FZD2_HUMAN
ID FZD2_HUMAN Reviewed; 565 AA.
AC Q14332; Q0VG82;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Frizzled-2;
DE Short=Fz-2;
DE Short=hFz2;
DE AltName: Full=FzE2;
DE Flags: Precursor;
GN Name=FZD2;
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].
RC TISSUE=Ovary;
RX PubMed=7558010; DOI=10.1006/geno.1995.1060;
RA Zhao Z., Lee C.C., Baldini A., Caskey C.T.;
RT "A human homologue of the Drosophila polarity gene frizzled has been
RT identified and mapped to 17q21.1.";
RL Genomics 27:370-373(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal lung;
RX PubMed=9813155; DOI=10.1006/bbrc.1998.9607;
RA Sagara N., Toda G., Hirai M., Terada M., Katoh M.;
RT "Molecular cloning, differential expression, and chromosomal localization
RT of human frizzled-1, frizzled-2, and frizzled-7.";
RL Biochem. Biophys. Res. Commun. 252:117-122(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 282-343.
RC TISSUE=Esophageal carcinoma;
RX PubMed=9707618; DOI=10.1073/pnas.95.17.10164;
RA Tanaka S., Akiyoshi T., Mori M., Wands J.R., Sugimachi K.;
RT "A novel frizzled gene identified in human esophageal carcinoma mediates
RT APC/beta-catenin signals.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10164-10169(1998).
RN [5]
RP FUNCTION, INVOLVEMENT IN OMOD2, VARIANT OMOD2 548-TRP--VAL-565 DEL, AND
RP CHARACTERIZATION OF VARIANT OMOD2 548-TRP--VAL-565 DEL.
RX PubMed=25759469; DOI=10.1093/hmg/ddv088;
RA Saal H.M., Prows C.A., Guerreiro I., Donlin M., Knudson L., Sund K.L.,
RA Chang C.F., Brugmann S.A., Stottmann R.W.;
RT "A mutation in FRIZZLED2 impairs Wnt signaling and causes autosomal
RT dominant omodysplasia.";
RL Hum. Mol. Genet. 24:3399-3409(2015).
RN [6]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH C.DIFFICILE TCDB
RP (MICROBIAL INFECTION).
RX PubMed=27680706; DOI=10.1038/nature19799;
RA Tao L., Zhang J., Meraner P., Tovaglieri A., Wu X., Gerhard R., Zhang X.,
RA Stallcup W.B., Miao J., He X., Hurdle J.G., Breault D.T., Brass A.L.,
RA Dong M.;
RT "Frizzled proteins are colonic epithelial receptors for C. difficile toxin
RT B.";
RL Nature 538:350-355(2016).
RN [7]
RP INTERACTION WITH C.DIFFICILE TCDB (MICROBIAL INFECTION).
RX PubMed=31233493; DOI=10.1371/journal.pbio.3000311;
RA Simeon R., Jiang M., Chamoun-Emanuelli A.M., Yu H., Zhang Y., Meng R.,
RA Peng Z., Jakana J., Zhang J., Feng H., Chen Z.;
RT "Selection and characterization of ultrahigh potency designed ankyrin
RT repeat protein inhibitors of C. difficile toxin B.";
RL PLoS Biol. 17:e3000311-e3000311(2019).
RN [8] {ECO:0007744|PDB:6C0B}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 34-156 IN COMPLEX WITH
RP C.DIFFICILE TCDB, DISULFIDE BONDS, GLYCOSYLATION AT ASN-53, FUNCTION
RP (MICROBIAL INFECTION), AND MUTAGENESIS OF TYR-77 AND LYS-127.
RX PubMed=29748286; DOI=10.1126/science.aar1999;
RA Chen P., Tao L., Wang T., Zhang J., He A., Lam K.H., Liu Z., He X.,
RA Perry K., Dong M., Jin R.;
RT "Structural basis for recognition of frizzled proteins by Clostridium
RT difficile toxin B.";
RL Science 360:664-669(2018).
RN [9]
RP VARIANT OMOD2 VAL-434.
RX PubMed=29230162; DOI=10.1159/000479721;
RA Tuerkmen S., Spielmann M., Guenes N., Knaus A., Floettmann R., Mundlos S.,
RA Tueysuez B.;
RT "A novel de novo FZD2 mutation in a patient with autosomal dominant
RT omodysplasia.";
RL Mol. Syndromol. 8:318-324(2017).
RN [10]
RP VARIANT OMOD2 547-SER--VAL-565 DEL.
RX PubMed=29383834; DOI=10.1002/ajmg.a.38623;
RA Nagasaki K., Nishimura G., Kikuchi T., Nyuzuki H., Sasaki S., Ogawa Y.,
RA Saitoh A.;
RT "Nonsense mutations in FZD2 cause autosomal-dominant omodysplasia: Robinow
RT syndrome-like phenotypes.";
RL Am. J. Med. Genet. A 176:739-742(2018).
RN [11]
RP INVOLVEMENT IN ROBINOW-LIKE SYNDROME, AND VARIANTS LEU-142;
RP 377-TRP--VAL-565 DEL; SER-434 AND VAL-434.
RX PubMed=29276006; DOI=10.1016/j.ajhg.2017.10.002;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA White J.J., Mazzeu J.F., Coban-Akdemir Z., Bayram Y., Bahrambeigi V.,
RA Hoischen A., van Bon B.W.M., Gezdirici A., Gulec E.Y., Ramond F.,
RA Touraine R., Thevenon J., Shinawi M., Beaver E., Heeley J., Hoover-Fong J.,
RA Durmaz C.D., Karabulut H.G., Marzioglu-Ozdemir E., Cayir A., Duz M.B.,
RA Seven M., Price S., Ferreira B.M., Vianna-Morgante A.M., Ellard S.,
RA Parrish A., Stals K., Flores-Daboub J., Jhangiani S.N., Gibbs R.A.,
RA Brunner H.G., Sutton V.R., Lupski J.R., Carvalho C.M.B.;
RT "WNT signaling perturbations underlie the genetic heterogeneity of Robinow
RT syndrome.";
RL Am. J. Hum. Genet. 102:27-43(2018).
RN [12]
RP VARIANTS OMOD2 VAL-434 AND 548-TRP--VAL-565 DEL.
RX PubMed=30455931; DOI=10.1002/ccr3.1818;
RA Warren H.E., Louie R.J., Friez M.J., Frias J.L., Leroy J.G., Spranger J.W.,
RA Skinner S.A., Champaigne N.L.;
RT "Two unrelated patients with autosomal dominant omodysplasia and FRIZZLED2
RT mutations.";
RL Clin. Case Rep. 6:2252-2255(2018).
CC -!- FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are
CC coupled to the beta-catenin canonical signaling pathway, which leads to
CC the activation of disheveled proteins, inhibition of GSK-3 kinase,
CC nuclear accumulation of beta-catenin and activation of Wnt target genes
CC (PubMed:25759469). A second signaling pathway involving PKC and calcium
CC fluxes has been seen for some family members, but it is not yet clear
CC if it represents a distinct pathway or if it can be integrated in the
CC canonical pathway, as PKC seems to be required for Wnt-mediated
CC inactivation of GSK-3 kinase. Both pathways seem to involve
CC interactions with G-proteins. May be involved in transduction and
CC intercellular transmission of polarity information during tissue
CC morphogenesis and/or in differentiated tissues.
CC {ECO:0000269|PubMed:25759469}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for C.difficile
CC toxin TcdB in the colonic epithelium (PubMed:27680706,
CC PubMed:29748286). TcdB occupies the binding site for Wnt-adducted
CC palmitoleate in frizzled receptors and TcdB-binding prevents Wnt-
CC binding and downstream Wnt signaling (PubMed:29748286).
CC {ECO:0000269|PubMed:27680706, ECO:0000269|PubMed:29748286}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.difficile toxin TcdB;
CC frizzled receptors constitute the major host receptors for TcdB in the
CC colonic epithelium. {ECO:0000269|PubMed:27680706,
CC ECO:0000269|PubMed:29748286, ECO:0000269|PubMed:31233493}.
CC -!- INTERACTION:
CC Q14332; P39688: Fyn; Xeno; NbExp=4; IntAct=EBI-6254477, EBI-524514;
CC Q14332; M4NKV9: tcdB; Xeno; NbExp=5; IntAct=EBI-6254477, EBI-20596828;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. In the adult, mainly found in
CC heart, placenta, skeletal muscle, lung, kidney, pancreas, prostate,
CC testis, ovary and colon. In the fetus, expressed in brain, lung and
CC kidney. Low levels in fetal liver.
CC -!- DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl
CC (Disheveled) family members and is involved in the activation of the
CC Wnt/beta-catenin signaling pathway. {ECO:0000250}.
CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by ZNRF3, leading to its degradation by the
CC proteasome. {ECO:0000250}.
CC -!- DISEASE: Omodysplasia 2 (OMOD2) [MIM:164745]: A rare autosomal dominant
CC skeletal dysplasia characterized by short humeri, radial head
CC dislocation, short first metacarpals, facial dysmorphism and
CC genitourinary anomalies. {ECO:0000269|PubMed:25759469,
CC ECO:0000269|PubMed:29230162, ECO:0000269|PubMed:29383834,
CC ECO:0000269|PubMed:30455931}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in FZD2 have been found in patients with Robinow
CC syndrome-like features including short-limb dwarfism, broad thumbs and
CC craniofacial abnormalities. {ECO:0000269|PubMed:29276006}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; L37882; AAB46397.1; -; mRNA.
DR EMBL; AB017364; BAA34667.1; -; mRNA.
DR EMBL; BC113402; AAI13403.1; -; mRNA.
DR EMBL; BC113404; AAI13405.1; -; mRNA.
DR CCDS; CCDS11484.1; -.
DR PIR; JE0338; JE0338.
DR RefSeq; NP_001457.1; NM_001466.3.
DR PDB; 6C0B; X-ray; 2.50 A; B=34-156.
DR PDB; 7N95; EM; 4.10 A; B=35-155.
DR PDB; 7N97; EM; 5.10 A; B=35-155.
DR PDB; 7N9S; EM; 5.10 A; B=35-155.
DR PDBsum; 6C0B; -.
DR PDBsum; 7N95; -.
DR PDBsum; 7N97; -.
DR PDBsum; 7N9S; -.
DR AlphaFoldDB; Q14332; -.
DR SMR; Q14332; -.
DR BioGRID; 108811; 68.
DR IntAct; Q14332; 18.
DR MINT; Q14332; -.
DR STRING; 9606.ENSP00000323901; -.
DR ChEMBL; CHEMBL3559686; -.
DR GuidetoPHARMACOLOGY; 230; -.
DR GlyGen; Q14332; 4 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q14332; -.
DR PhosphoSitePlus; Q14332; -.
DR BioMuta; FZD2; -.
DR DMDM; 17433019; -.
DR EPD; Q14332; -.
DR jPOST; Q14332; -.
DR MassIVE; Q14332; -.
DR MaxQB; Q14332; -.
DR PaxDb; Q14332; -.
DR PeptideAtlas; Q14332; -.
DR PRIDE; Q14332; -.
DR ProteomicsDB; 59968; -.
DR ABCD; Q14332; 36 sequenced antibodies.
DR Antibodypedia; 17503; 358 antibodies from 37 providers.
DR DNASU; 2535; -.
DR Ensembl; ENST00000315323.5; ENSP00000323901.3; ENSG00000180340.7.
DR GeneID; 2535; -.
DR KEGG; hsa:2535; -.
DR MANE-Select; ENST00000315323.5; ENSP00000323901.3; NM_001466.4; NP_001457.1.
DR UCSC; uc002igx.3; human.
DR CTD; 2535; -.
DR DisGeNET; 2535; -.
DR GeneCards; FZD2; -.
DR HGNC; HGNC:4040; FZD2.
DR HPA; ENSG00000180340; Tissue enhanced (choroid).
DR MalaCards; FZD2; -.
DR MIM; 164745; phenotype.
DR MIM; 600667; gene.
DR neXtProt; NX_Q14332; -.
DR OpenTargets; ENSG00000180340; -.
DR Orphanet; 93328; Autosomal dominant omodysplasia.
DR Orphanet; 3107; Autosomal dominant Robinow syndrome.
DR PharmGKB; PA28457; -.
DR VEuPathDB; HostDB:ENSG00000180340; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000161812; -.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; Q14332; -.
DR OMA; EIHFSRI; -.
DR OrthoDB; 330751at2759; -.
DR PhylomeDB; Q14332; -.
DR TreeFam; TF317907; -.
DR PathwayCommons; Q14332; -.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR SignaLink; Q14332; -.
DR SIGNOR; Q14332; -.
DR BioGRID-ORCS; 2535; 4 hits in 1063 CRISPR screens.
DR ChiTaRS; FZD2; human.
DR GeneWiki; FZD2; -.
DR GenomeRNAi; 2535; -.
DR Pharos; Q14332; Tbio.
DR PRO; PR:Q14332; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14332; protein.
DR Bgee; ENSG00000180340; Expressed in ventricular zone and 141 other tissues.
DR Genevisible; Q14332; HS.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0042813; F:Wnt receptor activity; IDA:WormBase.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0045446; P:endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0060022; P:hard palate development; IEA:Ensembl.
DR GO; GO:0060119; P:inner ear receptor cell development; IEA:Ensembl.
DR GO; GO:0003149; P:membranous septum morphogenesis; IEA:Ensembl.
DR GO; GO:0003150; P:muscular septum morphogenesis; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR CDD; cd07464; CRD_FZ2; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_TM.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR041778; FZ2_CRD.
DR InterPro; IPR026550; FZD1/2.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF34; PTHR11309:SF34; 1.
DR Pfam; PF01534; Frizzled; 1.
DR Pfam; PF01392; Fz; 1.
DR PRINTS; PR00489; FRIZZLED.
DR SMART; SM00063; FRI; 1.
DR SMART; SM01330; Frizzled; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Developmental protein; Disease variant;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Wnt signaling pathway.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..565
FT /note="Frizzled-2"
FT /id="PRO_0000012978"
FT TOPO_DOM 24..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..153
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 160..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 543..548
FT /note="Lys-Thr-X-X-X-Trp motif, mediates interaction with
FT the PDZ domain of Dvl family members"
FT /evidence="ECO:0000250"
FT MOTIF 563..565
FT /note="PDZ-binding"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29748286,
FT ECO:0007744|PDB:6C0B"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:29748286, ECO:0007744|PDB:6C0B"
FT DISULFID 47..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:29748286, ECO:0007744|PDB:6C0B"
FT DISULFID 84..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:29748286, ECO:0007744|PDB:6C0B"
FT DISULFID 110..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:29748286, ECO:0007744|PDB:6C0B"
FT DISULFID 114..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:29748286, ECO:0007744|PDB:6C0B"
FT VARIANT 142
FT /note="P -> L (found in a patient with features of Robinow
FT syndrome; unknown pathological significance;
FT dbSNP:rs759024435)"
FT /evidence="ECO:0000269|PubMed:29276006"
FT /id="VAR_083242"
FT VARIANT 377..565
FT /note="Missing (probable disease-associated variant found
FT in a patient with features of Robinow syndrome)"
FT /evidence="ECO:0000269|PubMed:29276006"
FT /id="VAR_083243"
FT VARIANT 434
FT /note="G -> S (probable disease-associated variant found in
FT a patient with features of Robinow syndrome;
FT dbSNP:rs1223920489)"
FT /evidence="ECO:0000269|PubMed:29276006"
FT /id="VAR_083244"
FT VARIANT 434
FT /note="G -> V (in OMOD2; also found in a patient with
FT features of Robinow syndrome; dbSNP:rs1555657073)"
FT /evidence="ECO:0000269|PubMed:29230162,
FT ECO:0000269|PubMed:29276006, ECO:0000269|PubMed:30455931"
FT /id="VAR_081993"
FT VARIANT 547..565
FT /note="Missing (in OMOD2)"
FT /evidence="ECO:0000269|PubMed:29383834"
FT /id="VAR_081994"
FT VARIANT 548..565
FT /note="Missing (in OMOD2; decreased Wnt signaling)"
FT /evidence="ECO:0000269|PubMed:25759469,
FT ECO:0000269|PubMed:30455931"
FT /id="VAR_081995"
FT MUTAGEN 77
FT /note="Y->A: Strongly reduced interaction with C.difficile
FT toxin TcdB."
FT /evidence="ECO:0000269|PubMed:29748286"
FT MUTAGEN 127
FT /note="K->A,E: Strongly reduced interaction with
FT C.difficile toxin TcdB."
FT /evidence="ECO:0000269|PubMed:29748286"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6C0B"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6C0B"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:6C0B"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:6C0B"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:6C0B"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:6C0B"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:6C0B"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:6C0B"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6C0B"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:6C0B"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:6C0B"
SQ SEQUENCE 565 AA; 63554 MW; AA387876A1DDE063 CRC64;
MRPRSALPRL LLPLLLLPAA GPAQFHGEKG ISIPDHGFCQ PISIPLCTDI AYNQTIMPNL
LGHTNQEDAG LEVHQFYPLV KVQCSPELRF FLCSMYAPVC TVLEQAIPPC RSICERARQG
CEALMNKFGF QWPERLRCEH FPRHGAEQIC VGQNHSEDGA PALLTTAPPP GLQPGAGGTP
GGPGGGGAPP RYATLEHPFH CPRVLKVPSY LSYKFLGERD CAAPCEPARP DGSMFFSQEE
TRFARLWILT WSVLCCASTF FTVTTYLVDM QRFRYPERPI IFLSGCYTMV SVAYIAGFVL
QERVVCNERF SEDGYRTVVQ GTKKEGCTIL FMMLYFFSMA SSIWWVILSL TWFLAAGMKW
GHEAIEANSQ YFHLAAWAVP AVKTITILAM GQIDGDLLSG VCFVGLNSLD PLRGFVLAPL
FVYLFIGTSF LLAGFVSLFR IRTIMKHDGT KTEKLERLMV RIGVFSVLYT VPATIVIACY
FYEQAFREHW ERSWVSQHCK SLAIPCPAHY TPRMSPDFTV YMIKYLMTLI VGITSGFWIW
SGKTLHSWRK FYTRLTNSRH GETTV
