FZD7_CHICK
ID FZD7_CHICK Reviewed; 567 AA.
AC O57329; Q9IA04;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Frizzled-7;
DE Short=Fz-7;
DE Short=cFz-7;
DE Flags: Precursor;
GN Name=FZD7; Synonyms=FZ7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Limb bud;
RX PubMed=9598377;
RA Kengaku M., Twombly V., Tabin C.;
RT "Expression of Wnt and Frizzled genes during chick limb bud development.";
RL Cold Spring Harb. Symp. Quant. Biol. 62:421-429(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=10781956; DOI=10.1016/s0925-4773(00)00263-x;
RA Stark M.R., Biggs J.J., Schoenwolf G.C., Rao M.S.;
RT "Characterization of avian frizzled genes in cranial placode development.";
RL Mech. Dev. 93:195-200(2000).
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. May be involved in transduction and
CC intercellular transmission of polarity information during tissue
CC morphogenesis and/or in differentiated tissues.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75084};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O75084}. Endosome
CC membrane {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 broadly in cranial ectoderm. Also
CC expressed in the developing somites and in other cranial placodes,
CC including the olfactory, lens, otic placodes (lateral half of the
CC vesicle) and epibranchial placodes. Low level of expression in all the
CC mesoderm derivatives in the limb buds.
CC -!- DEVELOPMENTAL STAGE: First detected as stage 6 in the forming neural
CC tube and somites, but not in trunk surface ectoderm. By stage 8,
CC expression persists in the cranial ectoderm and is up-regulated in the
CC presomptive olfactory placodes. By stages 11-12, expression declines in
CC the neural tube, but not in the cranial ectoderm; in somites, expressed
CC all along the rostral-caudal axis as well as in presegmental mesenchyme
CC caudal to the developing somites. Lens and otic placode expression
CC first visible at stage 12, strongest at stages 13-16. Detected
CC uniformly in ectoderm and mesenchyme of the limb primordia at stage 17.
CC By stage 18, decrease of ectodermal, otic, lens and olfactory placode
CC expression; expression appears in the epibranchial placodes. By stages
CC 22-30, highest levels in the most distal mesoderm of the autopod, in
CC the ventricular zone of the neural tube from the forebrain to the
CC spinal cord, in the dermomyotomes and the tail buds.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; AF031831; AAB87969.1; -; mRNA.
DR EMBL; AF224317; AAF61097.1; -; mRNA.
DR RefSeq; NP_989552.1; NM_204221.2.
DR AlphaFoldDB; O57329; -.
DR SMR; O57329; -.
DR STRING; 9031.ENSGALP00000030969; -.
DR PaxDb; O57329; -.
DR GeneID; 374060; -.
DR KEGG; gga:374060; -.
DR CTD; 8324; -.
DR VEuPathDB; HostDB:geneid_374060; -.
DR eggNOG; KOG3577; Eukaryota.
DR InParanoid; O57329; -.
DR OrthoDB; 330751at2759; -.
DR PhylomeDB; O57329; -.
DR PRO; PR:O57329; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0042813; F:Wnt receptor activity; IEA:InterPro.
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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..567
FT /note="Frizzled-7"
FT /id="PRO_0000012998"
FT TOPO_DOM 32..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..330
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..161
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT MOTIF 545..550
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 565..567
FT /note="PDZ-binding"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 55..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 92..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 118..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 122..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 34..35
FT /note="HE -> QD (in Ref. 2; AAF61097)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="V -> L (in Ref. 2; AAF61097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 62811 MW; 3EFF0381FC899BC3 CRC64;
MRPAAGEAGA GLRWLGLAAL LAALLGTPCA AAHHEDKAIS VPDHGFCQPI SIPLCTDIAY
NQTILPNLLG HTNQEDAGLE VHQFYPLVKV QCSAELKFFL CSMYAPVCTV LEQAIPPCRS
LCERARQGCE ALMNKFGFQW PERLRCENFP VHGAGEICVG QNTSDAPPGP GGAGGRGATA
QPTAGYLPDL LTPPQPAAGF SFSCPRQLKV PPYLGYRFLG ERDCGAPCEP GRPNGLMYFK
EAEVRFARLW VGVWSVLCCA STLFTVLTYL VDMRRFSYPE RPIIFLSGCY FMVAVAYAAG
FLLEERVVCL ERFSEDGYRT VAQGTKKEGC TILFMILYFF GMASSIWWVI LSLTWFLAAG
MKWGHEAIEA NSQYFHLAAW AVPAVKTITI LAMGQVDGDV LSGVCYVGIY SVDSLRGFVL
APLFVYLFIG TSFLLAGFVS LFRIRTIMKH DGTKTEKLEK LMVRIGVFSV LYTVPATIVV
ACYFYEQAFR STWEKTWLLQ TCKTYAVPCP SHFAPMSPDF TVFMIKYLMT MIVGITTGFW
IWSGKTLQSW RRFYHRLSTG SKGETAV
