LGR5_RAT
ID LGR5_RAT Reviewed; 907 AA.
AC D4AC13;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Leucine-rich repeat-containing G-protein coupled receptor 5;
DE Flags: Precursor;
GN Name=Lgr5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt
CC signaling pathway and acts as a stem cell marker of the intestinal
CC epithelium and the hair follicle. Upon binding to R-spondins (RSPO1,
CC RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and
CC frizzled receptors that are activated by extracellular Wnt receptors,
CC triggering the canonical Wnt signaling pathway to increase expression
CC of target genes. In contrast to classical G-protein coupled receptors,
CC does not activate heterotrimeric G-proteins to transduce the signal.
CC Involved in the development and/or maintenance of the adult intestinal
CC stem cells during postembryonic development (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Identified in a complex composed of RNF43, LGR5 and RSPO1 (By
CC similarity). Also interacts with other R-spondin ligands, including
CC RSPO2, RSPO3 and RSPO4 (By similarity). {ECO:0000250|UniProtKB:O75473}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Rapidly
CC and constitutively internalized to the trans-Golgi network at steady
CC state. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AABR06049740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06049741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06049742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06049743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06049744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473960; EDM16685.1; -; Genomic_DNA.
DR RefSeq; NP_001100254.1; NM_001106784.1.
DR AlphaFoldDB; D4AC13; -.
DR SMR; D4AC13; -.
DR STRING; 10116.ENSRNOP00000005814; -.
DR GlyGen; D4AC13; 3 sites.
DR PhosphoSitePlus; D4AC13; -.
DR PaxDb; D4AC13; -.
DR Ensembl; ENSRNOT00000005814; ENSRNOP00000005814; ENSRNOG00000004221.
DR GeneID; 299802; -.
DR KEGG; rno:299802; -.
DR UCSC; RGD:1307733; rat.
DR CTD; 8549; -.
DR RGD; 1307733; Lgr5.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000160214; -.
DR HOGENOM; CLU_006843_0_0_1; -.
DR InParanoid; D4AC13; -.
DR OMA; LHHNEIY; -.
DR OrthoDB; 340670at2759; -.
DR PhylomeDB; D4AC13; -.
DR TreeFam; TF316814; -.
DR Reactome; R-RNO-4641263; Regulation of FZD by ubiquitination.
DR PRO; PR:D4AC13; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000004221; Expressed in cerebellum and 11 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0016500; F:protein-hormone receptor activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:UniProtKB.
DR GO; GO:2001013; P:epithelial cell proliferation involved in renal tubule morphogenesis; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0001942; P:hair follicle development; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0009994; P:oocyte differentiation; ISO:RGD.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
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; PF00001; 7tm_1; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01462; LRRNT; 1.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Golgi apparatus; Leucine-rich repeat; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..907
FT /note="Leucine-rich repeat-containing G-protein coupled
FT receptor 5"
FT /id="PRO_0000422818"
FT TOPO_DOM 22..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..638
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 704..723
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745..775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 776..796
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 797..802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..64
FT /note="LRRNT"
FT REPEAT 44..64
FT /note="LRR 1"
FT REPEAT 65..88
FT /note="LRR 2"
FT REPEAT 89..112
FT /note="LRR 3"
FT REPEAT 114..136
FT /note="LRR 4"
FT REPEAT 137..160
FT /note="LRR 5"
FT REPEAT 162..184
FT /note="LRR 6"
FT REPEAT 186..208
FT /note="LRR 7"
FT REPEAT 209..232
FT /note="LRR 8"
FT REPEAT 233..256
FT /note="LRR 9"
FT REPEAT 257..279
FT /note="LRR 10"
FT REPEAT 281..303
FT /note="LRR 11"
FT REPEAT 304..327
FT /note="LRR 12"
FT REPEAT 328..350
FT /note="LRR 13"
FT REPEAT 351..375
FT /note="LRR 14"
FT REPEAT 377..396
FT /note="LRR 15"
FT REPEAT 397..420
FT /note="LRR 16"
FT REPEAT 422..444
FT /note="LRR 17"
FT REPEAT 564..585
FT /note="LRR 18"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 38..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 348..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 479..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 637..712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 907 AA; 99958 MW; FE853BED1075E793 CRC64;
MDTSRVRMLL SLLALLQLVA AGSPPRPDTM PRGCPSYCHC ELDGRMLLRV DCSDLGLSEL
PSNLSVFTSY LDLSMNNISQ LPASLLHRLR FLEELRLAGN ALTHIPKGAF AGLHSLKVLM
LQNNQLRQVP EEALQNLRSL QSLRLDANHI SYVPPSCFSG LHSLRHLWLD DNALTDVPVQ
AFRSLSALQA MTLALNKIHH IADHAFGNLS SLVVLHLHNN RIHSLGKKCF DGLHSLETLD
LNYNNLDEFP TAIKTLSNLK ELGFHSNNIR SIPERAFVGN PSLITIHFYD NPIQFVGISA
FQHLPELRTL TLNGASQITE FPDLTGTATL ESLTLTGAKI SSLPQTVCDQ LPNLQVLDLS
YNLLEDLPSL SGCQKLQKID LRHNEIYEIK GGTFQQLFNL RSLNLARNKI AIIHPNAFST
LPSLIKLDLS SNLLSSFPVT GLHGLTHLKL TGNRALQSLI PSANFPELKI IEMPYAYQCC
AFGGCENVYK IPNQWNKDDS SSVDDLRKKD AGLFQVQDER DLEDFLLDFE EDLKVLHSVQ
CSPPPGPFKP CEHLFGSWLI RIGVWTTAVL ALSCNALVAF TVFRTPLYIS SIKLLIGVIA
VVDILMGVSS AILAVVDTFT FGSFAQHGAW WEGGIGCQIV GFLSIFASES SVFLLTLAAL
ERGFSVKCSS KFEMKAPLSS LKAIILLCVL LALTIATVPL LGGSEYNASP LCLPLPFGEP
STTGYMVALV LLNSLCFLIM TIAYTRLYCS LEKGELENLW DCSMVKHTAL LLFTNCILYC
PVAFLSFSSL LNLTFISPEV IKFILLVIVP LPACLNPLLY IVFNPHFKED MGSLGKQTRF
WTRAKHPSLL SINSDDVEKR SCDSTQALVS FTHASIAYDL PSDSGSSPAY PMTESCHLSS
VAFVPCL
