Skip Header

Contribute Send feedback
Read comments (?) or add your own

P49683 (PRLHR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Prolactin-releasing peptide receptor

Short name=PrRP receptor
Short name=PrRPR
Alternative name(s):
G-protein coupled receptor 10
hGR3
Gene names
Name:PRLHR
Synonyms:GPR10, GR3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for prolactin-releasing peptide (PrRP). Implicated in lactation, regulation of food intake and pain-signal processing.

Subunit structure

Interacts through its C-terminal region with the PDZ domain-containing proteins GRIP1, GRIP2 and PICK1. Interacts with PDZ domains 4 and 5 of GRIP1 and with the PDZ domain of PICK1. Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Only detected in the pituitary gland and in all cell types of pituitary adenomas. Ref.3 Ref.6

Induction

Repressed by bromocriptine, a dopamine agonist. Ref.3

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence caution

The sequence AAC50504.1 differs from that shown. Reason: Frameshift at positions 168 and 175.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Prolactin-releasing peptide receptor
PRO_0000069524

Regions

Topological domain1 – 6262Extracellular Potential
Transmembrane63 – 8321Helical; Name=1; Potential
Topological domain84 – 10118Cytoplasmic Potential
Transmembrane102 – 12221Helical; Name=2; Potential
Topological domain123 – 1264Extracellular Potential
Transmembrane127 – 14721Helical; Name=3; Potential
Topological domain148 – 17528Cytoplasmic Potential
Transmembrane176 – 19621Helical; Name=4; Potential
Topological domain197 – 22529Extracellular Potential
Transmembrane226 – 24621Helical; Name=5; Potential
Topological domain247 – 27630Cytoplasmic Potential
Transmembrane277 – 29721Helical; Name=6; Potential
Topological domain298 – 31720Extracellular Potential
Transmembrane318 – 33821Helical; Name=7; Potential
Topological domain339 – 36931Cytoplasmic Potential
Region365 – 3706Required for interaction with GRIP1, GRIP2 and PICK1

Amino acid modifications

Glycosylation271N-linked (GlcNAc...) Potential
Glycosylation361N-linked (GlcNAc...) Potential
Disulfide bond134 ↔ 211 By similarity

Natural variations

Natural variant2831I → V. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs1613448 [ dbSNP | Ensembl ].
VAR_023948
Natural variant3021D → G.
Corresponds to variant rs8192523 [ dbSNP | Ensembl ].
VAR_029746

Experimental info

Mutagenesis365 – 3706Missing: Abolishes binding to GRIP1 and PICK1. Ref.7
Mutagenesis3651T → A: No effect on binding to GRIP1. Ref.7
Mutagenesis3661V → A: No effect on binding to GRIP1. Ref.7
Mutagenesis3671S → A: Abolishes binding to GRIP1. Ref.7
Mutagenesis3681V → A: Abolishes binding to GRIP1. Ref.7
Mutagenesis3691V → A: No effect on binding to GRIP1. Ref.7
Mutagenesis3701I → A: Abolishes binding to GRIP1. Ref.7
Sequence conflict891R → P in AAC50504. Ref.1
Sequence conflict1941A → P in AAC50504. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49683 [UniParc].

Last modified November 2, 2010. Version 3.
Checksum: 47F71490A080C81F

FASTA37041,121
        10         20         30         40         50         60 
MASSTTRGPR VSDLFSGLPP AVTTPANQSA EASAGNGSVA GADAPAVTPF QSLQLVHQLK 

        70         80         90        100        110        120 
GLIVLLYSVV VVVGLVGNCL LVLVIARVRR LHNVTNFLIG NLALSDVLMC TACVPLTLAY 

       130        140        150        160        170        180 
AFEPRGWVFG GGLCHLVFFL QPVTVYVSVF TLTTIAVDRY VVLVHPLRRR ISLRLSAYAV 

       190        200        210        220        230        240 
LAIWALSAVL ALPAAVHTYH VELKPHDVRL CEEFWGSQER QRQLYAWGLL LVTYLLPLLV 

       250        260        270        280        290        300 
ILLSYVRVSV KLRNRVVPGC VTQSQADWDR ARRRRTFCLL VVIVVVFAVC WLPLHVFNLL 

       310        320        330        340        350        360 
RDLDPHAIDP YAFGLVQLLC HWLAMSSACY NPFIYAWLHD SFREELRKLL VAWPRKIAPH 

       370 
GQNMTVSVVI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and chromosomal mapping of three novel genes, GPR9, GPR10, and GPR14, encoding receptors related to interleukin 8, neuropeptide Y, and somatostatin receptors."
Marchese A., Heiber M., Nguyen T., Heng H.H.Q., Saldivia V.R., Cheng R., Murphy P.M., Tsui L.-C., Shi X., Gregor P., George S.R., O'Dowd B.F., Docherty J.M.
Genomics 29:335-344(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-283.
[2]"A prolactin-releasing peptide in the brain."
Hinuma S., Habata Y., Fujii R., Kawamata Y., Hosoya M., Fukusumi S., Kitada C., Masuo Y., Asano T., Matsumoto H., Sekiguchi M., Kurokawa T., Nishimura O., Onda H., Fujino M.
Nature 393:272-276(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-283.
[3]"Transcriptional regulation of the human PRL-releasing peptide (PrRP) receptor gene by a dopamine 2 receptor agonist: cloning and characterization of the human PrRP receptor gene and its promoter region."
Ozawa A., Yamada M., Satoh T., Monden T., Hashimoto K., Kohga H., Hashiba Y., Sasaki T., Mori M.
Mol. Endocrinol. 16:785-798(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION, VARIANT VAL-283.
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
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], VARIANT VAL-283.
[6]"Tissue distribution of prolactin-releasing peptide (PrRP) and its receptor."
Fujii R., Fukusumi S., Hosoya M., Kawamata Y., Habata Y., Hinuma S., Sekiguchi M., Kitada C., Kurokawa T., Nishimura O., Onda H., Sumino Y., Fujino M.
Regul. Pept. 83:1-10(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"The carboxyl terminus of the prolactin-releasing peptide receptor interacts with PDZ domain proteins involved in alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor clustering."
Lin S.H.S., Arai A.C., Wang Z., Nothacker H.-P., Civelli O.
Mol. Pharmacol. 60:916-923(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRIP1; GRIP2 AND PICK1, MUTAGENESIS OF THR-365; VAL-366; SER-367; VAL-368; VAL-369 AND ILE-370.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U32672 Genomic DNA. Translation: AAC50504.1. Frameshift.
AB015745 mRNA. Translation: BAA31159.1.
AB048946 Genomic DNA. Translation: BAB83030.1.
AL356865 Genomic DNA. Translation: CAH73066.1.
BC095539 mRNA. Translation: AAH95539.1.
BC101490 mRNA. Translation: AAI01491.1.
BC101492 mRNA. Translation: AAI01493.1.
IPIIPI00027755.
RefSeqNP_004239.1. NM_004248.2.
UniGeneHs.248119.

3D structure databases

ProteinModelPortalP49683.
SMRP49683. Positions 67-350.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1785715.
STRING9606.ENSP00000239032.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP49683.

Polymorphism databases

DMDM311033415.

Proteomic databases

PaxDbP49683.
PRIDEP49683.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000239032; ENSP00000239032; ENSG00000119973.
ENST00000369169; ENSP00000358167; ENSG00000119973.
GeneID2834.
KEGGhsa:2834.
UCSCuc021pzm.1. human.

Organism-specific databases

CTD2834.
GeneCardsGC10M120344.
H-InvDBHIX0170463.
HGNCHGNC:4464. PRLHR.
HPAHPA039361.
MIM600895. gene.
neXtProtNX_P49683.
PharmGKBPA28847.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267229.
HOGENOMHOG000050229.
HOVERGENHBG101109.
InParanoidP49683.
KOK04314.
OMAFIYAWLH.
OrthoDBEOG4WDDC5.
PhylomeDBP49683.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP49683.
CleanExHS_PRLHR.
GenevestigatorP49683.
GermOnlineENSG00000119973. Homo sapiens.

Family and domain databases

InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001402. Prolrel_pep_rcpt.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR01018. PRPRECEPTOR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP49683.
ChEMBLCHEMBL1681611.
GenomeRNAi2834.
NextBio11185.
SOURCESearch...

Entry information

Entry namePRLHR_HUMAN
AccessionPrimary (citable) accession number: P49683
Secondary accession number(s): O75194, Q502U8, Q5VXR9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 2, 2010
Last modified: May 1, 2013
This is version 118 of the entry and version 3 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

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families