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GP173_RAT
ID   GP173_RAT               Reviewed;         373 AA.
AC   Q9JJH2;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Probable G-protein coupled receptor 173;
DE   AltName: Full=Super conserved receptor expressed in brain 3;
GN   Name=Gpr173; Synonyms=Sreb3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=10833454; DOI=10.1006/bbrc.2000.2829;
RA   Matsumoto M., Saito T., Takasaki J., Kamohara M., Sugimoto T.,
RA   Kobayashi M., Tadokoro M., Matsumoto S., Ohishi T., Furuichi K.;
RT   "An evolutionarily conserved G-protein coupled receptor family, SREB,
RT   expressed in the central nervous system.";
RL   Biochem. Biophys. Res. Commun. 272:576-582(2000).
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=27440717; DOI=10.1152/ajpregu.00191.2016;
RA   Stein L.M., Tullock C.W., Mathews S.K., Garcia-Galiano D., Elias C.F.,
RA   Samson W.K., Yosten G.L.;
RT   "Hypothalamic action of phoenixin to control reproductive hormone secretion
RT   in females: importance of the orphan G protein-coupled receptor Gpr173.";
RL   Am. J. Physiol. 311:R489-R496(2016).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=30251651; DOI=10.1016/j.bbalip.2018.09.006;
RA   Billert M., Wojciechowicz T., Jasaszwili M., Szczepankiewicz D., Wasko J.,
RA   Kazmierczak S., Strowski M.Z., Nowak K.W., Skrzypski M.;
RT   "Phoenixin-14 stimulates differentiation of 3T3-L1 preadipocytes via
RT   cAMP/Epac-dependent mechanism.";
RL   Biochim. Biophys. Acta 1863:1449-1457(2018).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=31422055; DOI=10.1016/j.bbamcr.2019.118533;
RA   Billert M., Kolodziejski P.A., Strowski M.Z., Nowak K.W., Skrzypski M.;
RT   "Phoenixin-14 stimulates proliferation and insulin secretion in insulin
RT   producing INS-1E cells.";
RL   Biochim. Biophys. Acta 1866:118533-118533(2019).
CC   -!- FUNCTION: Is a receptor for the SMIM20 derived peptides Phoenixin-14
CC       and Phoenixin-20 (PubMed:27440717). It mediates the Phoenixin-14 and
CC       Phoenixin-20 augmentation of gonadotropin-releasing hormone (GNRH)
CC       signaling in the hypothalamus and pituitary gland (PubMed:27440717). In
CC       the ovary, it mediates the effects of Phoenixin-14 and Phoenixin-20
CC       induced granulosa cell proliferation during follicular growth (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NS66,
CC       ECO:0000269|PubMed:27440717}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, preadipocytes and
CC       pancreatic islet cells. {ECO:0000269|PubMed:27440717,
CC       ECO:0000269|PubMed:30251651, ECO:0000269|PubMed:31422055}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AB040804; BAA96650.1; -; mRNA.
DR   RefSeq; NP_071591.1; NM_022255.1.
DR   AlphaFoldDB; Q9JJH2; -.
DR   SMR; Q9JJH2; -.
DR   GlyGen; Q9JJH2; 2 sites.
DR   PhosphoSitePlus; Q9JJH2; -.
DR   Ensembl; ENSRNOT00000079982; ENSRNOP00000096581; ENSRNOG00000060137.
DR   GeneID; 64021; -.
DR   KEGG; rno:64021; -.
DR   CTD; 54328; -.
DR   RGD; 620748; Gpr173.
DR   GeneTree; ENSGT00890000139436; -.
DR   InParanoid; Q9JJH2; -.
DR   OrthoDB; 1311948at2759; -.
DR   PhylomeDB; Q9JJH2; -.
DR   PRO; PR:Q9JJH2; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0004968; F:gonadotropin-releasing hormone receptor activity; ISO:RGD.
DR   GO; GO:2001223; P:negative regulation of neuron migration; ISO:RGD.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..373
FT                   /note="Probable G-protein coupled receptor 173"
FT                   /id="PRO_0000069652"
FT   TOPO_DOM        1..26
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..59
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..97
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..287
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..322
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        344..373
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        96..174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   373 AA;  41511 MW;  C06DEA2F0E88CAF5 CRC64;
     MANTTGEPEE VSGALSLPSA SAYVKLVLLG LIMCVSLAGN AILSLLVLKE RALHKAPYYF
     LLDLCLADGI RSAICFPFVL ASVRHGSSWT FSALSCKIVA FMAVLFCFHA AFMLFCISVT
     RYMAIAHHRF YAKRMTLWTC AAVICMAWTL SVAMAFPPVF DVGTYKFIRE EDQCIFEHRY
     FKANDTLGFM LMLAVLMAAT HAVYGKLLLF EYRHRKMKPV QMVPAISQNW TFHGPGATGQ
     AAANWIAGFG RGPMPPTLLG IRQNGHAASR RLLGMDEVKG EKQLGRMFYA ITLLFLLLWS
     PYIVACYWRV FVKACAVPHR YLATAVWMSF AQAAVNPIVC FLLNKDLKKC LRTHAPCWGT
     GGAPAPREPY CVM
 
 
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