GP161_BOVIN
ID GP161_BOVIN Reviewed; 528 AA.
AC Q2YDN1; F1MSH4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=G protein-coupled receptor 161;
GN Name=GPR161;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key negative regulator of Shh signaling, which promotes the
CC processing of GLI3 into GLI3R during neural tube development. Recruited
CC by TULP3 and the IFT-A complex to primary cilia and acts as a regulator
CC of the PKA-dependent basal repression machinery in Shh signaling by
CC increasing cAMP levels, leading to promote the PKA-dependent processing
CC of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH,
CC it is removed from primary cilia and is internalized into recycling
CC endosomes, preventing its activity and allowing activation of the Shh
CC signaling. Its ligand is unknown (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 in a TULP3 and IFT-A complex-dependent manner. In
CC presence of SHH, it is removed from primary cilia and is internalized
CC into recycling endosomes and is apparently not degraded (By
CC similarity). {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; DAAA02006728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110145; AAI10146.1; -; mRNA.
DR RefSeq; NP_001070534.1; NM_001077066.1.
DR AlphaFoldDB; Q2YDN1; -.
DR SMR; Q2YDN1; -.
DR STRING; 9913.ENSBTAP00000000809; -.
DR PaxDb; Q2YDN1; -.
DR Ensembl; ENSBTAT00000000809; ENSBTAP00000000809; ENSBTAG00000000616.
DR GeneID; 768006; -.
DR KEGG; bta:768006; -.
DR CTD; 23432; -.
DR VEuPathDB; HostDB:ENSBTAG00000000616; -.
DR VGNC; VGNC:29566; GPR161.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000157829; -.
DR HOGENOM; CLU_038027_0_0_1; -.
DR InParanoid; Q2YDN1; -.
DR OMA; VQRHRTS; -.
DR OrthoDB; 1262707at2759; -.
DR TreeFam; TF331895; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000000616; Expressed in semen and 108 other tissues.
DR ExpressionAtlas; Q2YDN1; baseline.
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..528
FT /note="G protein-coupled receptor 161"
FT /id="PRO_0000379072"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 528 AA; 58349 MW; 0F22F2321977873C CRC64;
MSLNSSLGHR KELSNLTEGA SDQGGSGVTE FVAIVIITVF VCLGNLVIVI TLYRKSYLLT
LSNKFVFSLT LSNFLLSVLV LPFVVTSSIR REWIFGVVWC NFSALLYLLI SSASMLTLGI
IAVDRYYAVL YPMAYPMKIT GNRAVMVLAY IWLHSLIGCL PPLFGWSSVE FDEFKWMCVA
AWHREPGYTA FWQIWCALLP FLVMLVCYGF IFRVARVKAR KVHCGAVVTV EVGVQRTGRK
NSSTSTSSSG SRKSAFQGVV YSANQCKALV TILVVIGAFM VTWGPYMVVI TSEALWGKNC
VSPTLETWAT WLSFTSAICH PLIYGLWNKT VRKELLGMCF GDRYYREPFV QRQRTSRLFS
ISNRITDLGL SPHLTALMAG EQPLGNSSST GDTGFSCSQD SGTDVMLLED YTSDDNPLHG
TCPPKRRSSV TFEDEVEQIK EAAKNPILHV KADVHKSLDS YATSLAKAIE AEAKINLFGE
EALPGVLLTA RTVPGIGFGS RRGSRTLAGQ RLQLQSIEEG DVLATEQR
