LGR5A_XENLA
ID LGR5A_XENLA Reviewed; 902 AA.
AC E5DHB5;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Leucine-rich repeat-containing G-protein coupled receptor 5A;
DE Short=LGR5a;
DE Flags: Precursor;
GN Name=lgr5-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21042589; DOI=10.1371/journal.pone.0013605;
RA Sun G., Hasebe T., Fujimoto K., Lu R., Fu L., Matsuda H., Kajita M.,
RA Ishizuya-Oka A., Shi Y.B.;
RT "Spatio-temporal expression profile of stem cell-associated gene LGR5 in
RT the intestine during thyroid hormone-dependent metamorphosis in Xenopus
RT laevis.";
RL PLoS ONE 5:E13605-E13605(2010).
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 -!- 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 -!- TISSUE SPECIFICITY: Expressed in the developing epithelial stem cells
CC of the intestine. {ECO:0000269|PubMed:21042589}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the limb, tail and intestine by T3
CC during metamorphosis. {ECO:0000269|PubMed:21042589}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; GU296021; ADK66918.1; -; mRNA.
DR RefSeq; NP_001186152.1; NM_001199223.1.
DR AlphaFoldDB; E5DHB5; -.
DR SMR; E5DHB5; -.
DR GeneID; 100526795; -.
DR KEGG; xla:100526795; -.
DR CTD; 100526795; -.
DR Xenbase; XB-GENE-11536385; lgr5.L.
DR OrthoDB; 340670at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 100526795; Expressed in internal ear and 12 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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:0007186; P:G protein-coupled receptor signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
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; 5.
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; 14.
PE 2: Evidence at transcript level;
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..902
FT /note="Leucine-rich repeat-containing G-protein coupled
FT receptor 5A"
FT /id="PRO_0000422819"
FT TOPO_DOM 23..557
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..634
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..655
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 656..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 700..718
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 740..763
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 764..784
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 785..798
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 799..819
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 820..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..61
FT /note="LRRNT"
FT REPEAT 41..61
FT /note="LRR 1"
FT REPEAT 62..85
FT /note="LRR 2"
FT REPEAT 86..109
FT /note="LRR 3"
FT REPEAT 111..133
FT /note="LRR 4"
FT REPEAT 134..157
FT /note="LRR 5"
FT REPEAT 159..181
FT /note="LRR 6"
FT REPEAT 182..205
FT /note="LRR 7"
FT REPEAT 207..229
FT /note="LRR 8"
FT REPEAT 230..253
FT /note="LRR 9"
FT REPEAT 254..276
FT /note="LRR 10"
FT REPEAT 278..300
FT /note="LRR 11"
FT REPEAT 301..324
FT /note="LRR 12"
FT REPEAT 325..347
FT /note="LRR 13"
FT REPEAT 348..372
FT /note="LRR 14"
FT REPEAT 374..393
FT /note="LRR 15"
FT REPEAT 394..417
FT /note="LRR 16"
FT REPEAT 418..441
FT /note="LRR 17"
FT REPEAT 598..619
FT /note="LRR 18"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 36..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 345..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 476..537
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 633..708
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 902 AA; 99911 MW; 7868E52FF49DDA5A CRC64;
MDTSRTSLFL CSVLYSLQLV GSARPGKQHR SCPTPCECEQ DGMLVRVDCS DRGLTGLPRN
ISIFTSYLDL SMNNITKLPS NALHNLHFLE ELRLAGNDLT YIPKGAFAGL GSLKVLMLQN
NLLRQVPSEA LQNLRSLQSL RLDANHISYV PPSSFNGLFS LRHLWLDDNS LTEIPVRALE
SLSALQAMTL ALNKIHHIPD YAFGNLSSLV VLHLHNNRIY SLGKKCFDGL HSLETLDLNY
NNLDEFPAAI KTLKNLKELG FHSNNIKSIP EQAFIGNPSL ITTHFYDNPI QHVGRSAFQH
LPELRTLILN GASQITEFPD LTGTTSLESL TLTGAQLVYL PSAVCNQLPN LKVIDLSYNH
IKDLPSFSGC QRLQKIDLRH NEVYEIRFTT FQQLVGLRSL DLAWNKIAVI HPSSFSSLPS
LIKLDLSSNH LTSFPVTGLH GLTHLKLTGN SALQDLIPSE HFPKLRVMEM PYAYQCCAFA
VCENLKHSGQ MNKDENSSAD DFYRKDIGLL HLQDDRDFED FLLDFEEDVK VLHSVQCTPS
AGPFKPCDHL FGSWLTRIGV WLIVLLSFVC NALVIATVFR PLSYVPSIKL LIGLIAIINT
LMGLSSGVLA TVDALTFGNF AQYGAWWESG VGCQITGFLS VFAAETSVFL LTVAALERGF
SIKCTTKFET KSSFLSVKLS IVFCFLLSII IAVSPLMSGS TYGTSPFCFP LLFGDPSSMV
FMVALVLLNS LCFLVMTVAY TKLYCSLEKG ELENVWDCSM VKHIALLLFT NCILYCPVAF
LSFSSLLNLT FISPEVNKSI LLLIIPLPAC LNPLLYILFN PHFKEDIGSL KNGDMLWSRS
RHTSFASVSS EDAEKQSCDS TQALVTFASS SISFDLPATS SSSSYQMSNN YKLSAVAFVP
CH
