FZD1_CHICK
ID FZD1_CHICK Reviewed; 592 AA.
AC O57328; Q9IA07;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Frizzled-1;
DE Short=Fz-1;
DE Short=cFz-1;
DE Flags: Precursor;
GN Name=FZD1; Synonyms=FZ1;
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] OF 307-592.
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. Functions in the canonical
CC Wnt/beta-catenin signaling pathway. The canonical Wnt/beta-catenin
CC signaling pathway leads to the activation of disheveled proteins,
CC inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and
CC activation of Wnt target genes (By similarity). A second signaling
CC pathway involving PKC and calcium fluxes has been seen for some family
CC members, but it is not yet clear if it represents a distinct pathway or
CC if it can be integrated in the canonical pathway, as PKC seems to be
CC required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways
CC seem to involve interactions with G-proteins. May be involved in
CC transduction and intercellular transmission of polarity information
CC during tissue morphogenesis and/or in differentiated tissues
CC (Probable). {ECO:0000250|UniProtKB:Q9UP38, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UP38};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the lens, otic placode (medial wall of
CC the vesicle) and in epibranchial placode. Also expressed in the
CC developing somites (dermomyotome).
CC -!- DEVELOPMENTAL STAGE: Somites and placodal expression appears at stage
CC 9. At this stage, more obvious expression is detected in the neural
CC tube (midbrain and rostral hindbrain), and persists through about stage
CC 15. Strongly expressed in the ectoderm and around the otic placodes at
CC stage 12. At stage 16, otic expression declines, expression in
CC epibranchial placodes begins and peaks at stage 20. Expression in the
CC lens of the eye is first seen at about stage 15, more evident at stage
CC 16. At stage 17, seen in the ectoderm and mesenchyme of the limb
CC primordia. Detected at stage 20 in the lip of the optic cup, in the
CC mesenchyme surrounding the eye, in the ectoderm overlying the lens and
CC in the ectoderm caudal and ventral of the olfactory placodes. From
CC stages 20-30, expressed in cartilage and in the dermomyotomes and
CC migrating sclerotomal cells forming vertebrae.
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; AF031830; AAB87968.1; -; mRNA.
DR EMBL; AF224314; AAF61094.1; -; mRNA.
DR RefSeq; NP_001025508.1; NM_001030337.1.
DR AlphaFoldDB; O57328; -.
DR SMR; O57328; -.
DR STRING; 9031.ENSGALP00000014736; -.
DR PaxDb; O57328; -.
DR PRIDE; O57328; -.
DR GeneID; 374062; -.
DR KEGG; gga:374062; -.
DR CTD; 8321; -.
DR VEuPathDB; HostDB:geneid_374062; -.
DR eggNOG; KOG3577; Eukaryota.
DR InParanoid; O57328; -.
DR OrthoDB; 330751at2759; -.
DR PhylomeDB; O57328; -.
DR PRO; PR:O57328; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_TM.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR026550; FZD1/2.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF34; PTHR11309:SF34; 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;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..48
FT /evidence="ECO:0000255"
FT CHAIN 49..592
FT /note="Frizzled-1"
FT /id="PRO_0000012976"
FT TOPO_DOM 49..271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..351
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..546
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 65..184
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 570..575
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 590..592
FT /note="PDZ-binding"
FT COMPBIAS 186..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 78..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 115..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 141..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 145..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 592 AA; 65491 MW; 933E76063CA6109D CRC64;
MAERRGPAGG GSGEVGGGRR AGGDRCPRRP PALPLLLLLW AAALPAGGQP AAQPAALSER
GISIPDHGYC QPISIPLCTD IAYNQTIMPN LLGHTNQEDA GLEVHQFYPL VKVQCSAELK
FFLCSMYAPV CTVLEQALPP CRSLCERARQ GCEALMNKFG FQWPDTLRCE KFPVHGAGEL
CVGQNASERG TPTPALRPES WTSNPHRGGG AGGSGPGEAR GRFSCPRALK VPSYLNYRFL
GEKDCGAPCE PGRLYGLMYF GPEELRFSRT WIGIWSVLCC ASTLFTVLTY LVDMKRFSYP
ERPIIFLSGC YTAVAVAYIA GFLLEERVVC NERFAEDGSR TVAQGTKREG CTILFMMLYF
FGMASSIWWV ILSLTWFLAA GMKWGHEAIE ANSQYFHLAA WAVPAIKTIT ILALGQVDGD
VLSGVCFVGI NNVDALRGFV LAPLFVYLFI GTSFLLAGFV SLFRIRTIMK HDGTKTEKLE
KLMVRIGIFS VLYTVPATIV IACYFYEQAF REQWERSWVT QSCKSYAIPC PNNHSSHHPP
MSPDFTVFMI KYLMTLIVGI TSGFWIWSGK TLNSWRKFYT RLTNSKQGET TV
