ID GP157_HUMAN Reviewed; 335 AA. AC Q5UAW9; A2A334; Q8WWB8; Q9HA73; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 2. DT 24-JAN-2024, entry version 150. DE RecName: Full=G-protein coupled receptor 157; GN Name=GPR157; 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=Placenta, and Prostate; RA Bonner T.I., Kauffman D., Nagle J.W.; RT "Complete coding sequence of GPR157."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-127. RC TISSUE=Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). CC -!- FUNCTION: Orphan receptor that promotes neuronal differentiation of CC radial glial progenitors (RGPs). The activity of this receptor is CC mediated by a G(q)-protein that activates a phosphatidylinositol- CC calcium second messenger. {ECO:0000250|UniProtKB:Q8C206}. CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane CC {ECO:0000250|UniProtKB:Q8C206}; Multi-pass membrane protein CC {ECO:0000255}. Note=Expressed in the primary cilia of radial glial CC progenitors (RGPs) exposed to the cerebrospinal fluid. CC {ECO:0000250|UniProtKB:Q8C206}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB13982.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY768808; AAV35060.1; -; mRNA. DR EMBL; AL158048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK022194; BAB13982.1; ALT_SEQ; mRNA. DR CCDS; CCDS100.2; -. DR RefSeq; NP_079256.4; NM_024980.4. DR AlphaFoldDB; Q5UAW9; -. DR SMR; Q5UAW9; -. DR BioGRID; 123089; 1. DR STRING; 9606.ENSP00000366628; -. DR ChEMBL; CHEMBL4523875; -. DR iPTMnet; Q5UAW9; -. DR PhosphoSitePlus; Q5UAW9; -. DR BioMuta; GPR157; -. DR DMDM; 73621015; -. DR EPD; Q5UAW9; -. DR jPOST; Q5UAW9; -. DR MassIVE; Q5UAW9; -. DR MaxQB; Q5UAW9; -. DR PaxDb; 9606-ENSP00000366628; -. DR PeptideAtlas; Q5UAW9; -. DR ProteomicsDB; 65242; -. DR Antibodypedia; 27668; 155 antibodies from 23 providers. DR DNASU; 80045; -. DR Ensembl; ENST00000377411.5; ENSP00000366628.4; ENSG00000180758.12. DR GeneID; 80045; -. DR KEGG; hsa:80045; -. DR MANE-Select; ENST00000377411.5; ENSP00000366628.4; NM_024980.5; NP_079256.4. DR UCSC; uc001apq.2; human. DR AGR; HGNC:23687; -. DR CTD; 80045; -. DR DisGeNET; 80045; -. DR GeneCards; GPR157; -. DR HGNC; HGNC:23687; GPR157. DR HPA; ENSG00000180758; Tissue enhanced (skeletal). DR neXtProt; NX_Q5UAW9; -. DR OpenTargets; ENSG00000180758; -. DR PharmGKB; PA134876230; -. DR VEuPathDB; HostDB:ENSG00000180758; -. DR eggNOG; ENOG502QU1X; Eukaryota. DR GeneTree; ENSGT00390000012992; -. DR HOGENOM; CLU_052670_0_0_1; -. DR InParanoid; Q5UAW9; -. DR OMA; CIMFVLF; -. DR OrthoDB; 2952177at2759; -. DR PhylomeDB; Q5UAW9; -. DR TreeFam; TF330856; -. DR PathwayCommons; Q5UAW9; -. DR BioGRID-ORCS; 80045; 8 hits in 1139 CRISPR screens. DR ChiTaRS; GPR157; human. DR GeneWiki; GPR157; -. DR GenomeRNAi; 80045; -. DR Pharos; Q5UAW9; Tdark. DR PRO; PR:Q5UAW9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5UAW9; Protein. DR Bgee; ENSG00000180758; Expressed in esophagus squamous epithelium and 138 other cell types or tissues. DR ExpressionAtlas; Q5UAW9; baseline and differential. DR GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro. DR GO; GO:0048512; P:circadian behavior; IEA:Ensembl. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0060019; P:radial glial cell differentiation; ISS:UniProtKB. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR022343; GCR1-cAMP_receptor. DR InterPro; IPR017981; GPCR_2-like_7TM. DR InterPro; IPR000832; GPCR_2_secretin-like. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR23112; G PROTEIN-COUPLED RECEPTOR 157-RELATED; 1. DR PANTHER; PTHR23112:SF0; G-PROTEIN COUPLED RECEPTOR 157; 1. DR Pfam; PF00002; 7tm_2; 1. DR PRINTS; PR02001; GCR1CAMPR. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. DR Genevisible; Q5UAW9; HS. PE 2: Evidence at transcript level; KW Cell membrane; Cell projection; Developmental protein; Differentiation; KW G-protein coupled receptor; Membrane; Receptor; Reference proteome; KW Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1..335 FT /note="G-protein coupled receptor 157" FT /id="PRO_0000070339" FT TOPO_DOM 1..15 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 16..36 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 37..48 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 49..69 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 70..87 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 88..108 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 109..119 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 120..140 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 141..166 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 167..187 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 188..226 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 227..247 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 248..258 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 259..279 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 280..335 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 300..335 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 319..335 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 71 FT /note="N -> D (in Ref. 3; BAB13982)" FT /evidence="ECO:0000305" SQ SEQUENCE 335 AA; 36623 MW; C779B2D16C6D560C CRC64; MQPSPPPTEL VPSERAVVLL SCALSALGSG LLVATHALWP DLRSRARRLL LFLSLADLLS AASYFYGVLQ NFAGPSWDCV LQGALSTFAN TSSFFWTVAI ALYLYLSIVR AARGPRTDRL LWAFHVVSWG VPLVITVAAV ALKKIGYDAS DVSVGWCWID LEAKDHVLWM LLTGKLWEML AYVLLPLLYL LVRKHINRAH TALSEYRPIL SQEHRLLRHS SMADKKLVLI PLIFIGLRVW STVRFVLTLC GSPAVQTPVL VVLHGIGNTF QGGANCIMFV LCTRAVRTRL FSLCCCCCSS QPPTKSPAGT PKAPAPSKPG ESQESQGTPG ELPST //