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FZD3_MOUSE
ID   FZD3_MOUSE              Reviewed;         666 AA.
AC   Q61086;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=Frizzled-3;
DE            Short=Fz-3;
DE            Short=mFz3;
DE   Flags: Precursor;
GN   Name=Fzd3;
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.
RX   PubMed=8626800; DOI=10.1074/jbc.271.8.4468;
RA   Wang Y., Macke J.P., Abella B.S., Andreasson K., Worley P., Gilbert D.J.,
RA   Copeland N.G., Jenkins N.A., Nathans J.;
RT   "A large family of putative transmembrane receptors homologous to the
RT   product of the Drosophila tissue polarity gene frizzled.";
RL   J. Biol. Chem. 271:4468-4476(1996).
RN   [2]
RP   WNT-MEDIATED PKC ACTIVATION.
RX   PubMed=10395542; DOI=10.1016/s0960-9822(99)80310-8;
RA   Sheldahl L.C., Park M., Malbon C.C., Moon R.T.;
RT   "Protein kinase C is differentially stimulated by Wnt and Frizzled homologs
RT   in a G-protein-dependent manner.";
RL   Curr. Biol. 9:695-698(1999).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11407985; DOI=10.1046/j.1523-1747.2001.01336.x;
RA   Hung B.S., Wang X.-Q., Cam G.R., Rothnagel J.A.;
RT   "Characterization of mouse frizzled-3 expression in hair follicle
RT   development and identification of the human homolog in keratinocytes.";
RL   J. Invest. Dermatol. 116:940-946(2001).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=12351730; DOI=10.1523/jneurosci.22-19-08563.2002;
RA   Wang Y., Thekdi N., Smallwood P.M., Macke J.P., Nathans J.;
RT   "Frizzled-3 is required for the development of major fiber tracts in the
RT   rostral CNS.";
RL   J. Neurosci. 22:8563-8573(2002).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=14671310; DOI=10.1126/science.1089610;
RA   Lyuksyutova A.I., Lu C.C., Milanesio N., King L.A., Gu o N., Wang Y.,
RA   Nathans J., Tessier-Lavigne M., Zou Y.;
RT   "Anterior-posterior guidance of commissural axons by Wnt-frizzled
RT   signaling.";
RL   Science 302:1984-1988(2003).
RN   [6]
RP   FUNCTION.
RX   PubMed=16407530; DOI=10.1523/jneurosci.3221-05.2006;
RA   Wang Y., Zhang J., Mori S., Nathans J.;
RT   "Axonal growth and guidance defects in Frizzled3 knock-out mice: a
RT   comparison of diffusion tensor magnetic resonance imaging, neurofilament
RT   staining, and genetically directed cell labeling.";
RL   J. Neurosci. 26:355-364(2006).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16495441; DOI=10.1523/jneurosci.4698-05.2005;
RA   Wang Y., Guo N., Nathans J.;
RT   "The role of Frizzled3 and Frizzled6 in neural tube closure and in the
RT   planar polarity of inner-ear sensory hair cells.";
RL   J. Neurosci. 26:2147-2156(2006).
RN   [8]
RP   INTERACTION WITH VANGL2.
RX   PubMed=16687519; DOI=10.1523/jneurosci.4680-05.2006;
RA   Montcouquiol M., Sans N., Huss D., Kach J., Dickman J.D., Forge A.,
RA   Rachel R.A., Copeland N.G., Jenkins N.A., Bogani D., Murdoch J.,
RA   Warchol M.E., Wenthold R.J., Kelley M.W.;
RT   "Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms for
RT   planar cell polarity in mammals.";
RL   J. Neurosci. 26:5265-5275(2006).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=21325504; DOI=10.1523/jneurosci.4243-10.2011;
RA   Armstrong A., Ryu Y.K., Chieco D., Kuruvilla R.;
RT   "Frizzled3 is required for neurogenesis and target innervation during
RT   sympathetic nervous system development.";
RL   J. Neurosci. 31:2371-2381(2011).
RN   [10]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND CONDITIONAL KNOCKOUTS.
RX   PubMed=24347548; DOI=10.7554/elife.01482;
RA   Hua Z.L., Smallwood P.M., Nathans J.;
RT   "Frizzled3 controls axonal development in distinct populations of cranial
RT   and spinal motor neurons.";
RL   Elife 2:E01482-E01482(2013).
RN   [11]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND CONDITIONAL KNOCKOUTS.
RX   PubMed=24799694; DOI=10.1073/pnas.1406399111;
RA   Hua Z.L., Jeon S., Caterina M.J., Nathans J.;
RT   "Frizzled3 is required for the development of multiple axon tracts in the
RT   mouse central nervous system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:E3005-E3005(2014).
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
CC       genes. A second signaling pathway involving PKC and calcium fluxes has
CC       been seen for some family members, but it is not yet clear if it
CC       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. Activation by Wnt5A stimulates PKC
CC       activity via a G-protein-dependent mechanism. Involved in transduction
CC       and intercellular transmission of polarity information during tissue
CC       morphogenesis and/or in differentiated tissues. Plays a role in
CC       controlling early axon growth and guidance processes necessary for the
CC       formation of a subset of central and peripheral major fiber tracts.
CC       Required for the development of major fiber tracts in the central
CC       nervous system, including: the anterior commissure, the corpus
CC       callosum, the thalamocortical, corticothalamic and nigrostriatal
CC       tracts, the corticospinal tract, the fasciculus retroflexus, the
CC       mammillothalamic tract, the medial lemniscus, and ascending fiber
CC       tracts from the spinal cord to the brain. In the peripheral nervous
CC       system, controls axon growth in distinct populations of cranial and
CC       spinal motor neurons, including the facial branchimotor nerve, the
CC       hypoglossal nerve, the phrenic nerve, and motor nerves innervating
CC       dorsal limbs. Involved in the migration of cranial neural crest cells.
CC       May also be implicated in the transmission of sensory information from
CC       the trunk and limbs to the brain. Controls commissural sensory axons
CC       guidance after midline crossing along the anterior-posterior axis in
CC       the developing spinal cord in a Wnt-dependent signaling pathway.
CC       Together with FZD6, is involved in the neural tube closure and plays a
CC       role in the regulation of the establishment of planar cell polarity
CC       (PCP), particularly in the orientation of asymmetric bundles of
CC       stereocilia on the apical faces of a subset of auditory and vestibular
CC       sensory cells located in the inner ear. Promotes neurogenesis by
CC       maintaining sympathetic neuroblasts within the cell cycle in a beta-
CC       catenin-dependent manner. {ECO:0000269|PubMed:12351730,
CC       ECO:0000269|PubMed:14671310, ECO:0000269|PubMed:16407530,
CC       ECO:0000269|PubMed:16495441, ECO:0000269|PubMed:21325504,
CC       ECO:0000269|PubMed:24347548, ECO:0000269|PubMed:24799694}.
CC   -!- SUBUNIT: Interacts with VANGL2. {ECO:0000269|PubMed:16687519}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC       membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
CC       surface {ECO:0000269|PubMed:16495441}. Apical cell membrane
CC       {ECO:0000269|PubMed:16495441}; Multi-pass membrane protein.
CC       Note=Colocalizes with FZD6 at the apical face of the cell.
CC       {ECO:0000269|PubMed:16495441}.
CC   -!- TISSUE SPECIFICITY: Expressed in the cortex, diencephalon, rostral
CC       brainstem and little or no staining is seen in the striatum or
CC       cerebellum. Expressed in both hair cells and supporting cells in the
CC       utricle, saccule, cristae and the organ of Corti in the inner ear (at
CC       protein level). Highly expressed in the CNS. In skin, it is restricted
CC       to the epidermis and to the developing hair follicle.
CC       {ECO:0000269|PubMed:11407985, ECO:0000269|PubMed:12351730,
CC       ECO:0000269|PubMed:16495441, ECO:0000269|PubMed:8626800}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the developing central
CC       nervous system (CNS). Expressed in the cortex, diencephalon, and
CC       brainstem, with the most intense staining in the striatum and
CC       trigeminal ganglia at 18 dpc (at protein level). First detected in
CC       discrete foci in the developing epidermis of 13 days old embryos, later
CC       in the hair follicle placodes of 15 days old embryos. Expressed in the
CC       ventral and lateral margins of the spinal cord from 9.5 to 13.5 dpc,
CC       where post-crossing commissural axons project longitudinally. Expressed
CC       in superior sympathetic cervical ganglia (SCG) at 14.5 and 16.5 dpc, a
CC       stage when the SCG is comprised primarily of proliferating sympathetic
CC       neuroblasts. In 17 days embryos and 1 day old newborn, expression is
CC       limited to suprabasal keratinocytes and is not seen in pelage follicles
CC       until 3 days postpartum. In 7 days old neonatal skin, expression occurs
CC       throughout the epidermis and in the outer cell layers of hair
CC       follicles. {ECO:0000269|PubMed:11407985, ECO:0000269|PubMed:12351730,
CC       ECO:0000269|PubMed:14671310, ECO:0000269|PubMed:21325504}.
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   -!- DISRUPTION PHENOTYPE: Neonate knockout mice have a curly tail, flexed
CC       lower limbs, breathe irregularly and typically die within 30 min of
CC       birth. Central nervous system (CNS) shows severe defects in the
CC       development of several major axon tracts, including: a nearly complete
CC       absence of the three early most prominent axon tracts in the brain and
CC       the ventral branch of the trigeminal nerve, absence of subcortical and
CC       striatal axons, the anterior commissure, misrouting of thalamocortical
CC       axons, a nearly complete absence of the corticospinal tract, the
CC       fasciculus retroflexus, and the mammillothalamic tract, poor
CC       fasciculation of the medial lemniscus and a disorganization of axon
CC       bundles in the reticular formation, severe defect in the asymmetric
CC       rostrocaudal orientation of dopaminergic and serotonergic axons, a
CC       large reduction or complete absence of ascending spinal axon tracts in
CC       the braistem, midbrain and thalamus, peripheral nerves defect in
CC       several motor neurons, such as in the VIIth and XIIth cranial motor
CC       nerves, the phrenic nerve, and the spinal motor nerve which failed to
CC       form connections with their respective targets and display also
CC       aberrant migration of a subpopulation of cranial neural crest cells
CC       (PubMed:12351730, PubMed:24347548, PubMed:24799694). Neonate knockout
CC       mice show fewer S-phase proliferating neuroblasts, premature cell cycle
CC       exit and enhanced apoptosis in early-stage superior cervical ganglia
CC       (SCGs), and in some cases, complete absence of sympathetic innervation
CC       of several peripheral targets (PubMed:21325504). Display also impaired
CC       rostral turning by growth cones of spinal cord commissural sensory
CC       axons (PubMed:14671310). FZD3 and FZD6 double knockout embryos have a
CC       curled tail, exhibit defects in neural tube and eyelids closure, in the
CC       orientation of hair bundles on inner-ear sensory cells and die at birth
CC       (PubMed:16495441). The following conditional knockout mice display the
CC       corresponding phenotypes: dopaminergic neuron-specific shows a defect
CC       in the orientation and growth of midbrain dopaminergic axons with an
CC       absence of striatum innervation; retinal ganglion cell (RGC)-specific
CC       displays a misrouting of a subset of optic tract axons and a lack of
CC       the medial terminal nucleus (MTN) innervation; neocortex neuron-
CC       specific displays a total absence of the posterior part of the anterior
CC       commissure and aberrant axon trajectories appearing in the external
CC       capsule; ventral telencephalon neuron-specific shows corticothalamic,
CC       thalamocortical and corticospinal tracts defect to various extent;
CC       telencephalon neuron-specific exhibits the full spectrum of axon
CC       defects seen in the classical null mutant knockout mice; cholinergic
CC       neuron-specific shows an absence of cholinergic fiber tracts passing
CC       through the striatum, a defective caudal migration of neurons of the
CC       VIIth motor nucleus and a loss of motor innervation to the face, a
CC       decrease in motor innervation of the tongue by the XIIth nerve and a
CC       complete loss of cholinergic neurons in the vomeronasal organ;
CC       oligodendrocyte neuron-specific leads to the complete spectrum of motor
CC       neuron phenotypes shown by the classical mutant knockout mice; caudal
CC       and upper thorax region-specific leads to a loss of motor innervation
CC       and an atrophy of anterior compartment muscles in the lower hindlimb by
CC       the deep peroneal nerve and a nearly absence in ascending spinal
CC       sensory axons in the brainstem, midbrain and thalamus altering the
CC       ability to transmit sensory information from the trunk and limbs to the
CC       brain in postnatal life (PubMed:24347548, PubMed:24799694).
CC       {ECO:0000269|PubMed:12351730, ECO:0000269|PubMed:14671310,
CC       ECO:0000269|PubMed:16495441, ECO:0000269|PubMed:21325504,
CC       ECO:0000269|PubMed:24347548, ECO:0000269|PubMed:24799694}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC       {ECO:0000305}.
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DR   EMBL; U43205; AAC52429.1; -; mRNA.
DR   CCDS; CCDS27212.1; -.
DR   RefSeq; NP_067433.1; NM_021458.2.
DR   AlphaFoldDB; Q61086; -.
DR   SMR; Q61086; -.
DR   BioGRID; 199776; 1.
DR   STRING; 10090.ENSMUSP00000115325; -.
DR   GlyGen; Q61086; 3 sites.
DR   iPTMnet; Q61086; -.
DR   PhosphoSitePlus; Q61086; -.
DR   SwissPalm; Q61086; -.
DR   MaxQB; Q61086; -.
DR   PaxDb; Q61086; -.
DR   PRIDE; Q61086; -.
DR   ProteomicsDB; 272925; -.
DR   Antibodypedia; 10432; 461 antibodies from 35 providers.
DR   DNASU; 14365; -.
DR   Ensembl; ENSMUST00000131309; ENSMUSP00000115325; ENSMUSG00000007989.
DR   GeneID; 14365; -.
DR   KEGG; mmu:14365; -.
DR   UCSC; uc007ujb.2; mouse.
DR   CTD; 7976; -.
DR   MGI; MGI:108476; Fzd3.
DR   VEuPathDB; HostDB:ENSMUSG00000007989; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   GeneTree; ENSGT00940000156491; -.
DR   HOGENOM; CLU_007873_4_1_1; -.
DR   InParanoid; Q61086; -.
DR   OMA; WIVFYLW; -.
DR   OrthoDB; 330751at2759; -.
DR   PhylomeDB; Q61086; -.
DR   TreeFam; TF317907; -.
DR   Reactome; R-MMU-4086398; Ca2+ pathway.
DR   Reactome; R-MMU-4086400; PCP/CE pathway.
DR   Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR   BioGRID-ORCS; 14365; 4 hits in 71 CRISPR screens.
DR   ChiTaRS; Fzd3; mouse.
DR   PRO; PR:Q61086; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q61086; protein.
DR   Bgee; ENSMUSG00000007989; Expressed in medial ganglionic eminence and 257 other tissues.
DR   Genevisible; Q61086; MM.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0030424; C:axon; IDA:BHF-UCL.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR   GO; GO:0032433; C:filopodium tip; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
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; ISO:MGI.
DR   GO; GO:0042813; F:Wnt receptor activity; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0017147; F:Wnt-protein binding; ISO:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:MGI.
DR   GO; GO:0033278; P:cell proliferation in midbrain; IGI:MGI.
DR   GO; GO:0071679; P:commissural neuron axon guidance; IMP:MGI.
DR   GO; GO:0036514; P:dopaminergic neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0001736; P:establishment of planar polarity; IGI:MGI.
DR   GO; GO:0001942; P:hair follicle development; IEP:BHF-UCL.
DR   GO; GO:0042472; P:inner ear morphogenesis; IGI:MGI.
DR   GO; GO:0030901; P:midbrain development; IGI:MGI.
DR   GO; GO:0097475; P:motor neuron migration; IMP:MGI.
DR   GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IMP:UniProtKB.
DR   GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; IMP:UniProtKB.
DR   GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR   GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:UniProtKB.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR   GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0036515; P:serotonergic neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0061549; P:sympathetic ganglion development; IMP:UniProtKB.
DR   CDD; cd07449; CRD_FZ3; 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; IPR041769; FZ3_CRD.
DR   InterPro; IPR026553; FZD3_vertebrates.
DR   InterPro; IPR017981; GPCR_2-like.
DR   PANTHER; PTHR11309; PTHR11309; 1.
DR   PANTHER; PTHR11309:SF22; PTHR11309:SF22; 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   Cell membrane; Developmental protein; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Neurogenesis; Receptor;
KW   Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW   Ubl conjugation; Wnt signaling pathway.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..666
FT                   /note="Frizzled-3"
FT                   /id="PRO_0000012983"
FT   TOPO_DOM        23..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..237
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..288
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..328
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        350..374
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        396..420
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        442..477
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        478..498
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        499..666
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          23..136
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   REGION          538..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           502..507
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   COMPBIAS        545..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        36..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        73..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        99..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        103..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   666 AA;  76208 MW;  0920038B79A73335 CRC64;
     MAVSWIVFDL WLLTVFLGQI GGHSLFSCEP ITLRMCQDLP YNTTFMPNLL NHYDQQTAAL
     AMEPFHPMVN LDCSRDFRPF LCALYAPICM EYGRVTLPCR RLCQRAYSEC SKLMEMFGVP
     WPEDMECSRF PDCDEPYPRL VDLNLVGDPT EGAPVAVQRD YGFWCPRELK IDPDLGYSFL
     HVRDCSPPCP NMYFRREELS FARYFIGLIS IICLSATLFT FLTFLIDVTR FRYPERPIIF
     YAVCYMMVSL IFFIGFLLED RVACNASSPA QYKASTVTQG SHNKACTMLF MVLYFFTMAG
     SVWWVILTIT WFLAAVPKWG SEAIEKKALL FHASAWGIPG TLTIILLAMN KIEGDNISGV
     CFVGLYDVDA LRYFVLAPLC LYVVVGVSLL LAGIISLNRV RIEIPLEKEN QDKLVKFMIR
     IGVFSILYLV PLLVVIGCYF YEQAYRGIWE TTWIQERCRE YHIPCPYQVT QMSRPDLILF
     LMKYLMALIV GIPSIFWVGS KKTCFEWASF FHGRRKKEIV NESRQVLQEP DFAQSLLRDP
     NTPIIRKSRG TSTQGTSTHA SSTQLAMVDD QRSKAGSVHS KVSSYHGSLH RSRDGRYTPC
     SYRGMEERLP HGSMSRLTDH SRHSSSHRLN EQSRHSSIRD LSNNPMTHIT HGTSMNRVIE
     EDGTSA
 
 
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