LGR5_BOVIN
ID LGR5_BOVIN Reviewed; 907 AA.
AC F1MT22;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Leucine-rich repeat-containing G-protein coupled receptor 5;
DE Flags: Precursor;
GN Name=LGR5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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; DAAA02012284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02012285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02012286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02012287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02012288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1MT22; -.
DR SMR; F1MT22; -.
DR STRING; 9913.ENSBTAP00000017631; -.
DR PaxDb; F1MT22; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2087; Eukaryota.
DR HOGENOM; CLU_006843_0_0_1; -.
DR InParanoid; F1MT22; -.
DR OrthoDB; 340670at2759; -.
DR TreeFam; TF316814; -.
DR Proteomes; UP000009136; Unplaced.
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; 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_0000422817"
FT TOPO_DOM 22..553
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 575..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..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..767
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..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 185..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 421..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 CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
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; 99415 MW; 269964A8EF196A30 CRC64;
MDTSSVGVLL SLPVLLQLAA GGGSPRPGTL LRGCPAHCQC EPDGRMLLRV DCSDLGLSEL
PSNLSVFTSY LDLSMNNISQ LPPSPLHSLR FLEELRLAGN ALTYIPKGAF AGLYSLKVLM
LQNNHLRQVP TEALQNLRSL QSLRLDANRI SSVPPSCFSG LHSLRHLWLD DNALTEIPVQ
AFRSLSALQA MTLALNKIHH IPDYAFGNLS SLVVLHLHNN RIHSLGKKCF DGLHSLETLD
LNYNNLDEFP TAVRTLSNLK ELGFHSNNIK SIPEKAFVGN PSLITIHFYD NPIQLVGRSA
FQHLPELRTL TLNGASQITE FPDLTGTASL ESLTLTGAQI SSLPQTVCDQ LPNLQVLDLS
YNLLEDLPSF SVCQKLQKID LRHNEIYEIQ ADTFQQLFSL RSLNLAWNKI AIIDPNAFST
LPSLRKLDLS SNRLSSIPVT GLHGLTHLKL TGNHALQSLI SSENFPELKV IEMPYAYQCC
AFGVCENVYK ISNPWSKGDN STAEDLHKKD AGVFQVQDER DLEDFLLDFE EDLRALHPVR
CSPSPGPFKL CEYLFGSWLI RIGVWTIAVL ALTCNALVTS TVFRAAVYIS SIKLLIGLIA
AVNMLMGVSS AVLAGVDAFT FGSFAQHGAW WEQAVGCQVV GFLSIFASES SVFLLTLAAL
ERGWSVKCSA KFETQTPFPS LRATLALCAL LAGTVAAVPL LGGSEYSASP LCLPLPFGEP
RATGYMVALV LLNSLCFLVM TVAYTRLYCH LEKGDLESMW DCSMVKHVAL LLFTNCILHC
PVAFLSFSSL LNLTFISPEV IKFILLVIVP LPACLNPLLY ILFNPHFKED LGSLGKQTHF
WTRSKHTSLM SINSDDVEKQ SCDSTQALVT FTSASIAYDL PSSSGSPPAY PMTESCHLSS
VAFVPCL
