FZD6_CANLF
ID FZD6_CANLF Reviewed; 712 AA.
AC Q8WMU5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Frizzled-6;
DE Short=Fz-6;
DE Flags: Precursor;
GN Name=FZD6;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=15265686; DOI=10.1016/j.yexcr.2004.04.036;
RA Lyons J.P., Mueller U.W., Ji H., Everett C., Fang X., Hsieh J.C.,
RA Barth A.M., McCrea P.D.;
RT "Wnt-4 activates the canonical beta-catenin-mediated Wnt pathway and binds
RT Frizzled-6 CRD: functional implications of Wnt/beta-catenin activity in
RT kidney epithelial cells.";
RL Exp. Cell Res. 298:369-387(2004).
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. Together with FZD3, is
CC involved in the neural tube closure and plays a role in the regulation
CC of the establishment of planar cell polarity (PCP), particularly in the
CC orientation of asymmetric bundles of stereocilia on the apical faces of
CC a subset of auditory and vestibular sensory cells located in the inner
CC ear (By similarity). {ECO:0000250|UniProtKB:Q61089}.
CC -!- SUBUNIT: Interacts with LMBR1L. {ECO:0000250|UniProtKB:Q61089}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q61089}; Multi-
CC pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein
CC {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:Q61089}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalizes with FZD3 at the apical face of cells
CC (By similarity). Localizes to the endoplasmic reticulum membrane in the
CC presence of LMBR1L (By similarity). {ECO:0000250|UniProtKB:Q61089}.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; AY052750; AAL12245.1; -; mRNA.
DR RefSeq; NP_001003065.1; NM_001003065.1.
DR AlphaFoldDB; Q8WMU5; -.
DR SMR; Q8WMU5; -.
DR STRING; 9612.ENSCAFP00000000924; -.
DR PaxDb; Q8WMU5; -.
DR GeneID; 403610; -.
DR KEGG; cfa:403610; -.
DR CTD; 8323; -.
DR eggNOG; KOG3577; Eukaryota.
DR InParanoid; Q8WMU5; -.
DR OrthoDB; 330751at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd07450; CRD_FZ6; 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; IPR041770; FZ6_CRD.
DR InterPro; IPR026543; FZD6.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF75; PTHR11309:SF75; 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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Developmental protein; Disulfide bond;
KW Endoplasmic reticulum; G-protein coupled receptor; Glycoprotein; Membrane;
KW Neurogenesis; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix; Ubl conjugation; Wnt signaling pathway.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..712
FT /note="Frizzled-6"
FT /id="PRO_0000012993"
FT TOPO_DOM 19..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..473
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..712
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..132
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 588..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 498..503
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 664..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 32..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 69..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 95..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 99..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 712 AA; 80180 MW; B67F7C9056F645A6 CRC64;
MEMFTFLLTC VFLPFVRGHS LFTCEPITVP RCMKMAYNMT FFPNLMRHYD QSTAAVKMEP
FLPLANLECS PNIETFLCKA FVPACTDQIN VVPPCRKFCE KVYSDCKKLI DTFGMRWPEE
LECDRLQYCD ETVPVTFDPH TQFLGPQKNT EQVQRDIGFW CPRHLKTSGG QGYKFLGIDQ
CAPPCPNMYF KSDELEFAKS FIGIVSIFCL CATLFTFLTF LIDVKRFRYP ERPIIYYSVC
YSIVSLMYFI GFLLGDRTAC NKADEKLELG DTVVLGSQNK ACTVLFMFLY FFTMAGTVWW
VILTITWFLA AGRKWSCEAI EQKAVWFHAV AWGIPGFLTV MLLAMNKVEG DNISGVCFVG
LYDLDASRYF VLLPLCLCVF VGLSLLLAGI ISLNHVRQVI QHDGRNQEKL KKFMIRIGVF
SGLYLVPLVT LLGCYVYEQV NRITWEITWV SDHCRQYHIP CPYQAKTETR PELALFMIKY
LMTLIVGISA VFWVGSKKTC TEWAGFFKRN RKRDPISESR RVLQESCEFF LKHNSKVKHK
KKHYKPSSHK LKVISKSMGT STGATANHGT SAVAITNHDY LGQETLTEIQ TSPETSVREV
RADGASTPRS REQDCGEPAS PAASSSRLCE EQADRKGRAG NGTDKISISE STRSEGRVTP
KSDVTETGPM QSSSLQVPGS SEPGSLKGST SLLVHSASGG RKEHGTGSHS DT
