FZD6_PONAB
ID FZD6_PONAB Reviewed; 707 AA.
AC Q5RCN4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Frizzled-6;
DE Short=Fz-6;
DE Flags: Precursor;
GN Name=FZD6;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858236; CAH90473.1; -; mRNA.
DR RefSeq; NP_001125247.1; NM_001131775.2.
DR AlphaFoldDB; Q5RCN4; -.
DR SMR; Q5RCN4; -.
DR STRING; 9601.ENSPPYP00000021096; -.
DR GeneID; 100172142; -.
DR KEGG; pon:100172142; -.
DR CTD; 8323; -.
DR eggNOG; KOG3577; Eukaryota.
DR InParanoid; Q5RCN4; -.
DR OrthoDB; 330751at2759; -.
DR Proteomes; UP000001595; 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; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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 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; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transducer; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Wnt signaling pathway.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..707
FT /note="Frizzled-6"
FT /id="PRO_0000243938"
FT TOPO_DOM 20..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..474
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..707
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..133
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 589..707
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 659..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61089"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 33..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 70..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 96..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 100..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 707 AA; 79512 MW; 8898BD05E1615889 CRC64;
MEMFTFFLLT CIFLPLVRGH SLFTCEPITV PRCMKMAYNM TFFPNLMGHY DQSIAAVEME
HFLPLANLEC SPNIETFLCK AFVPTCTEQI HVVPPCRKLC EKVYSDCKKL IDTFGIRWPE
ELECDRLQYC DETVPVTFDP HTEFLGPQKK TEQVQRDIGF WCPRHLKTSG GQGYKFLGID
QCAPPCPNMY FKSDELEFAK SFIGTVSIFC LCATLFTFLT FLIDVRRFRY PERPIIYYSV
CYSIVSLMYF IGFLLGDSTA CNKADEKLEL GDTVVLGSQN KACTVLFMLL YFFTMAGTVW
WVILTITWFL AAGRKWSCEA IEQKAVWFHA VAWGTPGFLT VMLLAMNKVE GDNISGVCFV
GLYDLDASRY FVLLPLCLCV FVGLSLLLAG IISLNHVRQV IQHDGRNQEK LKKFMIRIGV
FSGLYLVPLV TLLGCYVYEQ VNRITWEITW VSDHCRQYHI PCPYQAKAKA RPELALFMIK
YLMTLIVGIS AVFWVGSKKT CTEWAGFFKR NRKRDPISES RRVLQESCEF FLKHNSKVKH
KKKHYKPSSH KLKVISKSMG TSTGATANHG TSAVAITSHD YLGQETLTEI QTSPETSMRE
VKADGASTPR LREQDCGEPA SPAASISRLS GEQVDRKGQA GSVSESARSE GRISPKSDIT
DTGLAQSNNL QVPSSSEPSS LKGSTSLLVH PVSGVRKEQG GGCHSDT
