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   27-MAR-2024, entry version 92.
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}.
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DR   EMBL; AF159106; AAD44331.1; -; mRNA.
DR   EMBL; BC042228; AAH42228.1; -; mRNA.
DR   AlphaFoldDB; Q8AVJ9; -.
DR   SMR; Q8AVJ9; -.
DR   IntAct; Q8AVJ9; 1.
DR   GlyCosmos; Q8AVJ9; 2 sites, No reported glycans.
DR   AGR; Xenbase:XB-GENE-483735; -.
DR   Xenbase; XB-GENE-17333315; fzd7.S.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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: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; cd15246; 7tmF_FZD7; 1.
DR   CDD; cd07466; CRD_FZ7; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR042742; Frizzled-7_CRD.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_7TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF31; FRIZZLED-7; 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; Frizzled cysteine-rich domain; 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
//