LGR6_DANRE
ID LGR6_DANRE Reviewed; 962 AA.
AC P0DM44;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Leucine-rich repeat-containing G-protein coupled receptor 6;
DE Flags: Precursor;
GN Name=lgr6;
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 DEVELOPMENTAL STAGE.
RX PubMed=21570488; DOI=10.1016/j.gep.2011.04.002;
RA Hirose K., Shimoda N., Kikuchi Y.;
RT "Expression patterns of lgr4 and lgr6 during zebrafish development.";
RL Gene Expr. Patterns 11:378-383(2011).
CC -!- FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt
CC signaling pathway. Upon binding to R-spondins (rspo1, rspo2, rspo3 or
CC rspo4), associates with phosphorylated lrp6 and frizzled receptors that
CC are activated by extracellular Wnt receptors, triggering the canonical
CC Wnt signaling pathway to increase expression of target genes. In
CC contrast to classical G-protein coupled receptors, does not activate
CC heterotrimeric G-proteins to transduce the signal (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the notochord, Kupffer's vesicle, the
CC most anterior region of diencephalon, otic vesicles, and the anterior
CC and posterior lateral line primordia by 24 hours post-fertilization
CC (hpf). From 48 to 72 hpf, expression is confined to the anterior and
CC posterior neuromasts, otic vesicles, pharyngeal arches, pectoral fin
CC buds, and cranial cartilages such as Meckel's cartilages, ceratohyals
CC and trabeculae. {ECO:0000269|PubMed:21570488}.
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; CABZ01030037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01030038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01030039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01030040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01030041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01030042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DM44; -.
DR SMR; P0DM44; -.
DR OrthoDB; 340670at2759; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0016500; F:protein-hormone receptor activity; IEA:InterPro.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002131; Gphrmn_rcpt_fam.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 5.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS51450; LRR; 15.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Leucine-rich repeat; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..962
FT /note="Leucine-rich repeat-containing G-protein coupled
FT receptor 6"
FT /id="PRO_0000422821"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 766..786
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 20..60
FT /note="LRRNT"
FT REPEAT 38..58
FT /note="LRR 1"
FT REPEAT 59..82
FT /note="LRR 2"
FT REPEAT 83..106
FT /note="LRR 3"
FT REPEAT 107..131
FT /note="LRR 4"
FT REPEAT 133..154
FT /note="LRR 5"
FT REPEAT 155..178
FT /note="LRR 6"
FT REPEAT 179..202
FT /note="LRR 7"
FT REPEAT 203..226
FT /note="LRR 8"
FT REPEAT 228..250
FT /note="LRR 9"
FT REPEAT 251..273
FT /note="LRR 10"
FT REPEAT 275..297
FT /note="LRR 11"
FT REPEAT 298..321
FT /note="LRR 12"
FT REPEAT 322..344
FT /note="LRR 13"
FT REPEAT 345..368
FT /note="LRR 14"
FT REPEAT 370..390
FT /note="LRR 15"
FT REPEAT 391..414
FT /note="LRR 16"
FT REPEAT 416..438
FT /note="LRR 17"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 633..708
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 962 AA; 105933 MW; 8A400E0C22130CA9 CRC64;
MLVVLLILHA VSCAHSHGSP GAAVPVKQCP SACQCEEDGI LLLVDCSEQG LSSVPTDLSP
LTSYLDLSMN NISEIQPNAF RNLHFLSELR LSGNHLRHIP GPMLQGLYNL KVLMLQNNQL
ERLPSEDPWE LPNLLSLRLD ANLIMEVPAR TLSGMRSLRH LWLDDNALTE IPVSALNDLS
SLQAMTLALN RITLIPDYAF RNLSNLVVLH LHNNMIRTLG QNCFEGLHSL ETLELNFNDL
QEFPVAIRTL AKLQELGFHN NNIKAIPERA FVGNPLLQTI HFYENPIQFV GRSAFQFLPK
LHTLSLNGAT EIREFPDLKG TTSLQVLTLT RAGLTSLPYD LCHLLPKLKV LELSHNVIEE
LPSFYHCTSL QEIGLQHNLI KQIEMNTFQQ LGSLRSLDLS WNSINSIHPD AFFSLQSLIK
LDLTGNRLSN LPMTGLTSLT HLKLKGNMAL SRSFGLEDFP NIRVIEMPYA YQCCVFGGCS
SYRSASQWEE QMGSEEEDFQ KKSPSLFPIH TDNNYDLDLE EFQLAIEESK LQTSIQCTPI
PGPFKPCDNL FDSWVVRLGM WLISLVSLMG NSLLILTVFT SPSYLSPVKF IIGTISGANL
LTGLCTGTLA LVDARTFGEF ALHGAQWEMG AGCRAVGFLS VLASEGSILF LTLAAVQCSV
SVSCARAYGK SPSLGSVRAA AVACLALSLA VAALPLIGVG EYGATPLCMP SPLPDGEPST
LGFMVALIMM NSLCFLVITG TYIKLYWDLM KGDFDSIWDC AMIKHVAWLI FTNCLLYCPV
AFLTFSSLLS LFPVSEEVVK SVVLVLLPLP ASINPLLYLL FNPHFREDMR LLLSRAHLNH
DRNLDSFVSV DTEKSSYDST QALVSFATEA DGVFESLSVP NPETVARFTC PPSVALIPCQ
MQMKPSTDRE NTGENLIRSA PGLIAKEQEH IRSSGVDTQN GTSIFSGAYH STGPSAHSQV
FT
