10267.
NextBio38898.
PROO60894.
SOURCESearch...

Entry information

Entry nameRAMP1_HUMAN
AccessionPrimary (citable) accession number: O60894
Secondary accession number(s): Q6FGS5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 116 of the entry and version 1 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 2

Human chromosome 2: entries, gene names and cross-references to MIM