GP161_XENTR
ID GP161_XENTR Reviewed; 518 AA.
AC B3DM66;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=G-protein coupled receptor 161;
GN Name=gpr161;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key negative regulator of Shh signaling during neural tube
CC development. Recruited to primary cilia and acts as a regulator of the
CC PKA-dependent basal repression machinery in Shh signaling by increasing
CC cAMP levels, leading to promote the PKA-dependent processing of gli3
CC into gli3r and repress the Shh signaling. In presence of shh, it is
CC removed from primary cilia, preventing its activity and allowing
CC activation of the Shh signaling (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Note=Mainly localizes to
CC primary cilium and is removed from primary cilia in presence of shh.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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; BC167720; AAI67720.1; -; mRNA.
DR RefSeq; NP_001123848.1; NM_001130376.1.
DR AlphaFoldDB; B3DM66; -.
DR SMR; B3DM66; -.
DR STRING; 8364.ENSXETP00000005135; -.
DR PaxDb; B3DM66; -.
DR GeneID; 100170613; -.
DR KEGG; xtr:100170613; -.
DR CTD; 23432; -.
DR Xenbase; XB-GENE-1003408; gpr161.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; B3DM66; -.
DR OrthoDB; 1262707at2759; -.
DR Reactome; R-XTR-5610787; Hedgehog 'off' state.
DR Reactome; R-XTR-5632684; Hedgehog 'on' state.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000002410; Expressed in embryo and 16 other tissues.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cilium; Developmental protein;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..518
FT /note="G-protein coupled receptor 161"
FT /id="PRO_0000379075"
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..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 429..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 518 AA; 57516 MW; 4532A285E301EAB4 CRC64;
MNSSSDGANE GAGAAADNGP TKVAESIAII IIDILICLGN LVIVVTLYKK SYLLSLSNKF
VFSLTFSNLL LSMLVLPFVV VSSILREWIF GVVWCNFSAL LYMLISSASM LTLGIIAIDR
YYAVLYPMVY PMKITGNRAV LALVYVWLHS LIGCLPPLFG WSTLEFDHFK WMCVAAWHKE
AGYTAFWQVW CALLPFIVMM ICYGFIFRVA RIKARKIHCG TVIIVQEASQ KNGRKNSSTS
TSSSGSRKNG FSSIVYSANQ CKALITILVV IGAFVLTWGP YMIVISTEAL KGKNSVSPVL
ETLATWLSFT SAICHPLIYG LWNKTVRKEL LGMCFGNRYR DPFHQQHRTS RMFSISNRIT
DLGLSPHLTA LMARGTESEH QSTTTNTGFS CSNESGTDVM LLDDTSSDAT QLHRVIYSRR
KSSVTFEDEV EQKNDARTMP TQPTAPSESL ESYAFNLAKA IEMDAKISLF GEDVFPSNVQ
ALPGNSGINR NRINFIQKQR VQLQSIEEGN IETSKCDV
