FZD7A_XENLA
ID FZD7A_XENLA Reviewed; 549 AA.
AC Q9PUK8; Q9IB13; Q9PWN7; Q9W703; Q9W743;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Frizzled-7-A;
DE Short=Fz-7-A;
DE Short=Xfz7-A;
DE Flags: Precursor;
GN Name=fzd7-a; Synonyms=fz7-a;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Oocyte;
RX PubMed=10751186; DOI=10.1242/dev.127.9.1981;
RA Sumanas S., Strege P., Heasman J., Ekker S.C.;
RT "The putative Wnt receptor Xenopus frizzled-7 functions upstream of beta-
RT catenin in vertebrate dorso-ventral mesoderm patterning.";
RL Development 127:1981-1990(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH WNT11, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula;
RX PubMed=10862746; DOI=10.1242/dev.127.14.3091;
RA Djiane A., Riou J.-F., Umbhauer M., Boucaut J.-C., Shi D.-L.;
RT "Role of frizzled 7 in the regulation of convergent extension movements
RT during gastrulation in Xenopus laevis.";
RL Development 127:3091-3100(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Oocyte;
RX DOI=10.1046/j.1440-169x.2000.00517.x;
RA Brown J.D., Hallagan S.E., McGrew L.L., Miller J.R., Moon R.T.;
RT "The maternal Xenopus beta-catenin signaling pathway, activated by frizzled
RT homologs, induces goosecoid in a cell non-autonomous manner.";
RL Dev. Growth Differ. 42:347-357(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Neurula;
RX PubMed=10727861; DOI=10.1016/s0925-4773(00)00240-9;
RA Medina A., Reintsch W., Steinbeisser H.;
RT "Xenopus frizzled 7 can act in canonical and non-canonical Wnt signaling
RT pathways: implications on early patterning and morphogenesis.";
RL Mech. Dev. 92:227-237(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gradl D., Buhrmann V., Wedlich D.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=10906785;
RX DOI=10.1002/1097-0177(2000)9999:9999<::aid-dvdy1017>3.0.co;2-9;
RA Medina A., Steinbeisser H.;
RT "Interaction of Frizzled 7 and Dishevelled in Xenopus.";
RL Dev. Dyn. 218:671-680(2000).
RN [7]
RP FUNCTION.
RX PubMed=10990458; DOI=10.1093/emboj/19.18.4944;
RA Umbhauer M., Djiane A., Goisset C., Penzo-Mendez A., Riou J.-F.,
RA Boucaut J.-C., Shi D.-L.;
RT "The C-terminal cytoplasmic Lys-Thr-X-X-X-Trp motif in frizzled receptors
RT mediates Wnt/beta-catenin signalling.";
RL EMBO J. 19:4944-4954(2000).
RN [8]
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 [9]
RP FUNCTION, AND DOMAIN.
RX PubMed=11291855;
RA Swain R.K., Medina A., Steinbeisser H.;
RT "Functional analysis of the Xenopus frizzled 7 protein domains using
RT chimeric receptors.";
RL Int. J. Dev. Biol. 45:259-264(2001).
RN [10]
RP FUNCTION.
RX PubMed=11677610; DOI=10.1038/35101621;
RA Winklbauer R., Medina A., Swain R.K., Steinbeisser H.;
RT "Frizzled-7 signalling controls tissue separation during Xenopus
RT gastrulation.";
RL Nature 413:856-860(2001).
RN [11]
RP FUNCTION, AND INTERACTION WITH PCDH8.
RX PubMed=15272309; DOI=10.1038/sj.emboj.7600329;
RA Medina A., Swain R.K., Kuerner K.-M., Steinbeisser H.;
RT "Xenopus paraxial protocadherin has signaling functions and is involved in
RT tissue separation.";
RL EMBO J. 23:3249-3258(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH SDC4.
RX PubMed=16604063; DOI=10.1038/ncb1399;
RA Munoz R., Moreno M., Oliva C., Orbenes C., Larrain J.;
RT "Syndecan-4 regulates non-canonical Wnt signalling and is essential for
RT convergent and extension movements in Xenopus embryos.";
RL Nat. Cell Biol. 8:492-500(2006).
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:0000269|PubMed:10727861,
CC ECO:0000269|PubMed:10751186, ECO:0000269|PubMed:10862746,
CC ECO:0000269|PubMed:10906785, ECO:0000269|PubMed:10990458,
CC ECO:0000269|PubMed:11291855, ECO:0000269|PubMed:11477687,
CC ECO:0000269|PubMed:11677610, ECO:0000269|PubMed:15272309,
CC ECO:0000269|PubMed:16604063, ECO:0000269|Ref.3}.
CC -!- SUBUNIT: Interacts with wnt11 and sdc4. The extracellular domain
CC interacts with the extracellular domain of pcdh8/papc.
CC {ECO:0000269|PubMed:10862746, ECO:0000269|PubMed:15272309,
CC ECO:0000269|PubMed:16604063}.
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: Expressed in the animal region of cleavage stage
CC embryos. During gastrulation, broadly expressed on the dorsal side of
CC the embryo in deep mesodermal cells surrounding the blastopore lip and
CC in presumptive anterior neuroectoderm. During neurulation, becomes
CC progressively more restricted to the dorsal epidermis, neural plate,
CC and neural tube. Expressed in the cranial neural crest of neurulae and
CC tailbud embryos as well as the pronephros of tailbud embryos. Localized
CC to the brain of neurulae, tailbud embryos and tadpoles. In tadpoles,
CC strongly expressed in the eye and developing heart.
CC {ECO:0000269|PubMed:10727861, ECO:0000269|PubMed:10862746,
CC ECO:0000269|Ref.3}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed at low levels during cleavage stages, with zygotic expression
CC increasing at the start of gastrulation, remaining constant through the
CC gastrulation stages and then decreasing from late neurula stage
CC onwards. {ECO:0000269|PubMed:10727861, ECO:0000269|PubMed:10862746,
CC ECO:0000269|Ref.3}.
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:0000269|PubMed:11291855}.
CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC {ECO:0000250}.
CC -!- DOMAIN: The extracellular domain interacts with Wnt proteins and the
CC intracellular C-terminus transmits the Wnt signal.
CC {ECO:0000269|PubMed:11291855}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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; AF039215; AAF63152.1; -; mRNA.
DR EMBL; AJ243323; CAB45875.1; -; mRNA.
DR EMBL; AF179213; AAD52671.1; -; mRNA.
DR EMBL; AF114151; AAD21247.1; -; mRNA.
DR RefSeq; NP_001079354.1; NM_001085885.1.
DR AlphaFoldDB; Q9PUK8; -.
DR SMR; Q9PUK8; -.
DR IntAct; Q9PUK8; 4.
DR MINT; Q9PUK8; -.
DR DNASU; 378787; -.
DR GeneID; 378787; -.
DR CTD; 378787; -.
DR Xenbase; XB-GENE-483735; fzd7.L.
DR OMA; SFSCPRQ; -.
DR OrthoDB; 330751at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 378787; Expressed in gastrula and 18 other tissues.
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; TAS:Reactome.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0045545; F:syndecan binding; IPI:UniProtKB.
DR GO; GO:0042813; F:Wnt receptor activity; IEA:InterPro.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:BHF-UCL.
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; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IGI:UniProtKB.
DR GO; GO:0048729; P:tissue morphogenesis; IGI: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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..549
FT /note="Frizzled-7-A"
FT /id="PRO_0000012999"
FT TOPO_DOM 23..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..503
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..151
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT MOTIF 527..532
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 547..549
FT /note="PDZ-binding"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 45..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 82..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 108..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 112..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 11
FT /note="C -> G (in Ref. 4; AAD52671)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="L -> F (in Ref. 5; AAD21247)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="T -> I (in Ref. 5; AAD21247)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="S -> F (in Ref. 5; AAD21247)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="G -> S (in Ref. 2; CAB45875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 62119 MW; DA44954BFF8F594B CRC64;
MSSTVSLLFC CLFLQLCPSA QQYHGEKGIS VPDHGFCQPI SIPLCTDIAY NQTIMPNLLG
HTNQEDAGLE VHQFYPLVKV QCSPELRFFL CSMYAPVCTV LEQAIPPCRS LCERARQGCE
ALMNKFGFQW PERLRCENFP VHGAGEICVG QNTSDNSPSG PTARPSPYLP DSITFQPHPH
RDFTCPRQLK VPPYLAYRFL GEKDCGAPCE PGKANGLMYF KEEEVRFARL WVGIWAILCC
ISTLFTVLTY LVDMRRFSYP ERPIIFLSGC YFMVAVAYTA GFLLEERAVC VERFSEDSYR
TVAQGTKKEG CTILFMILYF FGMASSIWWV ILSLTWFLSA GMKWGHEAIE ANSQYFHLAA
WAVPAVKTIT ILAMGQVDGD VLSGVCYVGI NSVDSLRGFV LAPLFVYLFI GTSFLLAGFV
SLFRIRTIMK HDGTKTEKLE KLMVRIGVFS VMYTVPATIV LACYFYEQAF RDTWEKTWLV
QTCKGYAVPC PNYNFAPMSP DFTVFMIKYL MTMIVGITSS FWIWSGKTLQ SWRRFYHRLS
NGSKGETAV
