FZD2_CHICK
ID FZD2_CHICK Reviewed; 523 AA.
AC Q9IA06; Q9PTW4;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Frizzled-2;
DE Short=Fz-2;
DE Short=cFz-2;
DE Flags: Fragment;
GN Name=FZD2; Synonyms=FZ2;
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].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 233-315.
RC TISSUE=Limb bud;
RX PubMed=10512196;
RA Nohno T., Kawakami Y., Wada N., Komaguchi C., Nishimatsu S.;
RT "Differential expression of the frizzled family involved in Wnt signaling
RT during chick limb development.";
RL Cell. Mol. Biol. 45:653-659(1999).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=25759469; DOI=10.1093/hmg/ddv088;
RA Saal H.M., Prows C.A., Guerreiro I., Donlin M., Knudson L., Sund K.L.,
RA Chang C.F., Brugmann S.A., Stottmann R.W.;
RT "A mutation in FRIZZLED2 impairs Wnt signaling and causes autosomal
RT dominant omodysplasia.";
RL Hum. Mol. Genet. 24:3399-3409(2015).
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 genes
CC (By similarity). A second signaling pathway involving PKC and calcium
CC fluxes has been seen for some family members, but it is not yet clear
CC if it 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 {ECO:0000250|UniProtKB:Q14332}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the developing head and limbs
CC (PubMed:25759469). Expressed broadly in cranial ectoderm. Also
CC expressed in the developing somites (dermomyotome) and in other cranial
CC placodes, including the olfactory, lens, and otic placodes (rostral rim
CC of the vesicle). {ECO:0000269|PubMed:25759469}.
CC -!- DEVELOPMENTAL STAGE: At stage 8, faintly expressed in cranial ectoderm
CC and in the somites. At stages 9-10, broadly expressed throughout the
CC cranial ectoderm. By stages 11-12, more robust expression is detected
CC in ectoderm adjacent to the hindbrain, including the otic placodes.
CC Transiently expressed in the lens placode and ectoderm of the head at
CC stages 13-15. Down-regulated in differentiating structures of older
CC embryos.
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; AF224315; AAF61095.1; -; mRNA.
DR EMBL; AB029449; BAA89399.1; -; mRNA.
DR AlphaFoldDB; Q9IA06; -.
DR SMR; Q9IA06; -.
DR STRING; 9031.ENSGALP00000034947; -.
DR PaxDb; Q9IA06; -.
DR VEuPathDB; HostDB:geneid_374061; -.
DR eggNOG; KOG3577; Eukaryota.
DR InParanoid; Q9IA06; -.
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 CDD; cd07464; CRD_FZ2; 1.
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; IPR041778; FZ2_CRD.
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; Transducer; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT CHAIN <1..523
FT /note="Frizzled-2"
FT /id="PRO_0000205975"
FT TOPO_DOM 1..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..372
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..477
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..120
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT MOTIF 501..506
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 521..523
FT /note="PDZ-binding"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 6..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 14..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 51..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 77..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 81..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT NON_TER 1
SQ SEQUENCE 523 AA; 59281 MW; 8547F5B018001CB7 CRC64;
PDHGFCQPIS IPLCTDIAYN QTIMPNLLGH TNQEDAGLEV HQFYPLVKVQ CSLELKFFLC
SMYAPVCTVL EQAIPPCRSI CERARQGCEA LMNKFGFQWP ERLRCENFPR HGAEQICVGQ
NHSEDGGSSA ALLTSAAPPA AHGTPGAPRY ATPDRPFHCP RALKVPGYLN YKFLGEKDCA
APCEPSRPDG HMFFNEDEIR FARVWILVWS VLCCASTFFT VTTYLVDMQR FRYPERPIIF
LSGCYTMVSV AYIAGFVLEE RVVCNERFQE DGYRTVVQGT KKEGCTILFM MLYFFSMASS
IWWVILSLTW FLAAGMKWGH EAIEANSQYF HLAAWAVPAV KTITILAMGQ IDGDLLSGVC
FVGLNGIDPL RGFVLAPLFV YLFIGTSFLL AGFVSLFRIR TIMKHGGTKT EKLERLMVRI
GVFSVLYTVP ATIVIACYFY EQAFRQHWER SWISQHCKSL AIPCPLHFTP RMTPDFTVYM
IKYLMTLIVG ITSGFWIFSG KTLHSWRKFY TRLTNSRQGE TTV
