AGRA3_DANRE
ID AGRA3_DANRE Reviewed; 1346 AA.
AC S4X0Q8;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Adhesion G protein-coupled receptor A3;
DE AltName: Full=G-protein coupled receptor 125;
DE Flags: Precursor;
GN Name=adgra3; Synonyms=gpr125;
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 {ECO:0000312|EMBL:AGP05313.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION
RP PHENOTYPE, INTERACTION WITH DISHEVELLED, AND SUBCELLULAR LOCATION.
RX PubMed=23821037; DOI=10.1242/dev.094839;
RA Li X., Roszko I., Sepich D.S., Ni M., Hamm H.E., Marlow F.L.,
RA Solnica-Krezel L.;
RT "Gpr125 modulates Dishevelled distribution and planar cell polarity
RT signaling.";
RL Development 140:3028-3039(2013).
RN [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=25715737; DOI=10.1186/s12864-015-1296-8;
RA Harty B.L., Krishnan A., Sanchez N.E., Schioeth H.B., Monk K.R.;
RT "Defining the gene repertoire and spatiotemporal expression profiles of
RT adhesion G protein-coupled receptors in zebrafish.";
RL BMC Genomics 16:62-62(2015).
RN [3]
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).
CC -!- FUNCTION: Orphan receptor that acts as a critical modulator of planar
CC cell polarity during gastrulation. Controls the localization of
CC dishevelled. {ECO:0000269|PubMed:23821037}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with disheveled proteins;
CC leading to the localization of dishevelled proteins to specific
CC membrane subdomains. {ECO:0000269|PubMed:23821037}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23821037};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at very low levels.
CC {ECO:0000269|PubMed:25715737}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during early development and then
CC ubiquitously expressed at very low levels at later larval stages.
CC {ECO:0000269|PubMed:23821037, ECO:0000269|PubMed:25715737}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein exacerbated
CC the convergence/ extension (C/E) phenotypes of other planar cell
CC polarity (PCP) family member mutants (vangl2, scribbled).
CC {ECO:0000269|PubMed:23821037}.
CC -!- MISCELLANEOUS: Most adhesion GPCRs proteins undergo autoproteolysis at
CC the GPS domain. ADGRA3 is predicted non-cleavable because of the lack
CC of a consensus catalytic triad sequence within GPS domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR EMBL; KC996731; AGP05313.1; -; mRNA.
DR EMBL; CABZ01086759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01086760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01086761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01086762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01086763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01086764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01086765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01086766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01086767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001289153.1; NM_001302224.1.
DR AlphaFoldDB; S4X0Q8; -.
DR SMR; S4X0Q8; -.
DR STRING; 7955.ENSDARP00000109414; -.
DR PaxDb; S4X0Q8; -.
DR PRIDE; S4X0Q8; -.
DR GeneID; 100003592; -.
DR KEGG; dre:100003592; -.
DR CTD; 166647; -.
DR ZFIN; ZDB-GENE-131003-2; adgra3.
DR eggNOG; KOG0619; Eukaryota.
DR OrthoDB; 31536at2759; -.
DR PRO; PR:S4X0Q8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IGI:ZFIN.
DR GO; GO:0097475; P:motor neuron migration; IGI:ZFIN.
DR GO; GO:0003402; P:planar cell polarity pathway involved in axis elongation; IDA:ZFIN.
DR GO; GO:2000095; P:regulation of Wnt signaling pathway, planar cell polarity pathway; IMP:ZFIN.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond;
KW G-protein coupled receptor; Immunoglobulin domain; Leucine-rich repeat;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1346
FT /note="Adhesion G protein-coupled receptor A3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433465"
FT TOPO_DOM 22..739
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 740..760
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 761..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 774..794
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..804
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 805..825
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 826..854
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 855..875
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 876..897
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 898..918
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 919..977
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 978..998
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 999..1005
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1006..1026
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1027..1346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 66..90
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 91..114
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 116..138
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 139..162
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 176..223
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT DOMAIN 229..327
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REPEAT 503..529
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 574..600
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 611..632
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT DOMAIN 676..727
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 18..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1344..1346
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1235..1257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 251..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1346 AA; 148655 MW; D8832F23778CA437 CRC64;
MSVLCVLLLA FVLPLRGSSS AGSTECKTYD ERSRSAGKSS PSGATLDRKV VCSNMEFRQV
PSPDTFPNRT VSLILSNNKI QELLNGSFVG LSSLERLDIK NNIITHIEPG AFYGLFSLKR
LDLSKNLIGC LHVDVFKGLT NLVKLNLSEN KFSSLSQGIF DSLGSLKILE FDSPYLLCDC
NLQWLVVWIK EKAIGVKETR CSFPRSLQGQ LITTLRAETL TCDAPLELPS FQMTPSQHQI
VFQGDSLPFQ CMASFVDEDM QVLWYQDGKM VEPDATQGIY IEKSMVQNCS LIASALTISN
IQPGFTGNWE CRVRTSRGNN TRTVHIVVLE SSAKYCLPDR VSNNKGEYRW PRTLAGITAY
LPCKRQVTGA GIYSGSSAED RRAWRRCDRG GQWAEDDYSR CEYMKDVTRV LYIINQMPLN
LTNVVQTAQQ LLAYTAEAPN FSDKVDVIFV AEMIEKIGKF AEKYKELGDV MVDISSNLLL
ADERVLWMAQ REARACSRMV ESLQRIALLR VSNGALAYST NSPNIALEAH AIKASSFNGM
TCTLFQKLSP ERTVMAHHGE ISPERQLSFK CNVTSNLSAL ALKNTIVEAS LQLPPTLFSS
LGSSGQAEEA VYKLHLLAFR NGKLFPPTGN SSILSDGSKR RSVVTPVMIT KIEGFPLRDL
LSPVNVTLRR FLQGSDAVPA FWNFSLQGGQ GGWQSDGCRI LHQDDNFTTV SCHSLNSYAV
LMDLNRTGYN VFIFRPLHPV IYSTALVLVL CLLSVIVSYI YHHKSVRISK KCWHMLVNLC
LHILLTCAVF VGGINQTYNA SVCQAMGIVL HYSTLATALW SGVTARNIYK QVTRKAKRYE
ELDEPPPPPR PMLRFYLIGG GIPIIVCGIT AAANIKNYGS QVNAPYCWMA WEPSLGAFYG
PAAFIVFVDC MYFLSILIQL RRHPERRFEL KEQSEEQQHL SVTEATEITP VHLESSPTAQ
PVPMSALENE HTFVSQLMGV AGSLTLYAAL WVFGALAISQ EHPADLVFAC LFGALALGLG
AFLVAHHCVN RQDMRRHWSQ ACCLIRRNYA VQVDSLLLPI AGSSGSVMTS RGNGEATKCP
ASSAESSCTN KSAPSLRNST QGCKLTNLQV EAAQCKVVAP STANGTAVLD NSLTEHSVDN
EIKMHVAPIE IQYRPSSVNN NNLPGNANIT GHPGRHHKNR SRAHRASRLT VLREYSYDVP
TSVEGSVQSV PNKRHHHESL HARNSRRAAY LAYRERQQSQ LQQDSSDAAS TSVPRRSRHF
SKGTRIGNGF GHGISNGGLL DGSEADVTNQ TKECPKQTLT VELEVQPKSY GLNLACQNGS
AKDSERLNVE SSGNVKTGLW KHETTV
