LGR6_HUMAN
ID LGR6_HUMAN Reviewed; 967 AA.
AC Q9HBX8; Q5T509; Q5T512; Q6UY15; Q86VU0; Q96K69; Q9BYD7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Leucine-rich repeat-containing G-protein coupled receptor 6;
DE Flags: Precursor;
GN Name=LGR6; ORFNames=UNQ6427/PRO21331, VTS20631;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10935549; DOI=10.1210/mend.14.8.0510;
RA Hsu S.Y., Kudo M., Chen T., Nakabayashi K., Bhalla A., van der Spek P.J.,
RA van Duin M., Hsueh A.J.W.;
RT "The three subfamilies of leucine-rich repeat-containing G protein-coupled
RT receptors (LGR): identification of LGR6 and LGR7 and the signaling
RT mechanism for LGR7.";
RL Mol. Endocrinol. 14:1257-1271(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-592.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 40-967 (ISOFORM 3), AND VARIANT ALA-592.
RA Okaze H., Hayashi A., Kozuma S., Saito T.;
RT "A member of the G-protein coupled receptor family.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 545-967.
RX PubMed=12044878; DOI=10.1016/s0014-5793(02)02775-8;
RA Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.;
RT "Identification of G protein-coupled receptor genes from the human genome
RT sequence.";
RL FEBS Lett. 520:97-101(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 570-967.
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH RSPO1; RSPO2; RSPO3 AND RSPO4.
RX PubMed=21727895; DOI=10.1038/nature10337;
RA de Lau W., Barker N., Low T.Y., Koo B.K., Li V.S., Teunissen H., Kujala P.,
RA Haegebarth A., Peters P.J., van de Wetering M., Stange D.E., van Es J.E.,
RA Guardavaccaro D., Schasfoort R.B., Mohri Y., Nishimori K., Mohammed S.,
RA Heck A.J., Clevers H.;
RT "Lgr5 homologues associate with Wnt receptors and mediate R-spondin
RT signalling.";
RL Nature 476:293-297(2011).
RN [9]
RP FUNCTION, INTERACTION WITH RSPO1; RSPO2 AND RSPO3, SUBCELLULAR LOCATION,
RP AND CHARACTERIZATION OF VARIANTS CYS-725 AND HIS-928.
RX PubMed=22615920; DOI=10.1371/journal.pone.0037137;
RA Gong X., Carmon K.S., Lin Q., Thomas A., Yi J., Liu Q.;
RT "LGR6 is a high affinity receptor of R-spondins and potentially functions
RT as a tumor suppressor.";
RL PLoS ONE 7:E37137-E37137(2012).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-725 AND HIS-928.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt
CC signaling pathway and acts as a marker of multipotent stem cells in the
CC epidermis. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4),
CC associates with phosphorylated LRP6 and frizzled receptors that are
CC activated by extracellular Wnt receptors, triggering the canonical Wnt
CC signaling pathway to increase expression of target genes. In contrast
CC to classical G-protein coupled receptors, does not activate
CC heterotrimeric G-proteins to transduce the signal. May act as a tumor
CC suppressor. {ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:22615920}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22615920};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22615920}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q9HBX8-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9HBX8-1; Sequence=VSP_028006, VSP_028007;
CC Name=2;
CC IsoId=Q9HBX8-2; Sequence=VSP_013596;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55071.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF190501; AAG17168.1; -; mRNA.
DR EMBL; AY358119; AAQ88486.1; -; mRNA.
DR EMBL; AL356953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047905; AAH47905.2; -; mRNA.
DR EMBL; AB049405; BAB39854.1; -; mRNA.
DR EMBL; AB083616; BAB89329.1; -; Genomic_DNA.
DR EMBL; AK027377; BAB55071.1; ALT_INIT; mRNA.
DR CCDS; CCDS1424.1; -. [Q9HBX8-2]
DR CCDS; CCDS30971.1; -. [Q9HBX8-3]
DR CCDS; CCDS30972.1; -. [Q9HBX8-1]
DR RefSeq; NP_001017403.1; NM_001017403.1. [Q9HBX8-3]
DR RefSeq; NP_001017404.1; NM_001017404.1. [Q9HBX8-1]
DR RefSeq; NP_067649.2; NM_021636.2. [Q9HBX8-2]
DR AlphaFoldDB; Q9HBX8; -.
DR SMR; Q9HBX8; -.
DR BioGRID; 121893; 4.
DR STRING; 9606.ENSP00000356247; -.
DR GuidetoPHARMACOLOGY; 149; -.
DR GlyGen; Q9HBX8; 2 sites.
DR iPTMnet; Q9HBX8; -.
DR PhosphoSitePlus; Q9HBX8; -.
DR BioMuta; LGR6; -.
DR DMDM; 158519993; -.
DR MassIVE; Q9HBX8; -.
DR PaxDb; Q9HBX8; -.
DR PeptideAtlas; Q9HBX8; -.
DR PRIDE; Q9HBX8; -.
DR ProteomicsDB; 81604; -. [Q9HBX8-3]
DR ProteomicsDB; 81605; -. [Q9HBX8-1]
DR ProteomicsDB; 81606; -. [Q9HBX8-2]
DR Antibodypedia; 34525; 362 antibodies from 33 providers.
DR DNASU; 59352; -.
DR Ensembl; ENST00000255432.11; ENSP00000255432.7; ENSG00000133067.18. [Q9HBX8-2]
DR Ensembl; ENST00000367278.8; ENSP00000356247.3; ENSG00000133067.18. [Q9HBX8-3]
DR Ensembl; ENST00000439764.2; ENSP00000387869.2; ENSG00000133067.18. [Q9HBX8-1]
DR GeneID; 59352; -.
DR KEGG; hsa:59352; -.
DR MANE-Select; ENST00000367278.8; ENSP00000356247.3; NM_001017403.2; NP_001017403.1.
DR UCSC; uc001gxu.4; human. [Q9HBX8-3]
DR CTD; 59352; -.
DR DisGeNET; 59352; -.
DR GeneCards; LGR6; -.
DR HGNC; HGNC:19719; LGR6.
DR HPA; ENSG00000133067; Tissue enhanced (brain, pituitary gland).
DR MIM; 606653; gene.
DR neXtProt; NX_Q9HBX8; -.
DR OpenTargets; ENSG00000133067; -.
DR PharmGKB; PA134927114; -.
DR VEuPathDB; HostDB:ENSG00000133067; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000159939; -.
DR HOGENOM; CLU_006843_0_0_1; -.
DR InParanoid; Q9HBX8; -.
DR OrthoDB; 340670at2759; -.
DR PhylomeDB; Q9HBX8; -.
DR TreeFam; TF316814; -.
DR PathwayCommons; Q9HBX8; -.
DR Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
DR BioGRID-ORCS; 59352; 11 hits in 1060 CRISPR screens.
DR GeneWiki; LGR6; -.
DR GenomeRNAi; 59352; -.
DR Pharos; Q9HBX8; Tbio.
DR PRO; PR:Q9HBX8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9HBX8; protein.
DR Bgee; ENSG00000133067; Expressed in right coronary artery and 140 other tissues.
DR ExpressionAtlas; Q9HBX8; baseline and differential.
DR Genevisible; Q9HBX8; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0016500; F:protein-hormone receptor activity; IEA:InterPro.
DR GO; GO:0048495; F:Roundabout binding; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:1990523; P:bone regeneration; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
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; 4.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 13.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Leucine-rich repeat; Membrane;
KW Receptor; Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix; Tumor suppressor; Wnt signaling pathway.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..967
FT /note="Leucine-rich repeat-containing G-protein coupled
FT receptor 6"
FT /id="PRO_0000069699"
FT TOPO_DOM 25..567
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..644
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..665
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..727
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..748
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 749..774
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 775..795
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 796..809
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 810..830
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 831..967
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..66
FT /note="LRRNT"
FT REPEAT 91..112
FT /note="LRR 1"
FT REPEAT 115..136
FT /note="LRR 2"
FT REPEAT 139..160
FT /note="LRR 3"
FT REPEAT 163..186
FT /note="LRR 4"
FT REPEAT 187..208
FT /note="LRR 5"
FT REPEAT 211..232
FT /note="LRR 6"
FT REPEAT 235..256
FT /note="LRR 7"
FT REPEAT 258..279
FT /note="LRR 8"
FT REPEAT 282..303
FT /note="LRR 9"
FT REPEAT 306..328
FT /note="LRR 10"
FT REPEAT 329..350
FT /note="LRR 11"
FT REPEAT 353..374
FT /note="LRR 12"
FT REPEAT 375..396
FT /note="LRR 13"
FT REPEAT 399..420
FT /note="LRR 14"
FT REPEAT 423..443
FT /note="LRR 15"
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 642..717
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..71
FT /note="MPSPPGLRALWLCAALCASRRAGGAPQPGPGPTACPAPCHCQEDGIMLSADC
FT SELGLSAVPGDLDPLTAYL -> MRLEGEGRSARAGQNLSRAGSARRGAPR (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:10935549"
FT /id="VSP_028006"
FT VAR_SEQ 1..71
FT /note="MPSPPGLRALWLCAALCASRRAGGAPQPGPGPTACPAPCHCQEDGIMLSADC
FT SELGLSAVPGDLDPLTAYL -> MGRPRLTLVCQVSIIISAR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013596"
FT VAR_SEQ 144..239
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10935549"
FT /id="VSP_028007"
FT VARIANT 267
FT /note="N -> K (in dbSNP:rs7553800)"
FT /id="VAR_049413"
FT VARIANT 516
FT /note="A -> S (in dbSNP:rs6668765)"
FT /id="VAR_033479"
FT VARIANT 592
FT /note="V -> A (in dbSNP:rs788795)"
FT /evidence="ECO:0000269|PubMed:12975309, ECO:0000269|Ref.5"
FT /id="VAR_059324"
FT VARIANT 725
FT /note="G -> C (in a colorectal cancer sample; somatic
FT mutation; no effect Wnt signlaing upon RSPO1-binding)"
FT /evidence="ECO:0000269|PubMed:16959974,
FT ECO:0000269|PubMed:22615920"
FT /id="VAR_035762"
FT VARIANT 928
FT /note="P -> H (in a colorectal cancer sample; somatic
FT mutation; no effect Wnt signlaing upon RSPO1-binding)"
FT /evidence="ECO:0000269|PubMed:16959974,
FT ECO:0000269|PubMed:22615920"
FT /id="VAR_035763"
FT CONFLICT 545..549
FT /note="CSPTP -> MISPT (in Ref. 6; BAB89329)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="W -> R (in Ref. 7; BAB55071)"
FT /evidence="ECO:0000305"
FT CONFLICT 963..967
FT /note="FASHV -> LLHTY (in Ref. 1; AAG17168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 967 AA; 104298 MW; 22E332E85DF8DCE0 CRC64;
MPSPPGLRAL WLCAALCASR RAGGAPQPGP GPTACPAPCH CQEDGIMLSA DCSELGLSAV
PGDLDPLTAY LDLSMNNLTE LQPGLFHHLR FLEELRLSGN HLSHIPGQAF SGLYSLKILM
LQNNQLGGIP AEALWELPSL QSLRLDANLI SLVPERSFEG LSSLRHLWLD DNALTEIPVR
ALNNLPALQA MTLALNRISH IPDYAFQNLT SLVVLHLHNN RIQHLGTHSF EGLHNLETLD
LNYNKLQEFP VAIRTLGRLQ ELGFHNNNIK AIPEKAFMGN PLLQTIHFYD NPIQFVGRSA
FQYLPKLHTL SLNGAMDIQE FPDLKGTTSL EILTLTRAGI RLLPSGMCQQ LPRLRVLELS
HNQIEELPSL HRCQKLEEIG LQHNRIWEIG ADTFSQLSSL QALDLSWNAI RSIHPEAFST
LHSLVKLDLT DNQLTTLPLA GLGGLMHLKL KGNLALSQAF SKDSFPKLRI LEVPYAYQCC
PYGMCASFFK ASGQWEAEDL HLDDEESSKR PLGLLARQAE NHYDQDLDEL QLEMEDSKPH
PSVQCSPTPG PFKPCEYLFE SWGIRLAVWA IVLLSVLCNG LVLLTVFAGG PVPLPPVKFV
VGAIAGANTL TGISCGLLAS VDALTFGQFS EYGARWETGL GCRATGFLAV LGSEASVLLL
TLAAVQCSVS VSCVRAYGKS PSLGSVRAGV LGCLALAGLA AALPLASVGE YGASPLCLPY
APPEGQPAAL GFTVALVMMN SFCFLVVAGA YIKLYCDLPR GDFEAVWDCA MVRHVAWLIF
ADGLLYCPVA FLSFASMLGL FPVTPEAVKS VLLVVLPLPA CLNPLLYLLF NPHFRDDLRR
LRPRAGDSGP LAYAAAGELE KSSCDSTQAL VAFSDVDLIL EASEAGRPPG LETYGFPSVT
LISCQQPGAP RLEGSHCVEP EGNHFGNPQP SMDGELLLRA EGSTPAGGGL SGGGGFQPSG
LAFASHV
