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O75473 (LGR5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine-rich repeat-containing G-protein coupled receptor 5
Alternative name(s):
G-protein coupled receptor 49
G-protein coupled receptor 67
G-protein coupled receptor HG38
Gene names
Name:LGR5
Synonyms:GPR49, GPR67
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length907 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14

Subunit structure

Identified in a complex composed of RNF43, LGR5 and RSPO1. Ref.15

Subcellular location

Cell membrane; Multi-pass membrane protein. Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein. Note: Rapidly and constitutively internalized to the trans-Golgi network at steady state. Internalization to the trans-Golgi network may be the result of phosphorylation at Ser-861 and Ser-864; however, the phosphorylation event has not been proven (Ref.13). Ref.11 Ref.12 Ref.13

Tissue specificity

Expressed in skeletal muscle, placenta, spinal cord, and various region of brain. Expressed at the base of crypts in colonic and small mucosa stem cells. In premalignant cancer expression is not restricted to the cript base. Overexpressed in cancers of the ovary, colon and liver. Ref.6 Ref.7 Ref.8

Miscellaneous

LGR5 is used as a marker of adult tissue stem cells in the intestine, stomach, hair follicle, and mammary epithelium (Ref.8).

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Contains 16 LRR (leucine-rich) repeats.

Contains 1 LRRNT domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75473-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O75473-2)

The sequence of this isoform differs from the canonical sequence as follows:
     263-286: Missing.
Isoform 3 (identifier: O75473-3)

The sequence of this isoform differs from the canonical sequence as follows:
     143-214: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 907886Leucine-rich repeat-containing G-protein coupled receptor 5
PRO_0000012794

Regions

Topological domain22 – 561540Extracellular Potential
Transmembrane562 – 58221Helical; Name=1; Potential
Topological domain583 – 59311Cytoplasmic Potential
Transmembrane594 – 61421Helical; Name=2; Potential
Topological domain615 – 63824Extracellular Potential
Transmembrane639 – 65921Helical; Name=3; Potential
Topological domain660 – 68223Cytoplasmic Potential
Transmembrane683 – 70321Helical; Name=4; Potential
Topological domain704 – 72219Extracellular Potential
Transmembrane723 – 74321Helical; Name=5; Potential
Topological domain744 – 76724Cytoplasmic Potential
Transmembrane768 – 78821Helical; Name=6; Potential
Topological domain789 – 80214Extracellular Potential
Transmembrane803 – 82321Helical; Name=7; Potential
Topological domain824 – 90784Cytoplasmic Potential
Domain25 – 6642LRRNT
Repeat67 – 9024LRR 1
Repeat91 – 11222LRR 2
Repeat115 – 13622LRR 3
Repeat139 – 16022LRR 4
Repeat163 – 18422LRR 5
Repeat187 – 20822LRR 6
Repeat211 – 23222LRR 7
Repeat235 – 25622LRR 8
Repeat258 – 27922LRR 9
Repeat282 – 30322LRR 10
Repeat306 – 32823LRR 11
Repeat329 – 35022LRR 12
Repeat353 – 37422LRR 13
Repeat375 – 39622LRR 14
Repeat399 – 42022LRR 15
Repeat423 – 44624LRR 16

Amino acid modifications

Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Ref.15
Glycosylation5001N-linked (GlcNAc...) Potential
Glycosylation7921N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 40 Ref.14 Ref.15
Disulfide bond38 ↔ 52 Ref.14 Ref.15
Disulfide bond348 ↔ 373 Ref.14 Ref.15
Disulfide bond479 ↔ 541 Ref.14 Ref.15
Disulfide bond637 ↔ 712 By similarity

Natural variations

Alternative sequence143 – 21472Missing in isoform 3.
VSP_054782
Alternative sequence263 – 28624Missing in isoform 2.
VSP_037746
Natural variant3831H → R.
Corresponds to variant rs12303775 [ dbSNP | Ensembl ].
VAR_049411
Natural variant6661V → A. Ref.5
Corresponds to variant rs17109924 [ dbSNP | Ensembl ].
VAR_049412

Experimental info

Mutagenesis1461D → F: Abolishes activation of Wnt signaling. Ref.14
Mutagenesis1701D → F: Abolishes activation of Wnt signaling. Ref.14
Mutagenesis1901A → D: Abolishes activation of Wnt signaling. Ref.14
Mutagenesis8611S → A: Impaired internalization to the trans-Golgi network; when associated with A-864. Ref.13
Mutagenesis8641S → A: Impaired internalization to the trans-Golgi network; when associated with A-861. Ref.13
Sequence conflict901R → H in AAC77911. Ref.2
Sequence conflict2121L → W in AAC77911. Ref.2

Secondary structure

.......................................................................... 907
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 822D5C5E6F0D9092

FASTA90799,998
        10         20         30         40         50         60 
MDTSRLGVLL SLPVLLQLAT GGSSPRSGVL LRGCPTHCHC EPDGRMLLRV DCSDLGLSEL 

        70         80         90        100        110        120 
PSNLSVFTSY LDLSMNNISQ LLPNPLPSLR FLEELRLAGN ALTYIPKGAF TGLYSLKVLM 

       130        140        150        160        170        180 
LQNNQLRHVP TEALQNLRSL QSLRLDANHI SYVPPSCFSG LHSLRHLWLD DNALTEIPVQ 

       190        200        210        220        230        240 
AFRSLSALQA MTLALNKIHH IPDYAFGNLS SLVVLHLHNN RIHSLGKKCF DGLHSLETLD 

       250        260        270        280        290        300 
LNYNNLDEFP TAIRTLSNLK ELGFHSNNIR SIPEKAFVGN PSLITIHFYD NPIQFVGRSA 

       310        320        330        340        350        360 
FQHLPELRTL TLNGASQITE FPDLTGTANL ESLTLTGAQI SSLPQTVCNQ LPNLQVLDLS 

       370        380        390        400        410        420 
YNLLEDLPSF SVCQKLQKID LRHNEIYEIK VDTFQQLLSL RSLNLAWNKI AIIHPNAFST 

       430        440        450        460        470        480 
LPSLIKLDLS SNLLSSFPIT GLHGLTHLKL TGNHALQSLI SSENFPELKV IEMPYAYQCC 

       490        500        510        520        530        540 
AFGVCENAYK ISNQWNKGDN SSMDDLHKKD AGMFQAQDER DLEDFLLDFE EDLKALHSVQ 

       550        560        570        580        590        600 
CSPSPGPFKP CEHLLDGWLI RIGVWTIAVL ALTCNALVTS TVFRSPLYIS PIKLLIGVIA 

       610        620        630        640        650        660 
AVNMLTGVSS AVLAGVDAFT FGSFARHGAW WENGVGCHVI GFLSIFASES SVFLLTLAAL 

       670        680        690        700        710        720 
ERGFSVKYSA KFETKAPFSS LKVIILLCAL LALTMAAVPL LGGSKYGASP LCLPLPFGEP 

       730        740        750        760        770        780 
STMGYMVALI LLNSLCFLMM TIAYTKLYCN LDKGDLENIW DCSMVKHIAL LLFTNCILNC 

       790        800        810        820        830        840 
PVAFLSFSSL INLTFISPEV IKFILLVVVP LPACLNPLLY ILFNPHFKED LVSLRKQTYV 

       850        860        870        880        890        900 
WTRSKHPSLM SINSDDVEKQ SCDSTQALVT FTSSSITYDL PPSSVPSPAY PVTESCHLSS 


VAFVPCL 

« Hide

Isoform 2 [UniParc].

Checksum: 50B293FCFCAED440
Show »

FASTA88397,404
Isoform 3 [UniParc].

Checksum: 352096C4523C1E2F
Show »

FASTA83592,006

References

« Hide 'large scale' references
[1]"Identification and cloning of an orphan G protein-coupled receptor of the glycoprotein hormone receptor subfamily."
McDonald T., Wang R., Bailey W., Xie G., Chen F., Caskey C.T., Liu Q.
Biochem. Biophys. Res. Commun. 247:266-270(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Characterization of two LGR genes homologous to gonadotropin and thyrotropin receptors with extracellular leucine-rich repeats and a G protein-coupled, seven-transmembrane region."
Hsu S.Y., Liang S.-G., Hsueh A.J.W.
Mol. Endocrinol. 12:1830-1845(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]"Alternatively spliced transcript of the GPR49-mRNA occur in different tumor cell lines and soft tissue sarcoma."
Rot S., Taubert H., Bache M., Vordermark D., Kappler M.
Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ALA-666.
[6]"Overexpression of orphan G-protein-coupled receptor, Gpr49, in human hepatocellular carcinomas with beta-catenin mutations."
Yamamoto Y., Sakamoto M., Fujii G., Tsuiji H., Kenetaka K., Asaka M., Hirohashi S.
Hepatology 37:528-533(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Identification of overexpression of orphan G protein-coupled receptor GPR49 in human colon and ovarian primary tumors."
McClanahan T., Koseoglu S., Smith K., Grein J., Gustafson E., Black S., Kirschmeier P., Samatar A.A.
Cancer Biol. Ther. 5:419-426(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Immunostaining of Lgr5, an intestinal stem cell marker, in normal and premalignant human gastrointestinal tissue."
Becker L., Huang Q., Mashimo H.
ScientificWorldJournal 8:1168-1176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"LGR4 and LGR5 are R-spondin receptors mediating Wnt/beta-catenin and Wnt/PCP signalling."
Glinka A., Dolde C., Kirsch N., Huang Y.L., Kazanskaya O., Ingelfinger D., Boutros M., Cruciat C.M., Niehrs C.
EMBO Rep. 12:1055-1061(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RSPO1; RSPO2; RSPO3 AND RSPO4.
[10]"Lgr5 homologues associate with Wnt receptors and mediate R-spondin signalling."
de Lau W., Barker N., Low T.Y., Koo B.K., Li V.S., Teunissen H., Kujala P., Haegebarth A., Peters P.J., van de Wetering M., Stange D.E., van Es J.E., Guardavaccaro D., Schasfoort R.B., Mohri Y., Nishimori K., Mohammed S., Heck A.J., Clevers H.
Nature 476:293-297(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RSPO1; RSPO2; RSPO3 AND RSPO4.
[11]"R-spondins function as ligands of the orphan receptors LGR4 and LGR5 to regulate Wnt/beta-catenin signaling."
Carmon K.S., Gong X., Lin Q., Thomas A., Liu Q.
Proc. Natl. Acad. Sci. U.S.A. 108:11452-11457(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RSPO1; RSPO2; RSPO3 AND RSPO4.
[12]"R-Spondin potentiates Wnt/beta-catenin signaling through orphan receptors LGR4 and LGR5."
Ruffner H., Sprunger J., Charlat O., Leighton-Davies J., Grosshans B., Salathe A., Zietzling S., Beck V., Therier M., Isken A., Xie Y., Zhang Y., Hao H., Shi X., Liu D., Song Q., Clay I., Hintzen G. expand/collapse author list , Tchorz J., Bouchez L.C., Michaud G., Finan P., Myer V.E., Bouwmeester T., Porter J., Hild M., Bassilana F., Parker C.N., Cong F.
PLoS ONE 7:E40976-E40976(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RSPO1.
[13]"Constitutive Internalization of the Leucine-rich G Protein-coupled Receptor-5 (LGR5) to the Trans-Golgi Network."
Snyder J.C., Rochelle L.K., Lyerly H.K., Caron M.G., Barak L.S.
J. Biol. Chem. 288:10286-10297(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF SER-861 AND SER-864.
[14]"Structure of stem cell growth factor R-spondin 1 in complex with the ectodomain of its receptor LGR5."
Peng W.C., de Lau W., Forneris F., Granneman J.C., Huch M., Clevers H., Gros P.
Cell Rep. 3:1885-1892(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 22-543 IN COMPLEX WITH RSPO1, FUNCTION, MUTAGENESIS OF ASP-146; ASP-170 AND ALA-190, DISULFIDE BONDS.
[15]"The structural basis of R-spondin recognition by LGR5 and RNF43."
Chen P.H., Chen X., Lin Z., Fang D., He X.
Genes Dev. 27:1345-1350(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 32-557 IN COMPLEX WITH RNF43 AND RSPO1, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-208.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF062006 mRNA. Translation: AAC28019.1.
AF061444 mRNA. Translation: AAC77911.1.
FN820440 mRNA. Translation: CBL95002.2.
AC078860 Genomic DNA. No translation available.
AC090116 Genomic DNA. No translation available.
BC096324 mRNA. Translation: AAH96324.1.
BC096325 mRNA. Translation: AAH96325.1.
BC096326 mRNA. Translation: AAH96326.1.
BC099650 mRNA. Translation: AAH99650.1.
CCDSCCDS61194.1. [O75473-2]
CCDS9000.1. [O75473-1]
PIRJE0176.
RefSeqNP_001264155.1. NM_001277226.1. [O75473-2]
NP_001264156.1. NM_001277227.1. [O75473-3]
NP_003658.1. NM_003667.3. [O75473-1]
UniGeneHs.658889.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BSRX-ray3.20A/B22-543[»]
4BSSX-ray3.20A/B/E/F22-543[»]
4BSTX-ray4.30A/B22-543[»]
4BSUX-ray3.20A/B/E/F22-543[»]
4KNGX-ray2.50A/B32-557[»]
ProteinModelPortalO75473.
SMRO75473. Positions 28-543.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114119. 1 interaction.
STRING9606.ENSP00000266674.

Chemistry

GuidetoPHARMACOLOGY148.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteO75473.

Proteomic databases

MaxQBO75473.
PaxDbO75473.
PRIDEO75473.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266674; ENSP00000266674; ENSG00000139292. [O75473-1]
ENST00000536515; ENSP00000443033; ENSG00000139292.
ENST00000540815; ENSP00000441035; ENSG00000139292. [O75473-2]
GeneID8549.
KEGGhsa:8549.
UCSCuc001swl.4. human. [O75473-1]
uc001swm.4. human. [O75473-2]

Organism-specific databases

CTD8549.
GeneCardsGC12P071833.
HGNCHGNC:4504. LGR5.
HPAHPA012530.
MIM606667. gene.
neXtProtNX_O75473.
PharmGKBPA28894.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000231829.
HOVERGENHBG031675.
InParanoidO75473.
KOK04308.
OMALENIWDC.
OrthoDBEOG7DNNTF.
PhylomeDBO75473.
TreeFamTF316814.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressO75473.
BgeeO75473.
CleanExHS_LGR5.
GenevestigatorO75473.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002131. Gphrmn_rcpt_fam.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR026906. LRR_5.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
PF00560. LRR_1. 1 hit.
PF13306. LRR_5. 1 hit.
PF13855. LRR_8. 2 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PRINTSPR00373. GLYCHORMONER.
PR00237. GPCRRHODOPSN.
SMARTSM00369. LRR_TYP. 8 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS51450. LRR. 15 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiLGR5.
GenomeRNAi8549.
NextBio35495810.
PROO75473.
SOURCESearch...

Entry information

Entry nameLGR5_HUMAN
AccessionPrimary (citable) accession number: O75473
Secondary accession number(s): D8MCT0 expand/collapse secondary AC list , Q4VAM0, Q4VAM2, Q9UP75
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries