RSPO3_HUMAN
ID RSPO3_HUMAN Reviewed; 272 AA.
AC Q9BXY4; B2RC27; Q5VTV4; Q96K87;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=R-spondin-3;
DE AltName: Full=Protein with TSP type-1 repeat;
DE Short=hPWTSR;
DE AltName: Full=Roof plate-specific spondin-3;
DE Short=hRspo3;
DE AltName: Full=Thrombospondin type-1 domain-containing protein 2;
DE Flags: Precursor;
GN Name=RSPO3; Synonyms=PWTSR, THSD2;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12463421; DOI=10.1023/a:1020479301379;
RA Chen J.-Z., Wang S., Tang R., Yang Q.-S., Zhao E., Chao Y., Ying K.,
RA Xie Y., Mao Y.-M.;
RT "Cloning and identification of a cDNA that encodes a novel human protein
RT with thrombospondin type I repeat domain, hPWTSR.";
RL Mol. Biol. Rep. 29:287-292(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [6]
RP FUNCTION, AND INTERACTION WITH LGR4 AND LGR5.
RX PubMed=21909076; DOI=10.1038/embor.2011.175;
RA Glinka A., Dolde C., Kirsch N., Huang Y.L., Kazanskaya O., Ingelfinger D.,
RA Boutros M., Cruciat C.M., Niehrs C.;
RT "LGR4 and LGR5 are R-spondin receptors mediating Wnt/beta-catenin and
RT Wnt/PCP signalling.";
RL EMBO Rep. 12:1055-1061(2011).
RN [7]
RP FUNCTION, AND INTERACTION WITH LGR4; LGR5 AND LGR6.
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 [8]
RP FUNCTION, AND INTERACTION WITH LGR6.
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=26766444; DOI=10.1016/j.devcel.2015.12.015;
RA Scholz B., Korn C., Wojtarowicz J., Mogler C., Augustin I., Boutros M.,
RA Niehrs C., Augustin H.G.;
RT "Endothelial RSPO3 controls vascular stability and pruning through non-
RT canonical WNT/Ca(2+)/NFAT signaling.";
RL Dev. Cell 36:79-93(2016).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF PHE-106 AND PHE-110.
RX PubMed=29769720; DOI=10.1038/s41586-018-0118-y;
RA Szenker-Ravi E., Altunoglu U., Leushacke M., Bosso-Lefevre C., Khatoo M.,
RA Thi Tran H., Naert T., Noelanders R., Hajamohideen A., Beneteau C.,
RA de Sousa S.B., Karaman B., Latypova X., Basaran S., Yuecel E.B., Tan T.T.,
RA Vlaminck L., Nayak S.S., Shukla A., Girisha K.M., Le Caignec C.,
RA Soshnikova N., Uyguner Z.O., Vleminckx K., Barker N., Kayserili H.,
RA Reversade B.;
RT "RSPO2 inhibition of RNF43 and ZNRF3 governs limb development independently
RT of LGR4/5/6.";
RL Nature 557:564-569(2018).
CC -!- FUNCTION: Activator of the canonical Wnt signaling pathway by acting as
CC a ligand for LGR4-6 receptors, which acts as a key regulator of
CC angiogenesis. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6
CC associate 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. Also
CC regulates the canonical Wnt/beta-catenin-dependent pathway and non-
CC canonical Wnt signaling by acting as an inhibitor of ZNRF3, an
CC important regulator of the Wnt signaling pathway. Acts as a ligand for
CC frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway
CC (PubMed:21727895, PubMed:21909076, PubMed:22615920). Acts as a key
CC regulator of angiogenesis by controlling vascular stability and
CC pruning: acts by activating the non-canonical Wnt signaling pathway in
CC endothelial cells (By similarity) (PubMed:21727895, PubMed:21909076,
CC PubMed:22615920). Can also amplify Wnt signaling pathway independently
CC of LGR4-6 receptors, possibly by acting as a direct antagonistic ligand
CC to RNF43 and ZNRF3 (PubMed:29769720). {ECO:0000250|UniProtKB:Q2TJ95,
CC ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:21909076,
CC ECO:0000269|PubMed:22615920, ECO:0000269|PubMed:29769720}.
CC -!- SUBUNIT: Interacts with the extracellular domain of FZD8 and LRP6 (By
CC similarity). It however does not form a ternary complex with FZD8 and
CC LRP6 (By similarity). Interacts with WNT1 (By similarity). Binds
CC heparin. Interacts with LGR4, LGR5 and LGR6 (PubMed:21727895,
CC PubMed:21909076, PubMed:22615920). {ECO:0000250|UniProtKB:Q2TJ95,
CC ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:21909076,
CC ECO:0000269|PubMed:22615920}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q2TJ95}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BXY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXY4-2; Sequence=VSP_018324;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher level
CC in placenta, small intestine, fetal thymus and lymph node
CC (PubMed:12463421). Highly expressed in endothelial cells
CC (PubMed:26766444). {ECO:0000269|PubMed:12463421,
CC ECO:0000269|PubMed:26766444}.
CC -!- DOMAIN: The FU repeats are required for activation and stabilization of
CC beta-catenin. {ECO:0000250|UniProtKB:Q2TJ95}.
CC -!- SIMILARITY: Belongs to the R-spondin family. {ECO:0000305}.
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DR EMBL; AF251057; AAK34947.1; -; mRNA.
DR EMBL; AK027346; BAB55051.1; -; mRNA.
DR EMBL; AK314912; BAG37424.1; -; mRNA.
DR EMBL; AL590733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48115.1; -; Genomic_DNA.
DR EMBL; BC022367; AAH22367.1; -; mRNA.
DR CCDS; CCDS5135.1; -. [Q9BXY4-1]
DR RefSeq; NP_116173.2; NM_032784.4. [Q9BXY4-1]
DR AlphaFoldDB; Q9BXY4; -.
DR SMR; Q9BXY4; -.
DR BioGRID; 124315; 6.
DR CORUM; Q9BXY4; -.
DR IntAct; Q9BXY4; 5.
DR MINT; Q9BXY4; -.
DR STRING; 9606.ENSP00000349131; -.
DR GlyGen; Q9BXY4; 1 site.
DR iPTMnet; Q9BXY4; -.
DR PhosphoSitePlus; Q9BXY4; -.
DR BioMuta; RSPO3; -.
DR DMDM; 74752442; -.
DR jPOST; Q9BXY4; -.
DR MassIVE; Q9BXY4; -.
DR PaxDb; Q9BXY4; -.
DR PeptideAtlas; Q9BXY4; -.
DR PRIDE; Q9BXY4; -.
DR ProteomicsDB; 79540; -. [Q9BXY4-1]
DR ProteomicsDB; 79541; -. [Q9BXY4-2]
DR ABCD; Q9BXY4; 1 sequenced antibody.
DR Antibodypedia; 32746; 236 antibodies from 33 providers.
DR DNASU; 84870; -.
DR Ensembl; ENST00000356698.9; ENSP00000349131.4; ENSG00000146374.14. [Q9BXY4-1]
DR Ensembl; ENST00000368317.3; ENSP00000357300.3; ENSG00000146374.14. [Q9BXY4-2]
DR GeneID; 84870; -.
DR KEGG; hsa:84870; -.
DR MANE-Select; ENST00000356698.9; ENSP00000349131.4; NM_032784.5; NP_116173.2.
DR UCSC; uc003qar.5; human. [Q9BXY4-1]
DR CTD; 84870; -.
DR DisGeNET; 84870; -.
DR GeneCards; RSPO3; -.
DR HGNC; HGNC:20866; RSPO3.
DR HPA; ENSG00000146374; Tissue enhanced (endometrium).
DR MIM; 610574; gene.
DR neXtProt; NX_Q9BXY4; -.
DR OpenTargets; ENSG00000146374; -.
DR PharmGKB; PA134885289; -.
DR VEuPathDB; HostDB:ENSG00000146374; -.
DR eggNOG; KOG3525; Eukaryota.
DR GeneTree; ENSGT00940000157815; -.
DR HOGENOM; CLU_064219_0_0_1; -.
DR InParanoid; Q9BXY4; -.
DR OMA; WFFITLN; -.
DR OrthoDB; 1441603at2759; -.
DR PhylomeDB; Q9BXY4; -.
DR TreeFam; TF331799; -.
DR PathwayCommons; Q9BXY4; -.
DR Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
DR Reactome; R-HSA-8939256; RUNX1 regulates transcription of genes involved in WNT signaling.
DR SignaLink; Q9BXY4; -.
DR SIGNOR; Q9BXY4; -.
DR BioGRID-ORCS; 84870; 9 hits in 1064 CRISPR screens.
DR ChiTaRS; RSPO3; human.
DR GeneWiki; RSPO3; -.
DR GenomeRNAi; 84870; -.
DR Pharos; Q9BXY4; Tbio.
DR PRO; PR:Q9BXY4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9BXY4; protein.
DR Bgee; ENSG00000146374; Expressed in mucosa of stomach and 160 other tissues.
DR Genevisible; Q9BXY4; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0001974; P:blood vessel remodeling; ISS:UniProtKB.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; TAS:ParkinsonsUK-UCL.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR CDD; cd00064; FU; 1.
DR Gene3D; 2.20.100.10; -; 1.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR042994; RSPO3.
DR InterPro; IPR043601; Rspo_Fu-CRD_dom.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR044004; TSP1_spondin_dom.
DR PANTHER; PTHR46987:SF1; PTHR46987:SF1; 2.
DR Pfam; PF15913; Furin-like_2; 1.
DR Pfam; PF19028; TSP1_spondin; 1.
DR SMART; SM00261; FU; 2.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Heparin-binding;
KW Reference proteome; Repeat; Secreted; Sensory transduction; Signal;
KW Wnt signaling pathway.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..272
FT /note="R-spondin-3"
FT /id="PRO_0000234443"
FT REPEAT 35..86
FT /note="FU 1"
FT REPEAT 92..135
FT /note="FU 2"
FT DOMAIN 147..207
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 201..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 45..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 57..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 80..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 98..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 102..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 114..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 129..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 148..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 159..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 199..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT VAR_SEQ 266..272
FT /note="VSVSTVH -> GIEVTLAEGLTSVSQRTQPTPCRRRYL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018324"
FT MUTAGEN 106
FT /note="F->A: Loss of LGR4/5/6-binding, no effect on WNT3A
FT signaling; when associated with A-110."
FT /evidence="ECO:0000269|PubMed:29769720"
FT MUTAGEN 110
FT /note="F->A: Loss of LGR4/5/6-binding, no effect on WNT3A
FT signaling; when associated with A-106."
FT /evidence="ECO:0000269|PubMed:29769720"
FT CONFLICT 41
FT /note="C -> R (in Ref. 2; BAB55051)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="R -> I (in Ref. 2; BAB55051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 30929 MW; CACAEC6B7E781189 CRC64;
MHLRLISWLF IILNFMEYIG SQNASRGRRQ RRMHPNVSQG CQGGCATCSD YNGCLSCKPR
LFFALERIGM KQIGVCLSSC PSGYYGTRYP DINKCTKCKA DCDTCFNKNF CTKCKSGFYL
HLGKCLDNCP EGLEANNHTM ECVSIVHCEV SEWNPWSPCT KKGKTCGFKR GTETRVREII
QHPSAKGNLC PPTNETRKCT VQRKKCQKGE RGKKGRERKR KKPNKGESKE AIPDSKSLES
SKEIPEQREN KQQQKKRKVQ DKQKSVSVST VH
