FZD7B_XENLA
ID FZD7B_XENLA Reviewed; 548 AA.
AC Q8AVJ9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Frizzled-7-B;
DE Short=Fz-7-B;
DE Short=Xfz7-B;
DE Flags: Precursor;
GN Name=fzd7-b; Synonyms=fz7-b;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10446283; DOI=10.1016/s0925-4773(99)00117-3;
RA Wheeler G.N., Hoppler S.;
RT "Two novel Xenopus frizzled genes expressed in developing heart and
RT brain.";
RL Mech. Dev. 86:203-207(1999).
RN [2] {ECO:0000312|EMBL:AAH42228.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH42228.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=10899005; DOI=10.1016/s0960-9822(00)00596-0;
RA Wheeler G.N., Hamilton F.S., Hoppler S.;
RT "Inducible gene expression in transgenic Xenopus embryos.";
RL Curr. Biol. 10:849-852(2000).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=11477687; DOI=10.1002/gene.1044;
RA Sumanas S., Ekker S.C.;
RT "Xenopus frizzled-7 morphant displays defects in dorsoventral patterning
RT and convergent extension movements during gastrulation.";
RL Genesis 30:119-122(2001).
RN [5]
RP FUNCTION, INTERACTION WITH DVL1, AND MUTAGENESIS OF LYS-526 AND TRP-531.
RX PubMed=14636582; DOI=10.1016/s1097-2765(03)00427-1;
RA Wong H.C., Bourdelas A., Krauss A., Lee H.J., Shao Y., Wu D., Mlodzik M.,
RA Shi D.L., Zheng J.;
RT "Direct binding of the PDZ domain of Dishevelled to a conserved internal
RT sequence in the C-terminal region of Frizzled.";
RL Mol. Cell 12:1251-1260(2003).
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 cell
CC movements during gastrulation. Triggers phosphorylation of dvl2/dsh and
CC its 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. {ECO:0000250|UniProtKB:Q9PUK8,
CC ECO:0000269|PubMed:10899005, ECO:0000269|PubMed:11477687,
CC ECO:0000269|PubMed:14636582}.
CC -!- SUBUNIT: Interacts with wnt11 and sdc4. The extracellular domain
CC interacts with the extracellular domain of pcdh8/papc (By similarity).
CC Interacts (via C-terminus) with dvl1 (via PDZ domain). {ECO:0000250,
CC ECO:0000269|PubMed:14636582}.
CC -!- INTERACTION:
CC Q8AVJ9; P51141: Dvl1; Xeno; NbExp=3; IntAct=EBI-3870271, EBI-1538407;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. 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 -!- TISSUE SPECIFICITY: During gastrulation, broadly expressed on the
CC dorsal side of the embryo in deep mesodermal cells surrounding the
CC blastopore lip and in presumptive anterior neuroectoderm. During
CC neurulation, localized to the cranial neural crest and heart field
CC where expression is retained at later stages in addition to new areas
CC of expression in the neural tube, pronephros and tailbud. At tailbud
CC stage, expressed in the pronephric duct, and broad head expression
CC becomes more restricted to the hindbrain. In tadpoles, strongly
CC expressed in the eye and the pericardium and myocardium of the
CC developing heart. {ECO:0000269|PubMed:10446283}.
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.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000255}.
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; AF159106; AAD44331.1; -; mRNA.
DR EMBL; BC042228; AAH42228.1; -; mRNA.
DR AlphaFoldDB; Q8AVJ9; -.
DR SMR; Q8AVJ9; -.
DR IntAct; Q8AVJ9; 1.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0017147; F:Wnt-protein binding; ISS:UniProtKB.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP: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; IMP: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 1: Evidence at protein 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..548
FT /note="Frizzled-7-B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000282949"
FT TOPO_DOM 19..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..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..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:0000269|PubMed:14636582"
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 MUTAGEN 526
FT /note="K->M: Reduced binding to dvl1."
FT /evidence="ECO:0000269|PubMed:14636582"
FT MUTAGEN 531
FT /note="W->G: Reduced binding to dvl1."
FT /evidence="ECO:0000269|PubMed:14636582"
FT CONFLICT 168
FT /note="L -> P (in Ref. 1; AAD44331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 61906 MW; 97B3408B3C0EA273 CRC64;
MLAPVSLLFC LFLQLCPSAQ QYHGEKGISV PDHGFCQPIS IPLCTDIAYN QTIMPNLLGH
TNQEDAGLEV HQFYPLVKVQ CSPELRFFLC SMYAPVCTVL EQAIPPCRSL CERARQGCEA
LMNKFGFQWP ERLRCENFPV HGAGEICVGQ NTSDNSPSGP TARPTLNLPD SITFQPHPHR
DFTCPRQLKV PPYLGYRFLG EKDCGAPCEP GKANGLMYFK EEEVRFARLW VGIWAILCGI
STLFTVLTYL VDMRRFSYPE RPIIFLSGCY FMVAVAYTAG FLLEERAVCV ERFSEDSYRT
VAQGTKKEGC TILFMILYFF GMASSIWWVI LALTWFLSAG MKWGHEAIEA NSQYFHLAAW
AVPAVKTITI LAMGQVDGDV LSGVCYVGIN SVDSLRGFVL APLFVYLFLG TSFLLAGFVS
LFRIRTIMKH DGTKTEKLEK LMVRIGVFSV MYTVPATIVL ACYFYEQAFR DTWEKTWLVH
TCKGYAVPCP NYNFAPMSPD FTVFMIKYLM TMIVGITSSF WIWSGKTLQS WRRFYHRLGN
GSKGETAV
