TPBG_HUMAN
ID TPBG_HUMAN Reviewed; 420 AA.
AC Q13641; A8K555;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Trophoblast glycoprotein;
DE AltName: Full=5T4 oncofetal antigen;
DE AltName: Full=5T4 oncofetal trophoblast glycoprotein;
DE Short=5T4 oncotrophoblast glycoprotein;
DE AltName: Full=M6P1;
DE AltName: Full=Wnt-activated inhibitory factor 1;
DE Short=WAIF1;
DE Flags: Precursor;
GN Name=TPBG; Synonyms=5T4;
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], AND PROTEIN SEQUENCE OF 52-75 AND 199-235.
RC TISSUE=Placenta;
RX PubMed=8132670; DOI=10.1016/s0021-9258(17)37110-7;
RA Myers K.A., Rahi-Saund V., Davison M.D., Young J.A., Cheater A.J.,
RA Stern P.L.;
RT "Isolation of a cDNA encoding 5T4 oncofetal trophoblast glycoprotein: an
RT antigen associated with metastasis contains leucine rich repeats.";
RL J. Biol. Chem. 269:9319-9324(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [7]
RP USE IN TUMOR IMMUNOTHERAPHY.
RX PubMed=12481437;
RA Mulryan K., Ryan M.G., Myers K.A., Shaw D., Wang W., Kingsman S.M.,
RA Stern P.L., Carroll M.W.;
RT "Attenuated recombinant vaccinia virus expressing oncofetal antigen (tumor-
RT associated antigen) 5T4 induces active therapy of established tumors.";
RL Mol. Cancer Ther. 1:1129-1137(2002).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-124.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP FUNCTION, AND MISCELLANEOUS.
RX PubMed=22100263; DOI=10.1016/j.devcel.2011.10.015;
RA Kagermeier-Schenk B., Wehner D., Ozhan-Kizil G., Yamamoto H., Li J.,
RA Kirchner K., Hoffmann C., Stern P., Kikuchi A., Schambony A., Weidinger G.;
RT "Waif1/5T4 inhibits Wnt/beta-catenin signaling and activates noncanonical
RT Wnt pathways by modifying LRP6 subcellular localization.";
RL Dev. Cell 21:1129-1143(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 60-345, SUBCELLULAR LOCATION, LRR
RP REPEATS, GLYCOSYLATION, DISULFIDE BONDS, AND MUTAGENESIS OF LYS-76; PHE-97;
RP ASN-124; ARG-214 AND TYR-325.
RX PubMed=24582434; DOI=10.1016/j.str.2014.01.009;
RA Zhao Y., Malinauskas T., Harlos K., Jones E.Y.;
RT "Structural insights into the inhibition of Wnt signaling by cancer antigen
RT 5T4/Wnt-activated inhibitory factor 1.";
RL Structure 22:612-620(2014).
CC -!- FUNCTION: May function as an inhibitor of Wnt/beta-catenin signaling by
CC indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6
CC internalization. {ECO:0000269|PubMed:22100263}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24582434};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:24582434}.
CC -!- TISSUE SPECIFICITY: Expressed by all types of trophoblasts as early as
CC 9 weeks of development. Specific for trophoblastic cells except for
CC amniotic epithelium. In adult tissues, the expression is limited to a
CC few epithelial cell types but is found on a variety of carcinoma.
CC -!- DOMAIN: The C-terminus of LRR N-terminal cap (LRRNT) and LRR 1 are
CC essential for the inhibition of the Wnt signaling pathway.
CC {ECO:0000269|PubMed:24582434}.
CC -!- PTM: Highly glycosylated. {ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:24582434}.
CC -!- MISCELLANEOUS: Antigen 5T4 is overexpressed by a wide spectrum of
CC cancers, including colorectal, ovarian and gastric, but with a limited
CC normal tissue expression. Could be used for tumor immunotherapy.
CC -!- MISCELLANEOUS: Reduction of TPBG levels by siRNA significantly enhanced
CC the beta-catenin/TCF transcription-based reporter pBAR activation in
CC response to Wnt stimulation.
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DR EMBL; Z29083; CAA82324.1; -; mRNA.
DR EMBL; AK291170; BAF83859.1; -; mRNA.
DR EMBL; AK074790; BAG52001.1; -; mRNA.
DR EMBL; CH471051; EAW48683.1; -; Genomic_DNA.
DR EMBL; AL121977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ012159; CAA09930.1; -; Genomic_DNA.
DR EMBL; BC037161; AAH37161.1; -; mRNA.
DR CCDS; CCDS4995.1; -.
DR PIR; A53531; A53531.
DR RefSeq; NP_001159864.1; NM_001166392.1.
DR RefSeq; NP_006661.1; NM_006670.4.
DR RefSeq; XP_011534399.1; XM_011536097.2.
DR PDB; 4CNC; X-ray; 1.77 A; A/B=60-345.
DR PDB; 4CNM; X-ray; 1.75 A; A=60-345.
DR PDB; 6HBY; X-ray; 1.95 A; C/F=112-130.
DR PDBsum; 4CNC; -.
DR PDBsum; 4CNM; -.
DR PDBsum; 6HBY; -.
DR AlphaFoldDB; Q13641; -.
DR SMR; Q13641; -.
DR BioGRID; 113015; 39.
DR IntAct; Q13641; 3.
DR MINT; Q13641; -.
DR STRING; 9606.ENSP00000358765; -.
DR ChEMBL; CHEMBL3712934; -.
DR GuidetoPHARMACOLOGY; 3009; -.
DR GlyConnect; 1860; 4 N-Linked glycans (2 sites).
DR GlyGen; Q13641; 6 sites, 4 N-linked glycans (2 sites), 2 O-linked glycans (2 sites).
DR iPTMnet; Q13641; -.
DR PhosphoSitePlus; Q13641; -.
DR SwissPalm; Q13641; -.
DR BioMuta; TPBG; -.
DR DMDM; 73621980; -.
DR EPD; Q13641; -.
DR jPOST; Q13641; -.
DR MassIVE; Q13641; -.
DR MaxQB; Q13641; -.
DR PaxDb; Q13641; -.
DR PeptideAtlas; Q13641; -.
DR PRIDE; Q13641; -.
DR ProteomicsDB; 59641; -.
DR ABCD; Q13641; 24 sequenced antibodies.
DR Antibodypedia; 2135; 295 antibodies from 32 providers.
DR DNASU; 7162; -.
DR Ensembl; ENST00000369750.4; ENSP00000358765.4; ENSG00000146242.9.
DR Ensembl; ENST00000535040.4; ENSP00000441219.1; ENSG00000146242.9.
DR Ensembl; ENST00000543496.3; ENSP00000440049.1; ENSG00000146242.9.
DR Ensembl; ENST00000634817.1; ENSP00000489447.1; ENSG00000283085.3.
DR Ensembl; ENST00000634826.1; ENSP00000489140.1; ENSG00000283085.3.
DR Ensembl; ENST00000635036.3; ENSP00000489143.1; ENSG00000283085.3.
DR GeneID; 7162; -.
DR KEGG; hsa:7162; -.
DR MANE-Select; ENST00000369750.4; ENSP00000358765.4; NM_001376922.1; NP_001363851.1.
DR UCSC; uc003pjn.5; human.
DR CTD; 7162; -.
DR DisGeNET; 7162; -.
DR GeneCards; TPBG; -.
DR HGNC; HGNC:12004; TPBG.
DR HPA; ENSG00000146242; Low tissue specificity.
DR MIM; 190920; gene.
DR neXtProt; NX_Q13641; -.
DR OpenTargets; ENSG00000146242; -.
DR PharmGKB; PA36685; -.
DR VEuPathDB; HostDB:ENSG00000146242; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154868; -.
DR HOGENOM; CLU_064866_0_0_1; -.
DR InParanoid; Q13641; -.
DR OMA; EDCPEVH; -.
DR OrthoDB; 785938at2759; -.
DR PhylomeDB; Q13641; -.
DR TreeFam; TF351115; -.
DR PathwayCommons; Q13641; -.
DR SignaLink; Q13641; -.
DR BioGRID-ORCS; 7162; 22 hits in 1069 CRISPR screens.
DR GeneWiki; TPBG; -.
DR GenomeRNAi; 7162; -.
DR Pharos; Q13641; Tbio.
DR PRO; PR:Q13641; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q13641; protein.
DR Bgee; ENSG00000146242; Expressed in lower esophagus muscularis layer and 96 other tissues.
DR Genevisible; Q13641; HS.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR GO; GO:0140059; P:dendrite arborization; IEA:Ensembl.
DR GO; GO:0090497; P:mesenchymal cell migration; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0008355; P:olfactory learning; IEA:Ensembl.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IEA:Ensembl.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; 2.
DR Pfam; PF01463; LRRCT; 1.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..420
FT /note="Trophoblast glycoprotein"
FT /id="PRO_0000019591"
FT TOPO_DOM 32..355
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 53..91
FT /note="LRRNT"
FT REPEAT 92..113
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:24582434"
FT REPEAT 116..139
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:24582434"
FT REPEAT 141..163
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:24582434"
FT REPEAT 172..204
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:24582434"
FT REPEAT 209..232
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:24582434"
FT REPEAT 233..255
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:24582434"
FT REPEAT 256..275
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:24582434"
FT DOMAIN 283..346
FT /note="LRRCT"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQV5"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..68
FT /evidence="ECO:0000269|PubMed:24582434"
FT DISULFID 66..77
FT /evidence="ECO:0000269|PubMed:24582434"
FT DISULFID 298..323
FT /evidence="ECO:0000269|PubMed:24582434"
FT DISULFID 300..344
FT /evidence="ECO:0000269|PubMed:24582434"
FT MUTAGEN 76
FT /note="K->A: Strongly reduces Wnt inhibitory function."
FT /evidence="ECO:0000269|PubMed:24582434"
FT MUTAGEN 97
FT /note="F->T: Strongly reduces Wnt inhibitory function."
FT /evidence="ECO:0000269|PubMed:24582434"
FT MUTAGEN 124
FT /note="N->Q: Impaired trafficking to the cell surface."
FT /evidence="ECO:0000269|PubMed:24582434"
FT MUTAGEN 214
FT /note="R->E: Impaired trafficking to the cell surface."
FT /evidence="ECO:0000269|PubMed:24582434"
FT MUTAGEN 325
FT /note="Y->A: Reduces Wnt inhibitory function."
FT /evidence="ECO:0000269|PubMed:24582434"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4CNM"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4CNM"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:4CNM"
FT TURN 135..140
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4CNM"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:4CNM"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:4CNC"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4CNM"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:4CNM"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:4CNM"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4CNM"
SQ SEQUENCE 420 AA; 46032 MW; 3C403211F40F18BC CRC64;
MPGGCSRGPA AGDGRLRLAR LALVLLGWVS SSSPTSSASS FSSSAPFLAS AVSAQPPLPD
QCPALCECSE AARTVKCVNR NLTEVPTDLP AYVRNLFLTG NQLAVLPAGA FARRPPLAEL
AALNLSGSRL DEVRAGAFEH LPSLRQLDLS HNPLADLSPF AFSGSNASVS APSPLVELIL
NHIVPPEDER QNRSFEGMVV AALLAGRALQ GLRRLELASN HFLYLPRDVL AQLPSLRHLD
LSNNSLVSLT YVSFRNLTHL ESLHLEDNAL KVLHNGTLAE LQGLPHIRVF LDNNPWVCDC
HMADMVTWLK ETEVVQGKDR LTCAYPEKMR NRVLLELNSA DLDCDPILPP SLQTSYVFLG
IVLALIGAIF LLVLYLNRKG IKKWMHNIRD ACRDHMEGYH YRYEINADPR LTNLSSNSDV
