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Q99P50 (GHSR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: HGNC

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: Ensembl

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: Ensembl

regulation of synapse assembly

Inferred from mutant phenotype PubMed 17060947. Source: MGI

response to food

Inferred from direct assay PubMed 16513828. Source: MGI

response to hormone

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell surface

Inferred from sequence or structural similarity. Source: HGNC

integral component of 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_functionG-protein coupled receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

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: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Growth hormone secretagogue receptor type 1
PRO_0000069480

Regions

Topological domain1 – 4040Extracellular Potential
Transmembrane41 – 6626Helical; Name=1; Potential
Topological domain67 – 726Cytoplasmic Potential
Transmembrane73 – 9624Helical; Name=2; Potential
Topological domain97 – 11721Extracellular Potential
Transmembrane118 – 13922Helical; Name=3; Potential
Topological domain140 – 16223Cytoplasmic Potential
Transmembrane163 – 18321Helical; Name=4; Potential
Topological domain184 – 21128Extracellular Potential
Transmembrane212 – 23524Helical; Name=5; Potential
Topological domain236 – 26328Cytoplasmic Potential
Transmembrane264 – 28522Helical; Name=6; Potential
Topological domain286 – 30217Extracellular Potential
Transmembrane303 – 32624Helical; Name=7; Potential
Topological domain327 – 36438Cytoplasmic Potential

Amino acid modifications

Glycosylation131N-linked (GlcNAc...) Potential
Glycosylation261N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Disulfide bond115 ↔ 197 By similarity

Experimental info

Sequence conflict591G → S in AAL13336. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99P50 [UniParc].

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

FASTA36440,969
        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' 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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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.
CCDSCCDS17273.1.
RefSeqNP_796304.1. NM_177330.4.
UniGeneMm.194721.

3D structure databases

ProteinModelPortalQ99P50.
SMRQ99P50. Positions 45-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000061153.

Chemistry

BindingDBQ99P50.
ChEMBLCHEMBL3428.
GuidetoPHARMACOLOGY246.

Protein family/group databases

GPCRDBSearch...

Proteomic databases

PRIDEQ99P50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057186; ENSMUSP00000061153; ENSMUSG00000051136.
GeneID208188.
KEGGmmu:208188.
UCSCuc008oto.1. mouse.

Organism-specific databases

CTD2693.
MGIMGI:2441906. Ghsr.

Phylogenomic databases

eggNOGNOG303294.
GeneTreeENSGT00700000104070.
HOGENOMHOG000272571.
HOVERGENHBG006538.
InParanoidQ99P50.
KOK04284.
OMAMVWVSSV.
OrthoDBEOG7992QV.
PhylomeDBQ99P50.
TreeFamTF332184.

Gene expression databases

BgeeQ99P50.
CleanExMM_GHSR.
GenevestigatorQ99P50.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR003905. GHS-R.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR01417. GHSRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio372206.
PROQ99P50.
SOURCESearch...

Entry information

Entry nameGHSR_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries