Growth hormone secretagogue receptor type 1

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Q99P50 (GHSR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Growth hormone secretagogue receptor type 1
Short name=GHS-R

Alternative name(s):
GH-releasing peptide receptor
Short name=GHRP
Ghrelin receptor

Gene names

Name:

Ghsr

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Binds also other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-0677, adenosine) By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin polymerization or depolymerization Inferred from sequence or structural similarity. Source: UniProtKB adult feeding behavior Inferred from mutant phenotype PubMed 16322794. Source: HGNC cellular response to insulin stimulus Inferred from direct assay PubMed 16513828. Source: MGI decidualization Inferred from sequence or structural similarity. Source: UniProtKB growth hormone secretion Inferred from genetic interaction PubMed 15070777. Source: MGI hormone-mediated signaling pathway Inferred from sequence or structural similarity. Source: HGNC negative regulation of inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of insulin secretion Inferred from sequence orthology PubMed 17130496. Source: MGI negative regulation of interleukin-1 beta production Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of interleukin-6 biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of tumor necrosis factor biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of appetite Inferred from mutant phenotype PubMed 16322794. Source: HGNC positive regulation of fatty acid metabolic process Inferred from electronic annotation. Source: Compara positive regulation of insulin-like growth factor receptor signaling pathway Inferred from mutant phenotype PubMed 15070777. Source: MGI positive regulation of multicellular organism growth Inferred from sequence or structural similarity. Source: HGNC regulation of hindgut contraction Inferred from electronic annotation. Source: Compara regulation of synapse assembly Inferred from mutant phenotype PubMed 17060947. Source: MGI response to food Inferred from direct assay PubMed 16513828. Source: MGI
Cellular_component	cell surface Inferred from sequence or structural similarity. Source: HGNC integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane raft Inferred from sequence or structural similarity. Source: UniProtKB neuron projection Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	growth hormone secretagogue receptor activity Inferred from sequence or structural similarity. Source: HGNC growth hormone-releasing hormone receptor activity Inferred from sequence or structural similarity. Source: HGNC peptide hormone binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 364

364

Growth hormone secretagogue receptor type 1

PRO_0000069480

Regions

Topological domain

1 – 40

Extracellular Potential

Transmembrane

41 – 66

Helical; Name=1; Potential

Topological domain

67 – 72

Cytoplasmic Potential

Transmembrane

73 – 96

Helical; Name=2; Potential

Topological domain

97 – 117

Extracellular Potential

Transmembrane

118 – 139

Helical; Name=3; Potential

Topological domain

140 – 162

Cytoplasmic Potential

Transmembrane

163 – 183

Helical; Name=4; Potential

Topological domain

184 – 211

Extracellular Potential

Transmembrane

212 – 235

Helical; Name=5; Potential

Topological domain

236 – 263

Cytoplasmic Potential

Transmembrane

264 – 285

Helical; Name=6; Potential

Topological domain

286 – 302

Extracellular Potential

Transmembrane

303 – 326

Helical; Name=7; Potential

Topological domain

327 – 364

Cytoplasmic Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

187

N-linked (GlcNAc...) Potential

Disulfide bond

115 ↔ 197

By similarity

Experimental info

Sequence conflict

G → S in AAL13336. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q99P50 [UniParc].

Last modified May 10, 2004. Version 3.
Checksum: 8F1214E58EF3B2E8
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FASTA

364

40,969

        10         20         30         40         50         60 
MWNATPSEEP EPNVTLDLDW DASPGNDSLS DELLPLFPAP LLAGVTATCV ALFVVGISGN 

        70         80         90        100        110        120 
LLTMLVVSRF RELRTTTNLY LSSMAFSDLL IFLCMPLDLV RLWQYRPWNF GDLLCKLFQF 

       130        140        150        160        170        180 
VSESCTYATV LTITALSVER YFAICFPLRA KVVVTKGRVK LVILVIWAVA FCSAGPIFVL 

       190        200        210        220        230        240 
VGVEHENGTD PRDTNECRAT EFAVRSGLLT VMVWVSSVFF FLPVFCLTVL YSLIGRKLWR 

       250        260        270        280        290        300 
RRGDAAVGSS LRDQNHKQTV KMLAVVVFAF ILCWLPFHVG RYLFSKSFEP GSLEIAQISQ 

       310        320        330        340        350        360 
YCNLVSFVLF YLSAAINPIL YNIMSKKYRV AVFKLLGFES FSQRKLSTLK DESSRAWTKS 


SINT

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Spinal cord.
[2]	"Cloning of mouse ghrelin/growth hormone secretagogue receptor cDNA by rapid amplification of cDNA ends (RACE)." Kacsoh B. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-183. Strain: C57BL/6J. Tissue: Hypothalamus.
[3]	Peng X., Frohman L.A., Kineman R.D. Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 73-257. Strain: 129S3/SvImJ.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK049671 mRNA. Translation: BAC33866.1. AY056474 mRNA. Translation: AAL13336.1. AF332997 mRNA. Translation: AAG61141.1.
IPI	IPI00226537.
RefSeq	NP_796304.1. NM_177330.4.
UniGene	Mm.194721.
3D structure databases
ProteinModelPortal	Q99P50.
SMR	Q99P50. Positions 41-338.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000061153.
Protein family/group databases
GPCRDB	Search...
Proteomic databases
PRIDE	Q99P50.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000057186; ENSMUSP00000061153; ENSMUSG00000051136.
GeneID	208188.
KEGG	mmu:208188.
Organism-specific databases
CTD	2693.
MGI	MGI:2441906. Ghsr.
Phylogenomic databases
eggNOG	NOG303294.
GeneTree	ENSGT00700000104070.
HOGENOM	HOG000272571.
HOVERGEN	HBG006538.
InParanoid	Q99P50.
KO	K04284.
OMA	MVWVSSV.
OrthoDB	EOG4FFD28.
Gene expression databases
ArrayExpress	Q99P50.
Bgee	Q99P50.
CleanEx	MM_GHSR.
Genevestigator	Q99P50.
GermOnline	ENSMUSG00000051136. Mus musculus.
Family and domain databases
InterPro	IPR003905. GHS-R. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR01417. GHSRECEPTOR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q99P50.
ChEMBL	CHEMBL3428.
NextBio	372206.
SOURCE	Search...

Entry information

Entry name

GHSR_MOUSE

Accession

Primary (citable) accession number: Q99P50
Secondary accession number(s): Q8BWX8, Q91Z82

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 11, 2002
Last sequence update:	May 10, 2004
Last modified:	May 1, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents