WLS_HUMAN
ID WLS_HUMAN Reviewed; 541 AA.
AC Q5T9L3; B2RNT2; Q5JRS7; Q7Z2Z9; Q8NC43;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein wntless homolog;
DE AltName: Full=Integral membrane protein GPR177;
DE AltName: Full=Protein evenness interrupted homolog;
DE Short=EVI;
DE AltName: Full=Putative NF-kappa-B-activating protein 373;
GN Name=WLS; Synonyms=C1orf139, GPR177; ORFNames=UNQ85/PRO18667;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH WNT3A.
RX PubMed=16678095; DOI=10.1016/j.cell.2006.02.049;
RA Baenziger C., Soldini D., Schuett C., Zipperlen P., Hausmann G., Basler K.;
RT "Wntless, a conserved membrane protein dedicated to the secretion of Wnt
RT proteins from signaling cells.";
RL Cell 125:509-522(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ILE-465.
RC TISSUE=Endometrium, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and PNS;
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 [8]
RP FUNCTION.
RX PubMed=16678096; DOI=10.1016/j.cell.2006.04.009;
RA Bartscherer K., Pelte N., Ingelfinger D., Boutros M.;
RT "Secretion of Wnt ligands requires Evi, a conserved transmembrane
RT protein.";
RL Cell 125:523-533(2006).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=18160347; DOI=10.1016/j.devcel.2007.12.004;
RA Yang P.T., Lorenowicz M.J., Silhankova M., Coudreuse D.Y., Betist M.C.,
RA Korswagen H.C.;
RT "Wnt signaling requires retromer-dependent recycling of MIG-14/Wntless in
RT Wnt-producing cells.";
RL Dev. Cell 14:140-147(2008).
RN [10]
RP GLYCOSYLATION, AND TOPOLOGY.
RX PubMed=20652957; DOI=10.1002/dvdy.22369;
RA Jin J., Morse M., Frey C., Petko J., Levenson R.;
RT "Expression of GPR177 (Wntless/Evi/Sprinter), a highly conserved Wnt-
RT transport protein, in rat tissues, zebrafish embryos, and cultured human
RT cells.";
RL Dev. Dyn. 239:2426-2434(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP VARIANTS ZKS CYS-392; CYS-478; THR-531 AND CYS-536, CHARACTERIZATION OF
RP VARIANTS ZKS CYS-392; CYS-478; THR-531 AND CYS-536, INVOLVEMENT IN ZKS, AND
RP FUNCTION.
RX PubMed=34587386; DOI=10.1056/nejmoa2033911;
RA Chai G., Szenker-Ravi E., Chung C., Li Z., Wang L., Khatoo M., Marshall T.,
RA Jiang N., Yang X., McEvoy-Venneri J., Stanley V., Anzenberg P., Lang N.,
RA Wazny V., Yu J., Virshup D.M., Nygaard R., Mancia F., Merdzanic R.,
RA Toralles M.B.P., Pitanga P.M.L., Puri R.D., Hernan R., Chung W.K.,
RA Bertoli-Avella A.M., Al-Sannaa N., Zaki M.S., Willert K., Reversade B.,
RA Gleeson J.G.;
RT "A human pleiotropic multiorgan condition caused by deficient Wnt
RT secretion.";
RL N. Engl. J. Med. 385:1292-1301(2021).
CC -!- FUNCTION: Regulates Wnt proteins sorting and secretion in a feedback
CC regulatory mechanism. This reciprocal interaction plays a key role in
CC the regulation of expression, subcellular location, binding and
CC organelle-specific association of Wnt proteins (PubMed:34587386). Plays
CC also an important role in establishment of the anterior-posterior body
CC axis formation during development (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16678095, ECO:0000269|PubMed:16678096,
CC ECO:0000269|PubMed:34587386}.
CC -!- SUBUNIT: Interacts with WNT3A. Interacts with WNT1, WNT3 and WNT5A (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q5T9L3; P35372: OPRM1; NbExp=11; IntAct=EBI-2868748, EBI-2624570;
CC Q5T9L3; Q01959: SLC6A3; NbExp=2; IntAct=EBI-2868748, EBI-6661445;
CC Q5T9L3; P56704: WNT3A; NbExp=4; IntAct=EBI-2868748, EBI-6173037;
CC Q5T9L3-1; P29274: ADORA2A; NbExp=3; IntAct=EBI-22114623, EBI-2902702;
CC Q5T9L3-1; P55087: AQP4; NbExp=3; IntAct=EBI-22114623, EBI-10104898;
CC Q5T9L3-1; Q9NPA0: EMC7; NbExp=3; IntAct=EBI-22114623, EBI-6309137;
CC Q5T9L3-1; P51674: GPM6A; NbExp=2; IntAct=EBI-22114623, EBI-7187133;
CC Q5T9L3-1; Q9BQI5: SGIP1; NbExp=3; IntAct=EBI-22114623, EBI-2690801;
CC Q5T9L3-1; Q5T9L3-1: WLS; NbExp=3; IntAct=EBI-22114623, EBI-22114623;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16678095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16678095}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:16678095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16678095}. Cell membrane
CC {ECO:0000269|PubMed:18160347}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18160347}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18160347};
CC Multi-pass membrane protein {ECO:0000255}. Early endosome membrane
CC {ECO:0000269|PubMed:18160347}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Co-localizes with the adaptin AP2A2 at distinct
CC punctae. {ECO:0000269|PubMed:18160347}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5T9L3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T9L3-2; Sequence=VSP_022346, VSP_022347;
CC Name=3;
CC IsoId=Q5T9L3-3; Sequence=VSP_046143;
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20652957}.
CC -!- DISEASE: Zaki syndrome (ZKS) [MIM:619648]: An autosomal recessive
CC disorder characterized by developmental delay, progressive
CC microcephaly, and short stature, as well as dysmorphic features
CC including sparse scalp hair, cupped ears, wide nose and mouth, short
CC philtrum, and high-arched palate. Other variable features have been
CC observed, including ocular, skeletal, cardiac, and renal anomalies.
CC {ECO:0000269|PubMed:34587386}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the wntless family. {ECO:0000305}.
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DR EMBL; DQ323735; ABD58927.1; -; mRNA.
DR EMBL; AY359035; AAQ89394.1; -; mRNA.
DR EMBL; AK074984; BAC11333.1; -; mRNA.
DR EMBL; BX538320; CAD98094.1; -; mRNA.
DR EMBL; BX648748; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL513284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06480.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06481.1; -; Genomic_DNA.
DR EMBL; BC110826; AAI10827.1; -; mRNA.
DR EMBL; BC137109; AAI37110.1; -; mRNA.
DR EMBL; BC137113; AAI37114.1; -; mRNA.
DR CCDS; CCDS30750.1; -. [Q5T9L3-2]
DR CCDS; CCDS53331.1; -. [Q5T9L3-3]
DR CCDS; CCDS642.1; -. [Q5T9L3-1]
DR RefSeq; NP_001002292.3; NM_001002292.3. [Q5T9L3-2]
DR RefSeq; NP_001180263.1; NM_001193334.1. [Q5T9L3-3]
DR RefSeq; NP_079187.3; NM_024911.6. [Q5T9L3-1]
DR PDB; 7DRT; EM; 2.20 A; B=1-541.
DR PDB; 7KC4; EM; 3.19 A; B=1-541.
DR PDBsum; 7DRT; -.
DR PDBsum; 7KC4; -.
DR AlphaFoldDB; Q5T9L3; -.
DR SMR; Q5T9L3; -.
DR BioGRID; 123038; 98.
DR IntAct; Q5T9L3; 78.
DR MINT; Q5T9L3; -.
DR STRING; 9606.ENSP00000346829; -.
DR TCDB; 8.A.56.1.2; the wntless protein (wls) family.
DR iPTMnet; Q5T9L3; -.
DR PhosphoSitePlus; Q5T9L3; -.
DR BioMuta; WLS; -.
DR DMDM; 122063496; -.
DR EPD; Q5T9L3; -.
DR jPOST; Q5T9L3; -.
DR MassIVE; Q5T9L3; -.
DR MaxQB; Q5T9L3; -.
DR PaxDb; Q5T9L3; -.
DR PeptideAtlas; Q5T9L3; -.
DR PRIDE; Q5T9L3; -.
DR ProteomicsDB; 63111; -.
DR ProteomicsDB; 64804; -. [Q5T9L3-1]
DR ProteomicsDB; 64805; -. [Q5T9L3-2]
DR Antibodypedia; 33415; 130 antibodies from 27 providers.
DR DNASU; 79971; -.
DR Ensembl; ENST00000262348.9; ENSP00000262348.4; ENSG00000116729.14. [Q5T9L3-1]
DR Ensembl; ENST00000354777.6; ENSP00000346829.2; ENSG00000116729.14. [Q5T9L3-2]
DR Ensembl; ENST00000370976.7; ENSP00000360015.3; ENSG00000116729.14. [Q5T9L3-3]
DR GeneID; 79971; -.
DR KEGG; hsa:79971; -.
DR MANE-Select; ENST00000262348.9; ENSP00000262348.4; NM_024911.7; NP_079187.3.
DR UCSC; uc001dee.4; human. [Q5T9L3-1]
DR CTD; 79971; -.
DR DisGeNET; 79971; -.
DR GeneCards; WLS; -.
DR HGNC; HGNC:30238; WLS.
DR HPA; ENSG00000116729; Low tissue specificity.
DR MIM; 611514; gene.
DR MIM; 619648; phenotype.
DR neXtProt; NX_Q5T9L3; -.
DR OpenTargets; ENSG00000116729; -.
DR PharmGKB; PA165752781; -.
DR VEuPathDB; HostDB:ENSG00000116729; -.
DR eggNOG; ENOG502QSE2; Eukaryota.
DR GeneTree; ENSGT00390000005897; -.
DR HOGENOM; CLU_022911_0_0_1; -.
DR InParanoid; Q5T9L3; -.
DR OMA; YWRHLSA; -.
DR OrthoDB; 418201at2759; -.
DR PhylomeDB; Q5T9L3; -.
DR TreeFam; TF105975; -.
DR PathwayCommons; Q5T9L3; -.
DR Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
DR SignaLink; Q5T9L3; -.
DR SIGNOR; Q5T9L3; -.
DR BioGRID-ORCS; 79971; 20 hits in 1076 CRISPR screens.
DR ChiTaRS; WLS; human.
DR GeneWiki; GPR177; -.
DR GenomeRNAi; 79971; -.
DR Pharos; Q5T9L3; Tbio.
DR PRO; PR:Q5T9L3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T9L3; protein.
DR Bgee; ENSG00000116729; Expressed in stromal cell of endometrium and 200 other tissues.
DR ExpressionAtlas; Q5T9L3; baseline and differential.
DR Genevisible; Q5T9L3; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:WormBase.
DR GO; GO:0070062; C:extracellular exosome; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000139; C:Golgi membrane; IDA:WormBase.
DR GO; GO:0031301; C:integral component of organelle membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005802; C:trans-Golgi network; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:WormBase.
DR GO; GO:0009948; P:anterior/posterior axis specification; ISS:UniProtKB.
DR GO; GO:0071529; P:cementum mineralization; IEA:Ensembl.
DR GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl.
DR GO; GO:0030902; P:hindbrain development; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IMP:ParkinsonsUK-UCL.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0061357; P:positive regulation of Wnt protein secretion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0061355; P:Wnt protein secretion; IMP:WormBase.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:UniProtKB.
DR InterPro; IPR009551; Wntless.
DR PANTHER; PTHR13449; PTHR13449; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW Developmental protein; Disease variant; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT CHAIN 1..541
FT /note="Protein wntless homolog"
FT /id="PRO_0000271777"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..232
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TRANSMEM 233..253
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TOPO_DOM 254..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TRANSMEM 269..289
FT /note="Helical; Name=3"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TOPO_DOM 290..303
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TRANSMEM 304..324
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TOPO_DOM 325..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TRANSMEM 332..352
FT /note="Helical; Name=5"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TOPO_DOM 353..380
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TRANSMEM 381..401
FT /note="Helical; Name=6"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TOPO_DOM 402..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TRANSMEM 432..452
FT /note="Helical; Name=7"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TOPO_DOM 453..471
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TRANSMEM 472..492
FT /note="Helical; Name=8"
FT /evidence="ECO:0000305|PubMed:20652957"
FT TOPO_DOM 493..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20652957"
FT REGION 101..232
FT /note="Interaction with Wnt proteins"
FT /evidence="ECO:0000250"
FT VAR_SEQ 36..127
FT /note="APGPTTAVSYMSVKCVDARKNHHKTKWFVPWGPNHCDKIRDIEEAIPREIEA
FT NDIVFSVHIPLPHMEMSPWFQFMLFILQLDIAFKLNNQIR -> G (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_046143"
FT VAR_SEQ 36..37
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_022346"
FT VAR_SEQ 507..541
FT /note="DLGVHSGEELQLTTTITHVDGPTEIYKLTRKEAQE -> MQLPCKSREDCAL
FT FVSELYQELFSASKYSFINDNAASGI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_022347"
FT VARIANT 392
FT /note="Y -> C (in ZKS; results in decreased secretion of
FT WNT3A and WNT5A; decreased activation of WNT signaling)"
FT /evidence="ECO:0000269|PubMed:34587386"
FT /id="VAR_086565"
FT VARIANT 465
FT /note="V -> I (in dbSNP:rs983034)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_029991"
FT VARIANT 478
FT /note="Y -> C (in ZKS; results in decreased secretion of
FT WNT3A and WNT5A; decreased activation of WNT signaling)"
FT /evidence="ECO:0000269|PubMed:34587386"
FT /id="VAR_086566"
FT VARIANT 531
FT /note="I -> T (in ZKS; results in decreased secretion of
FT WNT3A and WNT5A; decreased activation of WNT signaling)"
FT /evidence="ECO:0000269|PubMed:34587386"
FT /id="VAR_086567"
FT VARIANT 536
FT /note="R -> C (in ZKS; results in decreased secretion of
FT WNT3A and WNT5A; decreased activation of WNT signaling)"
FT /evidence="ECO:0000269|PubMed:34587386"
FT /id="VAR_086568"
FT CONFLICT 136
FT /note="V -> A (in Ref. 4; CAD98094)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 11..34
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:7DRT"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:7KC4"
FT STRAND 131..143
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:7KC4"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 215..226
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 228..257
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 265..281
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:7DRT"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 296..321
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 336..362
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 372..410
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 419..454
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:7DRT"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:7DRT"
FT HELIX 469..491
FT /evidence="ECO:0007829|PDB:7DRT"
SQ SEQUENCE 541 AA; 62253 MW; 0DAFDF51BBA0C288 CRC64;
MAGAIIENMS TKKLCIVGGI LLVFQIIAFL VGGLIAPGPT TAVSYMSVKC VDARKNHHKT
KWFVPWGPNH CDKIRDIEEA IPREIEANDI VFSVHIPLPH MEMSPWFQFM LFILQLDIAF
KLNNQIRENA EVSMDVSLAY RDDAFAEWTE MAHERVPRKL KCTFTSPKTP EHEGRYYECD
VLPFMEIGSV AHKFYLLNIR LPVNEKKKIN VGIGEIKDIR LVGIHQNGGF TKVWFAMKTF
LTPSIFIIMV WYWRRITMMS RPPVLLEKVI FALGISMTFI NIPVEWFSIG FDWTWMLLFG
DIRQGIFYAM LLSFWIIFCG EHMMDQHERN HIAGYWKQVG PIAVGSFCLF IFDMCERGVQ
LTNPFYSIWT TDIGTELAMA FIIVAGICLC LYFLFLCFMV FQVFRNISGK QSSLPAMSKV
RRLHYEGLIF RFKFLMLITL ACAAMTVIFF IVSQVTEGHW KWGGVTVQVN SAFFTGIYGM
WNLYVFALMF LYAPSHKNYG EDQSNGDLGV HSGEELQLTT TITHVDGPTE IYKLTRKEAQ
E
