WNT3A_MOUSE
ID WNT3A_MOUSE Reviewed; 352 AA.
AC P27467;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Protein Wnt-3a;
DE Flags: Precursor;
GN Name=Wnt3a; Synonyms=Wnt-3a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=2001840; DOI=10.1101/gad.5.3.381;
RA Roelink H., Nusse R.;
RT "Expression of two members of the Wnt family during mouse development
RT -- restricted temporal and spatial patterns in the developing neural
RT tube.";
RL Genes Dev. 5:381-388(1991).
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=8299937; DOI=10.1101/gad.8.2.174;
RA Takada S., Stark K.L., Shea M.J., Vassileva G., McMahon J.A., McMahon A.P.;
RT "Wnt-3a regulates somite and tailbud formation in the mouse embryo.";
RL Genes Dev. 8:174-189(1994).
RN [3]
RP INTERACTION WITH PORCN.
RX PubMed=10866835; DOI=10.1046/j.1432-1033.2000.01478.x;
RA Tanaka K., Okabayashi H., Asashima M., Perrimon N., Kadowaki T.;
RT "The evolutionarily conserved porcupine gene family is involved in the
RT processing of the Wnt family.";
RL Eur. J. Biochem. 267:4300-4311(2000).
RN [4]
RP PRELIMINARY CYSTEINE PALMITOYLATION.
RX PubMed=12717451; DOI=10.1038/nature01611;
RA Willert K., Brown J.D., Danenberg E., Duncan A.W., Weissman I.L., Reya T.,
RA Yates J.R. III, Nusse R.;
RT "Wnt proteins are lipid-modified and can act as stem cell growth factors.";
RL Nature 423:448-452(2003).
RN [5]
RP PROTEOLYTIC PROCESSING BY TIKI1 AND TIKI2, DISULFIDE BONDS, SUBUNIT, AND
RP MUTAGENESIS OF 25-SER-LEU-26; 33-SER-SER-34 AND CYS-77.
RX PubMed=22726442; DOI=10.1016/j.cell.2012.04.039;
RA Zhang X., Abreu J.G., Yokota C., Macdonald B.T., Singh S., Coburn K.L.,
RA Cheong S.M., Zhang M.M., Ye Q.Z., Hang H.C., Steen H., He X.;
RT "Tiki1 is required for head formation via Wnt cleavage-oxidation and
RT inactivation.";
RL Cell 149:1565-1577(2012).
RN [6]
RP PALMITOLEOYLATION AT SER-209, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-77;
RP SER-209; SER-211; THR-216; SER-277 AND THR-292, AND GLYCOSYLATION.
RX PubMed=17141155; DOI=10.1016/j.devcel.2006.10.003;
RA Takada R., Satomi Y., Kurata T., Ueno N., Norioka S., Kondoh H., Takao T.,
RA Takada S.;
RT "Monounsaturated fatty acid modification of Wnt protein: its role in Wnt
RT secretion.";
RL Dev. Cell 11:791-801(2006).
RN [7]
RP PALMITOLEOYLATION AT SER-209.
RX PubMed=24798332; DOI=10.1074/jbc.m114.561209;
RA Rios-Esteves J., Haugen B., Resh M.D.;
RT "Identification of key residues and regions important for porcupine-
RT mediated Wnt acylation.";
RL J. Biol. Chem. 289:17009-17019(2014).
RN [8]
RP SUBUNIT, PALMITOLEOYLATION AT SER-209, DEPALMITOLEOYLATION AT SER-209, AND
RP MUTAGENESIS OF SER-209.
RX PubMed=25771893; DOI=10.1016/j.devcel.2015.02.014;
RA Zhang X., Cheong S.M., Amado N.G., Reis A.H., MacDonald B.T., Zebisch M.,
RA Jones E.Y., Abreu J.G., He X.;
RT "Notum is required for neural and head induction via Wnt deacylation,
RT oxidation, and inactivation.";
RL Dev. Cell 32:719-730(2015).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AFM.
RX PubMed=26902720; DOI=10.7554/elife.11621;
RA Mihara E., Hirai H., Yamamoto H., Tamura-Kawakami K., Matano M.,
RA Kikuchi A., Sato T., Takagi J.;
RT "Active and water-soluble form of lipidated Wnt protein is maintained by a
RT serum glycoprotein afamin/alpha-albumin.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors (Probable). Functions in the canonical Wnt
CC signaling pathway that results in activation of transcription factors
CC of the TCF/LEF family (PubMed:26902720). Required for normal embryonic
CC mesoderm development and formation of caudal somites (PubMed:8299937).
CC Required for normal morphogenesis of the developing neural tube
CC (PubMed:8299937). Mediates self-renewal of the stem cells at the bottom
CC on intestinal crypts (in vitro) (PubMed:26902720).
CC {ECO:0000269|PubMed:26902720, ECO:0000269|PubMed:8299937, ECO:0000305}.
CC -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC oligomerization and is required for prolonged biological activity
CC (PubMed:26902720). The complex with AFM may represent the physiological
CC form in body fluids (PubMed:26902720). Homooligomer; disulfide-linked,
CC leading to inactivation (PubMed:25771893). Interacts with APCDD1 and
CC WLS. Component of the Wnt-Fzd-LRP5-LRP6 signaling complex that contains
CC a WNT protein, a FZD protein and LRP5 or LRP6. Interacts directly in
CC the complex with LRP6 (By similarity). Interacts with PORCN
CC (PubMed:10866835). Interacts with glypican GPC3 (By similarity).
CC Interacts with PKD1 (via extracellular domain) (By similarity).
CC {ECO:0000250|UniProtKB:P56704, ECO:0000269|PubMed:10866835,
CC ECO:0000269|PubMed:22726442, ECO:0000269|PubMed:25771893,
CC ECO:0000269|PubMed:26902720}.
CC -!- INTERACTION:
CC P27467; Q61091: Fzd8; NbExp=3; IntAct=EBI-2899665, EBI-6171689;
CC P27467; E9Q612: Ptpro; NbExp=2; IntAct=EBI-2899665, EBI-8183885;
CC P27467; G3MYZ3: AFM; Xeno; NbExp=3; IntAct=EBI-2899665, EBI-22052138;
CC P27467; P43652: AFM; Xeno; NbExp=3; IntAct=EBI-2899665, EBI-20737924;
CC P27467; O75581: LRP6; Xeno; NbExp=4; IntAct=EBI-2899665, EBI-910915;
CC P27467; A6NFA1: TRABD2B; Xeno; NbExp=2; IntAct=EBI-2899665, EBI-6257471;
CC P27467; Q9Y5W5: WIF1; Xeno; NbExp=8; IntAct=EBI-2899665, EBI-3922719;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:17141155,
CC ECO:0000269|PubMed:26902720}.
CC -!- TISSUE SPECIFICITY: Dorsal portion of the neural tube (developing roof
CC plate), and mesenchyme tissue surrounding the umbilical veins.
CC {ECO:0000269|PubMed:2001840}.
CC -!- DEVELOPMENTAL STAGE: Detected in the dorsal primitive streak region at
CC 8.5 dpc. Detected in the tailbud region and in the developing central
CC nervous system (CNS) at 9.5 dpc. {ECO:0000269|PubMed:8299937}.
CC -!- PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and
CC formation of large disulfide-bond oligomers, leading to inactivation of
CC WNT3A. {ECO:0000269|PubMed:22726442}.
CC -!- PTM: Disulfide bonds have critical and distinct roles in secretion and
CC activity. Loss of each conserved cysteine in WNT3A results in high
CC molecular weight oxidized Wnt oligomers, which are formed through
CC inter-Wnt disulfide bonding. {ECO:0000269|PubMed:22726442}.
CC -!- PTM: Palmitoleoylation by PORCN is required for efficient binding to
CC frizzled receptors. Palmitoleoylation is required for proper
CC trafficking to cell surface, vacuolar acidification is critical to
CC release palmitoleoylated WNT3A from WLS in secretory vesicles
CC (PubMed:17141155, PubMed:24798332). Depalmitoleoylated by NOTUM,
CC leading to inhibit Wnt signaling pathway, possibly by promoting
CC disulfide bond formation and oligomerization (PubMed:25771893).
CC {ECO:0000250|UniProtKB:P56704, ECO:0000269|PubMed:17141155,
CC ECO:0000269|PubMed:24798332, ECO:0000269|PubMed:25771893}.
CC -!- MISCELLANEOUS: Gene targeting that leads to the production of a
CC truncated mRNA causes full embryonic lethality at 10.5 to 12.5 dpc.
CC {ECO:0000269|PubMed:8299937}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC -!- CAUTION: The formation of disulfide-linked oligomers may be an artifact
CC that occurs upon heterologous expression in vitro (PubMed:25771893,
CC PubMed:26902720). Formation of disulfide-linked oligomers is not
CC observed when the protein is coexpressed with AFM (PubMed:26902720).
CC {ECO:0000269|PubMed:25771893, ECO:0000269|PubMed:26902720}.
CC -!- CAUTION: A palmitoylation site was proposed at Cys-77, but it was later
CC shown that this cysteine is engaged in a disulfide bond.
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DR EMBL; X56842; CAA40173.1; -; mRNA.
DR CCDS; CCDS24766.1; -.
DR PIR; A39532; A39532.
DR RefSeq; NP_033548.1; NM_009522.2.
DR AlphaFoldDB; P27467; -.
DR SMR; P27467; -.
DR BioGRID; 204575; 9.
DR CORUM; P27467; -.
DR DIP; DIP-55954N; -.
DR ELM; P27467; -.
DR IntAct; P27467; 11.
DR MINT; P27467; -.
DR STRING; 10090.ENSMUSP00000010044; -.
DR BindingDB; P27467; -.
DR ChEMBL; CHEMBL5617; -.
DR GlyGen; P27467; 2 sites.
DR PhosphoSitePlus; P27467; -.
DR SwissPalm; P27467; -.
DR MaxQB; P27467; -.
DR PaxDb; P27467; -.
DR PeptideAtlas; P27467; -.
DR PRIDE; P27467; -.
DR ProteomicsDB; 299996; -.
DR Antibodypedia; 34658; 607 antibodies from 36 providers.
DR DNASU; 22416; -.
DR Ensembl; ENSMUST00000010044; ENSMUSP00000010044; ENSMUSG00000009900.
DR GeneID; 22416; -.
DR KEGG; mmu:22416; -.
DR UCSC; uc007jdp.2; mouse.
DR CTD; 89780; -.
DR MGI; MGI:98956; Wnt3a.
DR VEuPathDB; HostDB:ENSMUSG00000009900; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000160510; -.
DR HOGENOM; CLU_033039_1_0_1; -.
DR InParanoid; P27467; -.
DR OMA; GLTHVMA; -.
DR OrthoDB; 965867at2759; -.
DR PhylomeDB; P27467; -.
DR TreeFam; TF105310; -.
DR Reactome; R-MMU-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-4641263; Regulation of FZD by ubiquitination.
DR BioGRID-ORCS; 22416; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Wnt3a; mouse.
DR PRO; PR:P27467; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P27467; protein.
DR Bgee; ENSMUSG00000009900; Expressed in urethra and 127 other tissues.
DR Genevisible; P27467; MM.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:1990909; C:Wnt signalosome; NAS:ParkinsonsUK-UCL.
DR GO; GO:1990851; C:Wnt-Frizzled-LRP5/6 complex; ISO:MGI.
DR GO; GO:0039706; F:co-receptor binding; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0048018; F:receptor ligand activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IDA:MGI.
DR GO; GO:0090245; P:axis elongation involved in somitogenesis; IGI:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0042100; P:B cell proliferation; IDA:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:MGI.
DR GO; GO:0090676; P:calcium ion transmembrane transport via low voltage-gated calcium channel; IDA:ParkinsonsUK-UCL.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0061317; P:canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment; ISO:MGI.
DR GO; GO:0060923; P:cardiac muscle cell fate commitment; IGI:MGI.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0021846; P:cell proliferation in forebrain; IDA:BHF-UCL.
DR GO; GO:0033278; P:cell proliferation in midbrain; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007267; P:cell-cell signaling; TAS:MGI.
DR GO; GO:0010387; P:COP9 signalosome assembly; IDA:BHF-UCL.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IDA:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IGI:MGI.
DR GO; GO:0030879; P:mammary gland development; IDA:MGI.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0030901; P:midbrain development; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0045445; P:myoblast differentiation; IGI:MGI.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IDA:MGI.
DR GO; GO:1904339; P:negative regulation of dopaminergic neuron differentiation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI.
DR GO; GO:0003136; P:negative regulation of heart induction by canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IDA:BHF-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; IGI:ARUK-UCL.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
DR GO; GO:0048343; P:paraxial mesodermal cell fate commitment; IMP:MGI.
DR GO; GO:0030168; P:platelet activation; IDA:MGI.
DR GO; GO:0070527; P:platelet aggregation; IDA:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:MGI.
DR GO; GO:2000081; P:positive regulation of canonical Wnt signaling pathway involved in controlling type B pancreatic cell proliferation; IDA:UniProtKB.
DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IDA:MGI.
DR GO; GO:0048697; P:positive regulation of collateral sprouting in absence of injury; IDA:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:MGI.
DR GO; GO:0061184; P:positive regulation of dermatome development; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IDA:MGI.
DR GO; GO:0048337; P:positive regulation of mesodermal cell fate specification; ISO:MGI.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IDA:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IGI:MGI.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISO:MGI.
DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IMP:CACAO.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0050770; P:regulation of axonogenesis; IGI:MGI.
DR GO; GO:0045595; P:regulation of cell differentiation; IDA:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IGI:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:2001141; P:regulation of RNA biosynthetic process; IDA:MGI.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR GO; GO:0062009; P:secondary palate development; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IGI:MGI.
DR GO; GO:0048103; P:somatic stem cell division; IDA:MGI.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR GO; GO:0021527; P:spinal cord association neuron differentiation; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:MGI.
DR GO; GO:0021874; P:Wnt signaling pathway involved in forebrain neuroblast division; IMP:MGI.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR009141; Wnt3.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01843; WNT3PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..352
FT /note="Protein Wnt-3a"
FT /id="PRO_0000041419"
FT SITE 26..27
FT /note="Cleavage; by TIKI1 and TIKI2"
FT /evidence="ECO:0000269|PubMed:22726442"
FT LIPID 209
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000269|PubMed:17141155,
FT ECO:0000269|PubMed:24798332, ECO:0000269|PubMed:25771893"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..88
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 128..136
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 138..155
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 203..217
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 205..212
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 281..312
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 297..307
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 311..351
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 327..342
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 329..339
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 334..335
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT MUTAGEN 25..26
FT /note="SL->DD: Partially resistant to proteolysis by TIKI1
FT and TIKI2. Completely resistant to proteolysis by TIKI1 and
FT TIKI2; when associated with 33-D-D-34."
FT /evidence="ECO:0000269|PubMed:22726442"
FT MUTAGEN 33..34
FT /note="SS->DD: Completely resistant to proteolysis by TIKI1
FT and TIKI2; when associated with 25-D-D-26."
FT /evidence="ECO:0000269|PubMed:22726442"
FT MUTAGEN 77
FT /note="C->A: Forms oxidized oligomers regardless of TIKI2.
FT Does not affect palmitoleoylation."
FT /evidence="ECO:0000269|PubMed:17141155,
FT ECO:0000269|PubMed:22726442"
FT MUTAGEN 209
FT /note="S->A: Abolishes palmitoleoylation, promoting
FT formation of disulfide bonds and oligomerization."
FT /evidence="ECO:0000269|PubMed:17141155,
FT ECO:0000269|PubMed:25771893"
FT MUTAGEN 211
FT /note="S->A: Does not affect palmitoleoylation."
FT /evidence="ECO:0000269|PubMed:17141155"
FT MUTAGEN 216
FT /note="T->A: Does not affect palmitoleoylation."
FT /evidence="ECO:0000269|PubMed:17141155"
FT MUTAGEN 277
FT /note="S->A: Does not affect palmitoleoylation."
FT /evidence="ECO:0000269|PubMed:17141155"
FT MUTAGEN 292
FT /note="T->A: Does not affect palmitoleoylation."
FT /evidence="ECO:0000269|PubMed:17141155"
SQ SEQUENCE 352 AA; 39258 MW; 7ADFC5B38A8EFF63 CRC64;
MAPLGYLLVL CSLKQALGSY PIWWSLAVGP QYSSLSTQPI LCASIPGLVP KQLRFCRNYV
EIMPSVAEGV KAGIQECQHQ FRGRRWNCTT VSNSLAIFGP VLDKATRESA FVHAIASAGV
AFAVTRSCAE GSAAICGCSS RLQGSPGEGW KWGGCSEDIE FGGMVSREFA DARENRPDAR
SAMNRHNNEA GRQAIASHMH LKCKCHGLSG SCEVKTCWWS QPDFRTIGDF LKDKYDSASE
MVVEKHRESR GWVETLRPRY TYFKVPTERD LVYYEASPNF CEPNPETGSF GTRDRTCNVS
SHGIDGCDLL CCGRGHNART ERRREKCHCV FHWCCYVSCQ ECTRVYDVHT CK
