GP161_DANRE
ID GP161_DANRE Reviewed; 526 AA.
AC Q90X46; A4IGB3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=G-protein coupled receptor 161;
GN Name=gpr161; ORFNames=si:rp71-20i5.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18755178; DOI=10.1016/j.ydbio.2008.08.001;
RA Leung T., Humbert J.E., Stauffer A.M., Giger K.E., Chen H., Tsai H.-J.,
RA Wang C., Mirshahi T., Robishaw J.D.;
RT "The orphan G protein-coupled receptor 161 is required for left-right
RT patterning.";
RL Dev. Biol. 323:31-40(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) 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). Required in left/right
CC patterning by modulating Ca(2+) levels in the cells surrounding the
CC Kupffer vesicle. {ECO:0000250, ECO:0000269|PubMed:18755178}.
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 -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development. At
CC 9- to 16-somites, transcripts are broadly expressed with specific
CC staining observed in the developing nervous system, somites, and
CC precardiac mesoderm. At later stages 1- to 3-days post-fertilization,
CC transcripts become more localized within the dorsal diencephalon, the
CC otic vesicles, and the fin buds.
CC -!- DISRUPTION PHENOTYPE: Embryos exhibit perturb cardiac looping as the
CC result of a defect in left/right patterning.
CC {ECO:0000269|PubMed:18755178}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; EU090912; ABW77593.1; -; mRNA.
DR EMBL; AL590146; CAC94897.2; -; Genomic_DNA.
DR EMBL; BC135011; AAI35012.1; -; mRNA.
DR RefSeq; NP_001007200.2; NM_001007199.2.
DR AlphaFoldDB; Q90X46; -.
DR SMR; Q90X46; -.
DR STRING; 7955.ENSDARP00000072514; -.
DR PaxDb; Q90X46; -.
DR PRIDE; Q90X46; -.
DR Ensembl; ENSDART00000078051; ENSDARP00000072514; ENSDARG00000055659.
DR Ensembl; ENSDART00000143991; ENSDARP00000118097; ENSDARG00000055659.
DR GeneID; 368421; -.
DR KEGG; dre:368421; -.
DR CTD; 368421; -.
DR ZFIN; ZDB-GENE-030616-58; gpr161a.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000157829; -.
DR HOGENOM; CLU_038027_0_0_1; -.
DR InParanoid; Q90X46; -.
DR OMA; VQRHRTS; -.
DR OrthoDB; 1262707at2759; -.
DR PhylomeDB; Q90X46; -.
DR TreeFam; TF331895; -.
DR Reactome; R-DRE-5610787; Hedgehog 'off' state.
DR Reactome; R-DRE-5632684; Hedgehog 'on' state.
DR PRO; PR:Q90X46; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000055659; Expressed in habenula and 30 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:0007368; P:determination of left/right symmetry; IMP:ZFIN.
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 GO; GO:0051924; P:regulation of calcium ion transport; IMP:ZFIN.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
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..526
FT /note="G-protein coupled receptor 161"
FT /id="PRO_0000379074"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..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..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 231..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..526
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 84
FT /note="S -> T (in Ref. 3; AAI35012)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="E -> EE (in Ref. 3; AAI35012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 58485 MW; CACE795D638B5B3E CRC64;
MNGSKNGTAV ANSTNGLDDN GLMVLESVSI IIIAILACLG NLVIVVTLYK KPYLLTPSNK
FVFSLTSSNL LLSVLMLPFV VASSVRRDWM FGVVWCNFTA LLHLLVSSSS MLTLGAIAID
RYYAVLYPMI YPMKITGNRA VLAIVYIWLH SLVGCLPPLF GWSSFEFDRF KWTCTVSWHK
EISYTAFWVT WCCLLPLVAM LVCYGVIFRV ARIKARKVYC GSVVVSQEES SSQNNGRKNS
NTSTSSSGSR KSLIYSGSQC KAFITILVVL GTFLTTWGPY VVVISTEALL GKNSVSPQVE
TLVSWLSFTS AVCHPLIYGL WNKTVRKELL GMCFDDRYYR ESFVIRHRTS RLFSISNRIT
DLGMSPHLTA MLVGGGQLLG RGSSTGDTGF SYTQDSATDV MLLESYTSEA SHSAHCTANK
RRSSVTFEDQ VDHIPQGDPS VVQVTADIHK SLDSFASSLA KAIENDAKLQ LLGEWTQIPT
SLFTVRNTQR VPRYLDGQRL RMESIDEGIV KDDDDDEEEM EREEKM
