ZNRF3_HUMAN
ID ZNRF3_HUMAN Reviewed; 936 AA.
AC Q9ULT6; B3KU18; Q6ICH1; Q6NTF8; Q8WU18;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=E3 ubiquitin-protein ligase ZNRF3;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 203;
DE AltName: Full=RING-type E3 ubiquitin transferase ZNRF3;
DE AltName: Full=Zinc/RING finger protein 3;
DE Flags: Precursor;
GN Name=ZNRF3; Synonyms=KIAA1133, RNF203;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-936 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 77-936 (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-936.
RC TISSUE=Brain, and 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 FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, INTERACTION WITH FZD4;
RP FZD5; FZD6; FZD8; LRP6 AND RSPO1, AND MUTAGENESIS OF PRO-103.
RX PubMed=22575959; DOI=10.1038/nature11019;
RA Hao H.X., Xie Y., Zhang Y., Charlat O., Oster E., Avello M., Lei H.,
RA Mickanin C., Liu D., Ruffner H., Mao X., Ma Q., Zamponi R., Bouwmeester T.,
RA Finan P.M., Kirschner M.W., Porter J.A., Serluca F.C., Cong F.;
RT "ZNRF3 promotes Wnt receptor turnover in an R-spondin-sensitive manner.";
RL Nature 485:195-200(2012).
RN [8]
RP INTERACTION WITH RSPO2.
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).
RN [9]
RP INTERACTION WITH LMBR1L.
RX PubMed=31073040; DOI=10.1126/science.aau0812;
RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J.,
RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M.,
RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y.,
RA Beutler B.;
RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.";
RL Science 364:0-0(2019).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator
CC of the Wnt signaling pathway by mediating the ubiquitination and
CC subsequent degradation of Wnt receptor complex components Frizzled and
CC LRP6. Acts on both canonical and non-canonical Wnt signaling pathway.
CC Acts as a tumor suppressor in the intestinal stem cell zone by
CC inhibiting the Wnt signaling pathway, thereby resticting the size of
CC the intestinal stem cell zone (PubMed:22575959). Along with RSPO2 and
CC RNF43, constitutes a master switch that governs limb specification (By
CC similarity). {ECO:0000250|UniProtKB:Q08D68,
CC ECO:0000269|PubMed:22575959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- ACTIVITY REGULATION: Negatively regulated by R-spondin proteins such as
CC RSPO1: interaction with RSPO1 induces the indirect association between
CC ZNRF3 and LGR4, promoting membrane clearance of ZNRF3.
CC {ECO:0000269|PubMed:22575959}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with LRP6, FZD4, FZD5, FZD6 and FZD8
CC (PubMed:22575959). Interacts with RSPO1; interaction promotes indirect
CC interaction with LGR4 and membrane clearance of ZNRF3
CC (PubMed:22575959). Also interacts with RSPO2 (PubMed:29769720).
CC Interacts with LMBR1L (PubMed:31073040). {ECO:0000269|PubMed:22575959,
CC ECO:0000269|PubMed:29769720, ECO:0000305|PubMed:31073040}.
CC -!- INTERACTION:
CC Q9ULT6; O60353: FZD6; NbExp=2; IntAct=EBI-949772, EBI-8754490;
CC Q9ULT6; Q9BXB1: LGR4; NbExp=2; IntAct=EBI-949772, EBI-10965764;
CC Q9ULT6; O75581: LRP6; NbExp=2; IntAct=EBI-949772, EBI-910915;
CC Q9ULT6; Q2MKA7: RSPO1; NbExp=6; IntAct=EBI-949772, EBI-10045219;
CC Q9ULT6; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-949772, EBI-10243654;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22575959};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULT6-2; Sequence=VSP_044043;
CC -!- SIMILARITY: Belongs to the ZNRF3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG30283.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK096397; BAG53280.1; -; mRNA.
DR EMBL; Z95113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL021393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB051436; BAB33319.1; -; mRNA.
DR EMBL; CR456397; CAG30283.1; ALT_INIT; mRNA.
DR EMBL; BC021570; AAH21570.1; -; mRNA.
DR EMBL; BC069019; AAH69019.1; -; mRNA.
DR EMBL; BC094857; AAH94857.1; -; mRNA.
DR CCDS; CCDS42999.1; -. [Q9ULT6-2]
DR CCDS; CCDS56225.1; -. [Q9ULT6-1]
DR RefSeq; NP_001193927.1; NM_001206998.1. [Q9ULT6-1]
DR RefSeq; NP_115549.2; NM_032173.3. [Q9ULT6-2]
DR AlphaFoldDB; Q9ULT6; -.
DR SMR; Q9ULT6; -.
DR BioGRID; 123905; 32.
DR DIP; DIP-50030N; -.
DR IntAct; Q9ULT6; 12.
DR MINT; Q9ULT6; -.
DR STRING; 9606.ENSP00000443824; -.
DR iPTMnet; Q9ULT6; -.
DR PhosphoSitePlus; Q9ULT6; -.
DR BioMuta; ZNRF3; -.
DR DMDM; 126253847; -.
DR EPD; Q9ULT6; -.
DR jPOST; Q9ULT6; -.
DR MassIVE; Q9ULT6; -.
DR PaxDb; Q9ULT6; -.
DR PeptideAtlas; Q9ULT6; -.
DR PRIDE; Q9ULT6; -.
DR ProteomicsDB; 85106; -. [Q9ULT6-1]
DR ProteomicsDB; 85107; -. [Q9ULT6-2]
DR ABCD; Q9ULT6; 8 sequenced antibodies.
DR Antibodypedia; 48546; 84 antibodies from 14 providers.
DR DNASU; 84133; -.
DR Ensembl; ENST00000402174.5; ENSP00000384456.1; ENSG00000183579.16. [Q9ULT6-2]
DR Ensembl; ENST00000406323.3; ENSP00000384553.3; ENSG00000183579.16. [Q9ULT6-2]
DR Ensembl; ENST00000544604.7; ENSP00000443824.2; ENSG00000183579.16. [Q9ULT6-1]
DR GeneID; 84133; -.
DR KEGG; hsa:84133; -.
DR MANE-Select; ENST00000544604.7; ENSP00000443824.2; NM_001206998.2; NP_001193927.1.
DR UCSC; uc003aeg.4; human. [Q9ULT6-1]
DR CTD; 84133; -.
DR DisGeNET; 84133; -.
DR GeneCards; ZNRF3; -.
DR HGNC; HGNC:18126; ZNRF3.
DR HPA; ENSG00000183579; Low tissue specificity.
DR MIM; 612062; gene.
DR neXtProt; NX_Q9ULT6; -.
DR OpenTargets; ENSG00000183579; -.
DR PharmGKB; PA134983897; -.
DR VEuPathDB; HostDB:ENSG00000183579; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000154006; -.
DR HOGENOM; CLU_018099_1_0_1; -.
DR InParanoid; Q9ULT6; -.
DR OMA; CGPTGGE; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q9ULT6; -.
DR TreeFam; TF317074; -.
DR PathwayCommons; Q9ULT6; -.
DR Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
DR SignaLink; Q9ULT6; -.
DR SIGNOR; Q9ULT6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 84133; 13 hits in 1123 CRISPR screens.
DR ChiTaRS; ZNRF3; human.
DR GenomeRNAi; 84133; -.
DR Pharos; Q9ULT6; Tbio.
DR PRO; PR:Q9ULT6; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9ULT6; protein.
DR Bgee; ENSG00000183579; Expressed in corpus epididymis and 175 other tissues.
DR ExpressionAtlas; Q9ULT6; baseline and differential.
DR Genevisible; Q9ULT6; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0060173; P:limb development; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:2000051; P:negative regulation of non-canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:2000095; P:regulation of Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0038018; P:Wnt receptor catabolic process; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd16799; RING-H2_ZNRF3; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR040700; ZNRF-3_ecto.
DR InterPro; IPR045903; ZNRF3_Znf_RING.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF18212; ZNRF_3_ecto; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Developmental protein; Membrane;
KW Metal-binding; Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Wnt signaling pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..55
FT /evidence="ECO:0000255"
FT CHAIN 56..936
FT /note="E3 ubiquitin-protein ligase ZNRF3"
FT /id="PRO_0000277806"
FT TOPO_DOM 56..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..936
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 293..334
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..27
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044043"
FT MUTAGEN 103
FT /note="P->A: Abolishes interaction with RSPO1 and prevents
FT subsequent membrane clearance."
FT /evidence="ECO:0000269|PubMed:22575959"
SQ SEQUENCE 936 AA; 100574 MW; EE68B810BD3C9C74 CRC64;
MRPRSGGRPG ATGRRRRRLR RRPRGLRCSR LPPPPPLPLL LGLLLAAAGP GAARAKETAF
VEVVLFESSP SGDYTTYTTG LTGRFSRAGA TLSAEGEIVQ MHPLGLCNNN DEEDLYEYGW
VGVVKLEQPE LDPKPCLTVL GKAKRAVQRG ATAVIFDVSE NPEAIDQLNQ GSEDPLKRPV
VYVKGADAIK LMNIVNKQKV ARARIQHRPP RQPTEYFDMG IFLAFFVVVS LVCLILLVKI
KLKQRRSQNS MNRLAVQALE KMETRKFNSK SKGRREGSCG ALDTLSSSST SDCAICLEKY
IDGEELRVIP CTHRFHRKCV DPWLLQHHTC PHCRHNIIEQ KGNPSAVCVE TSNLSRGRQQ
RVTLPVHYPG RVHRTNAIPA YPTRTSMDSH GNPVTLLTMD RHGEQSLYSP QTPAYIRSYP
PLHLDHSLAA HRCGLEHRAY SPAHPFRRPK LSGRSFSKAA CFSQYETMYQ HYYFQGLSYP
EQEGQSPPSL APRGPARAFP PSGSGSLLFP TVVHVAPPSH LESGSTSSFS CYHGHRSVCS
GYLADCPGSD SSSSSSSGQC HCSSSDSVVD CTEVSNQGVY GSCSTFRSSL SSDYDPFIYR
SRSPCRASEA GGSGSSGRGP ALCFEGSPPP EELPAVHSHG AGRGEPWPGP ASPSGDQVST
CSLEMNYSSN SSLEHRGPNS STSEVGLEAS PGAAPDLRRT WKGGHELPSC ACCCEPQPSP
AGPSAGAAGS STLFLGPHLY EGSGPAGGEP QSGSSQGLYG LHPDHLPRTD GVKYEGLPCC
FYEEKQVARG GGGGSGCYTE DYSVSVQYTL TEEPPPGCYP GARDLSQRIP IIPEDVDCDL
GLPSDCQGTH SLGSWGGTRG PDTPRPHRGL GATREEERAL CCQARALLRP GCPPEEAGAV
RANFPSALQD TQESSTTATE AAGPRSHSAD SSSPGA
