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Protein

G-protein coupled receptor 39

Gene

GPR39

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Zn2+ acts as a agonist. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated mainly through G(q)-alpha and G(12)/G(13) proteins. Involved in regulation of body weight, gastrointestinal mobility, hormone secretion and cell death (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171Zinc1 Publication
Metal bindingi19 – 191Zinc1 Publication

GO - Molecular functioni

  • G-protein coupled receptor activity Source: ProtInc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • G-protein coupled receptor signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-373076. Class A/1 (Rhodopsin-like receptors).

Names & Taxonomyi

Protein namesi
Recommended name:
G-protein coupled receptor 39
Gene namesi
Name:GPR39
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:4496. GPR39.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3434ExtracellularBy similarityAdd
BLAST
Transmembranei35 – 5521Helical; Name=1By similarityAdd
BLAST
Topological domaini56 – 6914CytoplasmicBy similarityAdd
BLAST
Transmembranei70 – 8920Helical; Name=2By similarityAdd
BLAST
Topological domaini90 – 10920ExtracellularBy similarityAdd
BLAST
Transmembranei110 – 13122Helical; Name=3By similarityAdd
BLAST
Topological domaini132 – 15120CytoplasmicBy similarityAdd
BLAST
Transmembranei152 – 17221Helical; Name=4By similarityAdd
BLAST
Topological domaini173 – 21745ExtracellularBy similarityAdd
BLAST
Transmembranei218 – 24225Helical; Name=5By similarityAdd
BLAST
Topological domaini243 – 28341CytoplasmicBy similarityAdd
BLAST
Transmembranei284 – 30522Helical; Name=6By similarityAdd
BLAST
Topological domaini306 – 32318ExtracellularBy similarityAdd
BLAST
Transmembranei324 – 34421Helical; Name=7By similarityAdd
BLAST
Topological domaini345 – 453109CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171H → A: Decreases activation by Zn(2+). Abolishes activation by Zn(2+); when associated with A-19. 1 Publication
Mutagenesisi19 – 191H → A: Decreases activation by Zn(2+). Abolishes activation by Zn(2+); when associated with A-17. 1 Publication
Mutagenesisi312 – 3121H → A: Not affect constitutive or Zn(2+)-induced activation. 1 Publication
Mutagenesisi313 – 3131D → A: Induces very high constitutive activity and eliminates Zn(2+)-induced activation. 1 Publication

Organism-specific databases

PharmGKBiPA28885.

Chemistry

ChEMBLiCHEMBL3091266.
GuidetoPHARMACOLOGYi105.

Polymorphism and mutation databases

BioMutaiGPR39.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453G-protein coupled receptor 39PRO_0000069565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi11 ↔ 191PROSITE-ProRule annotation1 Publication
Disulfide bondi108 ↔ 210PROSITE-ProRule annotation1 Publication
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence analysis
Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence analysis
Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiO43194.
MaxQBiO43194.
PaxDbiO43194.
PRIDEiO43194.

PTM databases

PhosphoSiteiO43194.
SwissPalmiO43194.

Expressioni

Tissue specificityi

Expressed in many tissues, including the stomach, intestine and hypothalamus.1 Publication

Gene expression databases

BgeeiO43194.
CleanExiHS_GPR39.
ExpressionAtlasiO43194. baseline and differential.
GenevisibleiO43194. HS.

Organism-specific databases

HPAiHPA022111.

Interactioni

Protein-protein interaction databases

BioGridi109121. 1 interaction.
IntActiO43194. 1 interaction.
MINTiMINT-8247496.
STRINGi9606.ENSP00000327417.

Chemistry

BindingDBiO43194.

Structurei

3D structure databases

ProteinModelPortaliO43194.
SMRiO43194. Positions 30-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00700000104070.
HOGENOMiHOG000077769.
HOVERGENiHBG051809.
InParanoidiO43194.
KOiK08412.
OMAiSHRGLTC.
OrthoDBiEOG7N37CJ.
PhylomeDBiO43194.
TreeFamiTF331140.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43194-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPSLPGSD CSQIIDHSHV PEFEVATWIK ITLILVYLII FVMGLLGNSA
60 70 80 90 100
TIRVTQVLQK KGYLQKEVTD HMVSLACSDI LVFLIGMPME FYSIIWNPLT
110 120 130 140 150
TSSYTLSCKL HTFLFEACSY ATLLHVLTLS FERYIAICHP FRYKAVSGPC
160 170 180 190 200
QVKLLIGFVW VTSALVALPL LFAMGTEYPL VNVPSHRGLT CNRSSTRHHE
210 220 230 240 250
QPETSNMSIC TNLSSRWTVF QSSIFGAFVV YLVVLLSVAF MCWNMMQVLM
260 270 280 290 300
KSQKGSLAGG TRPPQLRKSE SEESRTARRQ TIIFLRLIVV TLAVCWMPNQ
310 320 330 340 350
IRRIMAAAKP KHDWTRSYFR AYMILLPFSE TFFYLSSVIN PLLYTVSSQQ
360 370 380 390 400
FRRVFVQVLC CRLSLQHANH EKRLRVHAHS TTDSARFVQR PLLFASRRQS
410 420 430 440 450
SARRTEKIFL STFQSEAEPQ SKSQSLSLES LEPNSGAKPA NSAAENGFQE

HEV
Length:453
Mass (Da):51,329
Last modified:June 1, 1998 - v1
Checksum:i8E3A233420D9021E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501A → V.1 Publication
Corresponds to variant rs2241764 [ dbSNP | Ensembl ].
VAR_022067
Natural varianti390 – 3901R → C.
Corresponds to variant rs16838944 [ dbSNP | Ensembl ].
VAR_049393

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034633 mRNA. Translation: AAC26082.1.
FJ348258 mRNA. Translation: ACI96302.1.
AK314895 mRNA. Translation: BAG37409.1.
AC098800 Genomic DNA. Translation: AAY24154.1.
AC079773 Genomic DNA. No translation available.
BC125046 mRNA. Translation: AAI25047.1.
CCDSiCCDS2170.1.
RefSeqiNP_001499.1. NM_001508.2.
UniGeneiHs.432395.
Hs.744392.

Genome annotation databases

EnsembliENST00000329321; ENSP00000327417; ENSG00000183840.
GeneIDi2863.
KEGGihsa:2863.
UCSCiuc002ttl.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034633 mRNA. Translation: AAC26082.1.
FJ348258 mRNA. Translation: ACI96302.1.
AK314895 mRNA. Translation: BAG37409.1.
AC098800 Genomic DNA. Translation: AAY24154.1.
AC079773 Genomic DNA. No translation available.
BC125046 mRNA. Translation: AAI25047.1.
CCDSiCCDS2170.1.
RefSeqiNP_001499.1. NM_001508.2.
UniGeneiHs.432395.
Hs.744392.

3D structure databases

ProteinModelPortaliO43194.
SMRiO43194. Positions 30-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109121. 1 interaction.
IntActiO43194. 1 interaction.
MINTiMINT-8247496.
STRINGi9606.ENSP00000327417.

Chemistry

BindingDBiO43194.
ChEMBLiCHEMBL3091266.
GuidetoPHARMACOLOGYi105.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiO43194.
SwissPalmiO43194.

Polymorphism and mutation databases

BioMutaiGPR39.

Proteomic databases

EPDiO43194.
MaxQBiO43194.
PaxDbiO43194.
PRIDEiO43194.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329321; ENSP00000327417; ENSG00000183840.
GeneIDi2863.
KEGGihsa:2863.
UCSCiuc002ttl.4. human.

Organism-specific databases

CTDi2863.
GeneCardsiGPR39.
H-InvDBHIX0023914.
HGNCiHGNC:4496. GPR39.
HPAiHPA022111.
MIMi602886. gene.
neXtProtiNX_O43194.
PharmGKBiPA28885.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00700000104070.
HOGENOMiHOG000077769.
HOVERGENiHBG051809.
InParanoidiO43194.
KOiK08412.
OMAiSHRGLTC.
OrthoDBiEOG7N37CJ.
PhylomeDBiO43194.
TreeFamiTF331140.

Enzyme and pathway databases

ReactomeiR-HSA-373076. Class A/1 (Rhodopsin-like receptors).

Miscellaneous databases

ChiTaRSiGPR39. human.
GeneWikiiGPR39.
GenomeRNAii2863.
NextBioi11289.
PROiO43194.
SOURCEiSearch...

Gene expression databases

BgeeiO43194.
CleanExiHS_GPR39.
ExpressionAtlasiO43194. baseline and differential.
GenevisibleiO43194. HS.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of two human G protein-coupled receptor genes (GPR38 and GPR39) related to the growth hormone secretagogue and neurotensin receptors."
    McKee K.K., Tan C.P., Palyha O.C., Liu J., Feighner S.D., Hreniuk D.L., Smith R.G., Howard A.D., van der Ploeg L.H.T.
    Genomics 46:426-434(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Isolation of cDNA coding for Homo sapiens G protein-coupled receptor 39 (GPR39)."
    Kaighin V.A., Martin A.L., Aronstam R.S.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-50.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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].
  6. "A second disulfide bridge from the N-terminal domain to extracellular loop 2 dampens receptor activity in GPR39."
    Storjohann L., Holst B., Schwartz T.W.
    Biochemistry 47:9198-9207(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  7. "Molecular mechanism of Zn2+ agonism in the extracellular domain of GPR39."
    Storjohann L., Holst B., Schwartz T.W.
    FEBS Lett. 582:2583-2588(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ZINC-BINDING SITES, MUTAGENESIS OF HIS-17; HIS-19; HIS-312 AND ASP-313.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGPR39_HUMAN
AccessioniPrimary (citable) accession number: O43194
Secondary accession number(s): B2RC12
, B6V9G4, Q08AS2, Q53R01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.