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   27-MAR-2024, entry version 195.
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; 41.
DR   IntAct; Q13641; 4.
DR   MINT; Q13641; -.
DR   STRING; 9606.ENSP00000358765; -.
DR   ChEMBL; CHEMBL3712934; -.
DR   GuidetoPHARMACOLOGY; 3009; -.
DR   GlyConnect; 1860; 4 N-Linked glycans (2 sites).
DR   GlyCosmos; Q13641; 5 sites, 6 glycans.
DR   GlyGen; Q13641; 7 sites, 4 N-linked glycans (2 sites), 3 O-linked glycans (3 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; 9606-ENSP00000358765; -.
DR   PeptideAtlas; Q13641; -.
DR   ProteomicsDB; 59641; -.
DR   Pumba; Q13641; -.
DR   ABCD; Q13641; 24 sequenced antibodies.
DR   Antibodypedia; 2135; 370 antibodies from 33 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   AGR; HGNC:12004; -.
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; CTNAGLR; -.
DR   OrthoDB; 2968652at2759; -.
DR   PhylomeDB; Q13641; -.
DR   TreeFam; TF351115; -.
DR   PathwayCommons; Q13641; -.
DR   SignaLink; Q13641; -.
DR   BioGRID-ORCS; 7162; 23 hits in 1143 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 97 other cell types or tissues.
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: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 phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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; Ribonuclease Inhibitor; 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   PANTHER; PTHR24364; LP06937P; 1.
DR   PANTHER; PTHR24364:SF17; TROPHOBLAST GLYCOPROTEIN; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF01463; LRRCT; 1.
DR   Pfam; PF01462; LRRNT; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 5.
DR   Genevisible; Q13641; HS.
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
//