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Database: UniProt
Entry: A0A3P9NAU0_POERE
LinkDB: A0A3P9NAU0_POERE
Original site: A0A3P9NAU0_POERE 
ID   A0A3P9NAU0_POERE        Unreviewed;       800 AA.
AC   A0A3P9NAU0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Metabotropic glutamate receptor 3 {ECO:0000256|ARBA:ARBA00020281};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000006671.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000006671.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000006671.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: G-protein coupled receptor for glutamate. Ligand binding
CC       causes a conformation change that triggers signaling via guanine
CC       nucleotide-binding proteins (G proteins) and modulates the activity of
CC       down-stream effectors. Signaling inhibits adenylate cyclase activity.
CC       {ECO:0000256|ARBA:ARBA00025645}.
CC   -!- SUBUNIT: Interacts with TAMALIN. {ECO:0000256|ARBA:ARBA00011150}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC       {ECO:0000256|ARBA:ARBA00007242}.
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DR   Ensembl; ENSPRET00000006758.1; ENSPREP00000006671.1; ENSPREG00000004457.1.
DR   GeneTree; ENSGT01030000234595; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000004457; Expressed in head.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   CDD; cd15284; 7tmC_mGluR_group2; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 2.10.50.30; GPCR, family 3, nine cysteines domain; 1.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR000337; GPCR_3.
DR   InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR   InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR017979; GPCR_3_CS.
DR   InterPro; IPR001234; GPCR_3_mGluR3.
DR   InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR24060; METABOTROPIC GLUTAMATE RECEPTOR; 1.
DR   PANTHER; PTHR24060:SF160; METABOTROPIC GLUTAMATE RECEPTOR 3; 1.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF07562; NCD3G; 1.
DR   PRINTS; PR00248; GPCRMGR.
DR   PRINTS; PR01053; MTABOTROPC3R.
DR   PRINTS; PR00593; MTABOTROPICR.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        492..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        531..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        608..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        656..675
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        687..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        715..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          493..761
FT                   /note="G-protein coupled receptors family 3 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50259"
SQ   SEQUENCE   800 AA;  89318 MW;  57A57248E21AB4B2 CRC64;
     MPFSYLCFKS CSKDKPQQHT PALEFVRASL TKVDDTEFIC PDGSYALQDD NPLAIAGVIG
     GSYSSVSIQV ANLLRLFQIP QISYASTSAK LSDKTRYDYF ARTVPPDFYQ AKAMAEILRF
     FNWTYVSTVA SEGDYGETGI EAFEQEARMR NICIATSEKV GRSNAKKSYE AVIRQLFQKP
     NAHVAVLFLR SDDARELIAA AARLNTSFIW VASDGWGAQE SIVKGNEITA EGAITLELAA
     NPIPDFNRYF LSLDPVKNHR NPWFRDFWEQ RFQCSLGAGG LGFGGTPLPP CDKNLSMDQR
     YFEPESKIMF VVNAVYAMAX ALHNMQRSLC LNTTKLCDSM KALDGRRLYR DYILNVSFTA
     PLSPPGSETV VKFDSQGDGM GRYNIFSYQR SGERYGYVPV GEWAESLSLN NDLIRWPKEV
     LPTSQCSDPC ERNEMKKMQA GEYCCWICTA CEPHEYLADE FTCSPCAPGQ WPTDDLTSCY
     DLPEDYIMWE DAWAIGPITI ACVGFVCTGL VVWVFVRHNN TPLVKASGRE LCYILLSGVF
     MCYAMTFLFL AKPSPAICAL RRLGLGTSFA VCYSALLTKT NRIARIFNGV KDGAGAVRPR
     FISPSSQVFI CLSLISVQLV MVSVWLLLEV PGTRRFTLPE RRQTVILKCN VRDSSMLLSL
     GYDVLLVILC TVYAFKTRKC PENFNEAKFI GFTMYTTCII WLAFLPIFYV TSSDYRVQTT
     TMCISVSLSG FVVLGCMFAP KVNIIMFQPQ KNVTSHHLNL NRFSVSGAAT TYASHASVSA
     HFVPTVCNGR EIVDSTTSSL
//
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