ID   GP173_HUMAN             Reviewed;         373 AA.
AC   Q9NS66; B1B0A5;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 158.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [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 (By similarity). It mediates the Phoenixin-14 and
CC       Phoenixin-20 augmentation of gonadotropin-releasing hormone (GNRH)
CC       signaling in the hypothalamus and pituitary gland (By similarity). 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:0000250|UniProtKB:Q9JJH2,
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 at high levels in
CC       brain. Lower levels in small intestine. In brain regions, detected in
CC       all regions tested. Highest levels in the cerebellum and cerebral
CC       cortex. {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; AB040801; BAA96647.1; -; mRNA.
DR   EMBL; BX322635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471154; EAW93142.1; -; Genomic_DNA.
DR   EMBL; BC009861; AAH09861.1; -; mRNA.
DR   CCDS; CCDS14349.1; -.
DR   PIR; JC7289; JC7289.
DR   RefSeq; NP_061842.1; NM_018969.5.
DR   RefSeq; XP_011529100.1; XM_011530798.2.
DR   AlphaFoldDB; Q9NS66; -.
DR   SMR; Q9NS66; -.
DR   BioGRID; 119931; 57.
DR   IntAct; Q9NS66; 1.
DR   STRING; 9606.ENSP00000331600; -.
DR   ChEMBL; CHEMBL4523922; -.
DR   GlyCosmos; Q9NS66; 2 sites, No reported glycans.
DR   GlyGen; Q9NS66; 2 sites.
DR   iPTMnet; Q9NS66; -.
DR   PhosphoSitePlus; Q9NS66; -.
DR   BioMuta; GPR173; -.
DR   DMDM; 15214315; -.
DR   PaxDb; 9606-ENSP00000331600; -.
DR   PeptideAtlas; Q9NS66; -.
DR   ProteomicsDB; 82496; -.
DR   Antibodypedia; 589; 236 antibodies from 26 providers.
DR   DNASU; 54328; -.
DR   Ensembl; ENST00000332582.5; ENSP00000331600.5; ENSG00000184194.6.
DR   GeneID; 54328; -.
DR   KEGG; hsa:54328; -.
DR   MANE-Select; ENST00000332582.5; ENSP00000331600.5; NM_018969.6; NP_061842.1.
DR   UCSC; uc004dru.4; human.
DR   AGR; HGNC:18186; -.
DR   CTD; 54328; -.
DR   GeneCards; GPR173; -.
DR   HGNC; HGNC:18186; GPR173.
DR   HPA; ENSG00000184194; Tissue enhanced (brain, pituitary gland).
DR   MIM; 300253; gene.
DR   neXtProt; NX_Q9NS66; -.
DR   OpenTargets; ENSG00000184194; -.
DR   PharmGKB; PA134896710; -.
DR   VEuPathDB; HostDB:ENSG00000184194; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00890000139436; -.
DR   HOGENOM; CLU_055518_0_0_1; -.
DR   InParanoid; Q9NS66; -.
DR   OMA; HIPCWRT; -.
DR   OrthoDB; 2962814at2759; -.
DR   PhylomeDB; Q9NS66; -.
DR   TreeFam; TF331163; -.
DR   PathwayCommons; Q9NS66; -.
DR   SignaLink; Q9NS66; -.
DR   BioGRID-ORCS; 54328; 12 hits in 760 CRISPR screens.
DR   ChiTaRS; GPR173; human.
DR   GeneWiki; GPR173; -.
DR   GenomeRNAi; 54328; -.
DR   Pharos; Q9NS66; Tbio.
DR   PRO; PR:Q9NS66; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9NS66; Protein.
DR   Bgee; ENSG00000184194; Expressed in cortical plate and 106 other cell types or tissues.
DR   ExpressionAtlas; Q9NS66; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0004968; F:gonadotropin-releasing hormone receptor activity; IBA:GO_Central.
DR   GO; GO:2001223; P:negative regulation of neuron migration; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd15217; 7tmA_SREB3_GPR173; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR19268; G PROTEIN-COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR19268:SF4; G-PROTEIN COUPLED RECEPTOR 173-RELATED; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q9NS66; HS.
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_0000069650"
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;  41481 MW;  8A227F914C9D8358 CRC64;
     MANTTGEPEE VSGALSPPSA SAYVKLVLLG LIMCVSLAGN AILSLLVLKE RALHKAPYYF
     LLDLCLADGI RSAVCFPFVL 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
//