FZD3_XENLA
ID FZD3_XENLA Reviewed; 664 AA.
AC O42579;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Frizzled-3;
DE Short=Fz-3;
DE Short=Xfz3;
DE Flags: Precursor;
GN Name=fzd3; Synonyms=fz3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9510023; DOI=10.1016/s0925-4773(97)00166-4;
RA Shi D.-L., Goisset C., Boucaut J.-C.;
RT "Expression of Xfz3, a Xenopus frizzled family member, is restricted to the
RT early nervous system.";
RL Mech. Dev. 70:35-47(1998).
RN [2]
RP MUTAGENESIS, DOMAIN K-T-X-X-X-W MOTIF, AND COUPLING TO BETA-CATENIN
RP PATHWAY.
RX PubMed=10990458; DOI=10.1093/emboj/19.18.4944;
RA Umbhauer M., Djiane A., Goisset C., Penzo-Mendez A., Riou J.-F.,
RA Boucaut J.-C., Shi D.-L.;
RT "The C-terminal cytoplasmic Lys-Thr-X-X-X-Trp motif in frizzled receptors
RT mediates Wnt/beta-catenin signalling.";
RL EMBO J. 19:4944-4954(2000).
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. Activated by Wnt8. Involved in
CC transduction and intercellular transmission of polarity information
CC during tissue morphogenesis and/or in differentiated tissues. Plays a
CC role in controlling early axon growth and guidance processes necessary
CC for the formation of a subset of central and peripheral major fiber
CC tracts. Involved in the migration of cranial neural crest cells. May
CC also be implicated in the transmission of sensory information from the
CC 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). Promotes neurogenesis by maintaining sympathetic neuroblasts
CC within the cell cycle in a beta-catenin-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q61086}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell
CC surface {ECO:0000250|UniProtKB:Q61086}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q61086}; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expression restricted to the early nervous system.
CC -!- DEVELOPMENTAL STAGE: Low expression from cleavage stages to the end of
CC gastrulation; increases from neurulation onward. During neurulation,
CC first localized to the anterior neural folds. As neurulation proceeds,
CC the expression extends to the trunk neural fold, with low levels in the
CC posterior neural fold. At the end of neurulation, strongly expressed as
CC a large band in the midbrain. After neural tube closure, also detected
CC in the optic lobes and otic vesicles. During the late development,
CC expression remains restricted to the nervous system. Detected until at
CC least the larval stages.
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:0000269|PubMed:10990458}.
CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ001754; CAA04977.1; -; mRNA.
DR RefSeq; NP_001083918.1; NM_001090449.1.
DR AlphaFoldDB; O42579; -.
DR SMR; O42579; -.
DR MINT; O42579; -.
DR GeneID; 399190; -.
DR KEGG; xla:399190; -.
DR CTD; 399190; -.
DR Xenbase; XB-GENE-865070; fzd3.L.
DR OrthoDB; 330751at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 399190; Expressed in brain and 17 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042813; F:Wnt receptor activity; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0014036; P:neural crest cell fate specification; TAS:AgBase.
DR GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
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 Wnt signaling pathway.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..664
FT /note="Frizzled-3"
FT /id="PRO_0000012984"
FT TOPO_DOM 17..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..373
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..476
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..135
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 537..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 501..506
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 544..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 35..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 72..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 98..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 102..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT MUTAGEN 501
FT /note="K->M: Complete loss of activity to induce the Wnt
FT target gene Siamois expression."
FT /evidence="ECO:0000269|PubMed:10990458"
FT MUTAGEN 502
FT /note="T->V: Complete loss of activity to induce the Wnt
FT target gene Siamois expression."
FT /evidence="ECO:0000269|PubMed:10990458"
FT MUTAGEN 503
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:10990458"
FT MUTAGEN 506
FT /note="W->G: Complete loss of activity to induce the Wnt
FT target gene Siamois expression."
FT /evidence="ECO:0000269|PubMed:10990458"
FT MUTAGEN 507
FT /note="A->V: No effect."
FT /evidence="ECO:0000269|PubMed:10990458"
FT MUTAGEN 508
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:10990458"
FT MUTAGEN 509
FT /note="F->L: No effect."
FT /evidence="ECO:0000269|PubMed:10990458"
SQ SEQUENCE 664 AA; 75619 MW; 51BCC43BDA1791E5 CRC64;
MAAYLISFIW VSVILAQKSM GHSLFACEPI TLRMCQDLPY NSTFMPNLLN HYDQQTAALA
MEPFHPMVNL ECSRDLRPFL CALYTPVCME YGRMTLPCRK LCQRAYNECF KLMEMFGVPW
PEEMECSRFP DCDEPYPRIV DISLSGEPSE ETPLAVQRDY GFWCPRELKI DPDLRSSFLG
VRDCSPPCPH MYFRREELSF ARYFIGVISI VCLSATLFTF LTFLIDVTRF RYPERPIIFY
AVCYMMVSLI FFIGFLLEDK VACNGANPSQ YKASTVTQGS HNKACTMLFM VLYFFTMAGS
VWWVILTITW FLAAVPKWGS EAIEKKALLF HASAWGIPGT LTIILLAMNK IEGDNISGVC
FVGLYDVHAL RYFVLAPLCL DVVVGVSLLL AGIISLNRVR IEIPLEKENQ DKLVKFMIRI
GVFSILYLVP LLVVIGCYFY EQAYRGVWET TWVQERCREY HIPCPYKVTQ TSRPDLILFL
MKYLMLLVVG IPSVFWVGSK KTCFEWASFF HGRKKKAGVN ESRQVLQEPD FAQSLLRDPN
TPIVRKSRGT STQGTSTHAS STQLAMLDDQ RSKAGSVQSK VSSYHGSLHR SRDGRYTPCS
YRGIEERLPH GSMSHLTDHS RHSSTHRLNE QSHQGSIRDL SNPLAHISHG TSMNRVIEAD
ATSA
