GPR22_DANRE
ID GPR22_DANRE Reviewed; 460 AA.
AC A0A2R9YJI3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=G-protein coupled receptor 22;
GN Name=gpr22a;
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 [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 [2]
RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=25335082; DOI=10.1371/journal.pone.0110484;
RA Verleyen D., Luyten F.P., Tylzanowski P.;
RT "Orphan G-protein coupled receptor 22 (Gpr22) regulates cilia length and
RT structure in the zebrafish Kupffer's vesicle.";
RL PLoS ONE 9:E110484-E110484(2014).
CC -!- FUNCTION: Orphan G-protein coupled receptor that regulates cilia length
CC and structure in the Kupffer's vesicle leading to the left-right
CC asymmetry development by establishing a directional fluid flow.
CC {ECO:0000269|PubMed:25335082}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D4A3U0};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously during early stages of
CC development. From bud stage onwards, the expression pattern becomes
CC restricted to the axial structures and the developing Kupffer's
CC vesicle. {ECO:0000269|PubMed:25335082}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein leads to
CC defective left-right (LR) axis formation in the embryo. Cilia number
CC and length are reduced in the Kupffer's vesicle (KV). Morpholino
CC knockdown of the protein in Kupffer's vesicle alone is still able to
CC generate the phenotype, indicating that Gpr22 regulates LR asymmetry
CC through the KV. {ECO:0000269|PubMed:25335082}.
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; BX072538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005164527.1; XM_005164470.3.
DR AlphaFoldDB; A0A2R9YJI3; -.
DR SMR; A0A2R9YJI3; -.
DR STRING; 7955.ENSDARP00000107735; -.
DR Ensembl; ENSDART00000128807; ENSDARP00000107735; ENSDARG00000004592.
DR GeneID; 504167; -.
DR CTD; 504167; -.
DR ZFIN; ZDB-GENE-041210-48; gpr22a.
DR GeneTree; ENSGT01050000244841; -.
DR OMA; ICIFTIP; -.
DR PRO; PR:A0A2R9YJI3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000004592; Expressed in heart and 31 other tissues.
DR ExpressionAtlas; A0A2R9YJI3; baseline.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IMP:ZFIN.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:ZFIN.
DR GO; GO:0003140; P:determination of left/right asymmetry in lateral mesoderm; IMP:ZFIN.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR GO; GO:0071910; P:determination of liver left/right asymmetry; IMP:ZFIN.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0070121; P:Kupffer's vesicle development; IMP:ZFIN.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cilium biogenesis/degradation; G-protein coupled receptor;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..460
FT /note="G-protein coupled receptor 22"
FT /id="PRO_0000445302"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..95
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..114
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 115..135
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..185
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 186..206
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 236..256
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..343
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 344..364
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 378..398
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..460
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 276..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 51763 MW; 64613D532E86444C CRC64;
MESMPSSLTH QRFGLLNKHL TRTGNTREGR MHTPPVLGFQ AIMSNVTVLD NIEPLDFEMD
LKTPYPVSFQ VSLTGFLMLE IVLGLSSNLT VLALYCMKSN LVSSVSNIVT MNLHVLDVLV
CVGCIPLTIV VVLLPLEGNN ALICCFHEAC VSFASVATAA NVLAITLDRY DISVRPANRV
LTMGRAVALL GSIWALSFFS FLVPFIEEGF FSQAGNERNQ TEAEEPSNEY YTELGLYYHL
LAQIPIFFFT AVVMLVTYYK ILQALNIRIG TRFHSVPKKK PRKKKTISMT STQPESTDAS
QSSAGRNAPL GMRTSVSVII ALRRAVKRHR ERRERQKRVF RMSLLIISTF LLCWTPITVL
NTVILSVGPS NFTVRLRLGF LVMAYGTTIF HPLLYAFTRQ KFQKVLKSKM KKRVVSVVEA
DPMPNNVVIH NSWIDPKRNK KVTFEETEVR QKCLSSEDVE
