FZD7_XENTR
ID FZD7_XENTR Reviewed; 548 AA.
AC Q5BL72; Q28J97;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Frizzled-7;
DE Short=Frz7;
DE Short=Fz-7;
DE Flags: Precursor;
GN Name=fzd7 {ECO:0000312|EMBL:CAJ82817.1}; ORFNames=TNeu065e03.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAZ06130.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Qin S., Dors M., Johnson E., Bloom S., Hood L., Rowen L.;
RT "Sequence of Xenopus tropicalis development genes.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAZ06130.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula {ECO:0000312|EMBL:CAJ82817.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAZ06130.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAH90579.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for Wnt proteins. Acts in both canonical and non-
CC canonical Wnt pathways. Although different papers report differing Wnt
CC preferences, wnt5a, wnt8b and wnt11 have been proposed as synergists.
CC In the canonical Wnt pathway, acts via beta-catenin to promote the
CC expression of the dorsal genes siamois, twin and nodal3 and to
CC establish the dorsal axis of the embryo and induce dorsal mesoderm
CC formation. In a non-canonical Wnt/planar cell polarity (PCP) pathway,
CC acts with sdc4 and dvl2/dsh to regulate convergent extension movements
CC in gastrulation. Triggers phosphorylation of dvl2/dsh and its
CC translocation to the plasma membrane. In a third branch of Wnt
CC signaling, acts in a non-canonical pathway via trimeric G proteins, and
CC independently of dvl2/dsh, to recruit protein kinase C (PKC) to the
CC membrane and thus activate PKC. PKC signaling controls cell sorting and
CC tissue separation during gastrulation (By similarity).
CC {ECO:0000250|UniProtKB:Q9PUK8}.
CC -!- SUBUNIT: Interacts with wnt11 and sdc4. The extracellular domain
CC interacts with the extracellular domain of pcdh8/papc (By similarity).
CC {ECO:0000250|UniProtKB:Q9PUK8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Endosome membrane
CC {ECO:0000250|UniProtKB:O75084}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O75084}. Note=Associated to the plasma membrane
CC in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate
CC (PIP2). Localized in recycling endosomes in other conditions.
CC {ECO:0000250|UniProtKB:O75084}.
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|UniProtKB:Q9VVX3}.
CC -!- DOMAIN: The extracellular domain interacts with Wnt proteins and the
CC intracellular C-terminus transmits the Wnt signal.
CC {ECO:0000250|UniProtKB:Q9PUK8}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000255}.
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DR EMBL; AC149036; AAZ06130.1; -; Genomic_DNA.
DR EMBL; CR759995; CAJ82817.1; -; mRNA.
DR EMBL; BC090579; AAH90579.1; -; mRNA.
DR RefSeq; NP_001016741.1; NM_001016741.2.
DR AlphaFoldDB; Q5BL72; -.
DR SMR; Q5BL72; -.
DR PaxDb; Q5BL72; -.
DR DNASU; 549495; -.
DR Ensembl; ENSXETT00000027115; ENSXETP00000027115; ENSXETG00000012404.
DR GeneID; 549495; -.
DR KEGG; xtr:549495; -.
DR CTD; 8324; -.
DR Xenbase; XB-GENE-483731; fzd7.
DR eggNOG; KOG3577; Eukaryota.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; Q5BL72; -.
DR OrthoDB; 330751at2759; -.
DR Reactome; R-XTR-4086400; PCP/CE pathway.
DR Reactome; R-XTR-4608870; Asymmetric localization of PCP proteins.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000012404; Expressed in gastrula and 18 other tissues.
DR ExpressionAtlas; Q5BL72; baseline.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0045545; F:syndecan binding; ISS:UniProtKB.
DR GO; GO:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; ISS:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; ISS:UniProtKB.
DR GO; GO:0009950; P:dorsal/ventral axis specification; ISS:UniProtKB.
DR GO; GO:0001707; P:mesoderm formation; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0048729; P:tissue morphogenesis; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:UniProtKB.
DR CDD; cd07466; CRD_FZ7; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR042742; Frizzled-7_CRD.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_TM.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR026552; FZD7.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF31; PTHR11309:SF31; 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; Developmental protein; Disulfide bond; Endosome;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..548
FT /note="Frizzled-7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000282950"
FT TOPO_DOM 20..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..502
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..150
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT MOTIF 526..531
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 MOTIF 546..548
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 44..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 81..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 107..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 111..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 140
FT /note="V -> I (in Ref. 2; CAJ82817)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="P -> L (in Ref. 2; CAJ82817)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 61872 MW; 6DC7815D767F54C3 CRC64;
MFATVSLLFC LLLQPSPSAQ QYHGEKGISV PDHGFCQPIS IPLCTDIAYN QTIMPNLLGH
TNQEDAGLEV HQFYPLVKVQ CSPELRFFLC SMYAPVCTVL EQAIPPCRSL CERARQGCEA
LMNKFGFQWP ERLRCENFPV HGAGEICVGQ NTSDNSPSGP TARPTPYLPD SITFHPHPNR
DFTCPRQLKV PPYLGYRFLG EKDCGAPCEP GKANGLMYFK EEEVRFARLW VGIWAILCGI
STLFTVLTYL VDMRRFSYPE RPIIFLSGCY FMVAVAYTAG FLLEERGVCV ERFSEDSYRT
VAQGTKKEGC TILFMILYFF GMASSIWWVI LSLTWFLAAG MKWGHEAIEA NSQYFHLAAW
AVPAVKTITI LAMGQVDGDI LSGVCYVGIN SVDSLRGFVL APLFVYLFIG TSFLLAGFVS
LFRIRTIMKH DGTKTEKLEK LMVRIGVFSV MYTVPATIVL ACYFYEQAFR DTWEKTWLVQ
TCKGFAVPCP NYNFAPMSPD FTVFMIKYLM TMIVGITSSF WIWSGKTLQS WRRFYHRLSN
GGKGETAV
