GP173_MOUSE
ID GP173_MOUSE Reviewed; 373 AA.
AC Q6PI62; A2AHI2; Q4VA66;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=27268078; DOI=10.1210/me.2016-1039;
RA Treen A.K., Luo V., Belsham D.D.;
RT "Phoenixin Activates Immortalized GnRH and Kisspeptin Neurons Through the
RT Novel Receptor GPR173.";
RL Mol. Endocrinol. 30:872-888(2016).
RN [4]
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30933929; DOI=10.1530/rep-19-0025;
RA Nguyen X.P., Nakamura T., Osuka S., Bayasula B., Nakanishi N., Kasahara Y.,
RA Muraoka A., Hayashi S., Nagai T., Murase T., Goto M., Iwase A., Kikkawa F.;
RT "Effect of the Neuropeptide Phoenixin and Its Receptor GPR173 During
RT Folliculogenesis.";
RL Reproduction 158:25-34(2019).
CC -!- FUNCTION: Is a receptor for the SMIM20 derived peptides Phoenixin-14
CC and Phoenixin-20 (PubMed:27268078). It mediates the Phoenixin-14 and
CC Phoenixin-20 augmentation of gonadotropin-releasing hormone (GNRH)
CC signaling in the hypothalamus and pituitary gland (PubMed:27268078). In
CC the ovary, it mediates the effects of Phoenixin-14 and Phoenixin-20
CC induced granulosa cell proliferation during follicular growth
CC (PubMed:30933929). {ECO:0000269|PubMed:27268078,
CC ECO:0000269|PubMed:30933929}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the ovary, specifically in granulosa
CC cells of follicles that have passed the primary stage and in oocytes
CC (at protein level) (PubMed:30933929). Expressed in preadipocytes
CC (PubMed:30251651). {ECO:0000269|PubMed:30251651,
CC ECO:0000269|PubMed:30933929}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AL731727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043021; AAH43021.1; -; mRNA.
DR EMBL; BC096520; AAH96520.1; -; mRNA.
DR CCDS; CCDS30475.1; -.
DR RefSeq; NP_001300677.1; NM_001313748.1.
DR RefSeq; NP_081819.2; NM_027543.4.
DR RefSeq; XP_006529044.1; XM_006528981.3.
DR RefSeq; XP_006529046.1; XM_006528983.3.
DR RefSeq; XP_011246173.1; XM_011247871.2.
DR AlphaFoldDB; Q6PI62; -.
DR SMR; Q6PI62; -.
DR STRING; 10090.ENSMUSP00000065533; -.
DR GlyGen; Q6PI62; 2 sites.
DR PhosphoSitePlus; Q6PI62; -.
DR PaxDb; Q6PI62; -.
DR PRIDE; Q6PI62; -.
DR Antibodypedia; 589; 223 antibodies from 26 providers.
DR DNASU; 70771; -.
DR Ensembl; ENSMUST00000070316; ENSMUSP00000065533; ENSMUSG00000056679.
DR GeneID; 70771; -.
DR KEGG; mmu:70771; -.
DR UCSC; uc009uqh.1; mouse.
DR CTD; 54328; -.
DR MGI; MGI:1918021; Gpr173.
DR VEuPathDB; HostDB:ENSMUSG00000056679; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00890000139436; -.
DR HOGENOM; CLU_055518_0_0_1; -.
DR InParanoid; Q6PI62; -.
DR OMA; ACTVPHR; -.
DR OrthoDB; 1311948at2759; -.
DR PhylomeDB; Q6PI62; -.
DR TreeFam; TF331163; -.
DR BioGRID-ORCS; 70771; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Gpr173; mouse.
DR PRO; PR:Q6PI62; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6PI62; protein.
DR Bgee; ENSMUSG00000056679; Expressed in lumbar dorsal root ganglion and 127 other tissues.
DR Genevisible; Q6PI62; MM.
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; IMP:MGI.
DR GO; GO:2001223; P:negative regulation of neuron migration; IMP:MGI.
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 1: Evidence at protein 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_0000069651"
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
