FZD2_XENLA
ID FZD2_XENLA Reviewed; 551 AA.
AC Q9PUU6; Q2TAR6;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Frizzled-2;
DE Short=Fz-2;
DE Short=Xfz2;
DE Flags: Precursor;
GN Name=fzd2; Synonyms=fz2;
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].
RC TISSUE=Head;
RX PubMed=10495293; DOI=10.1016/s0925-4773(99)00161-6;
RA Deardorff M.A., Klein P.S.;
RT "Xenopus frizzled-2 is expressed highly in the developing eye, otic vesicle
RT and somites.";
RL Mech. Dev. 87:229-233(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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: Membrane; Multi-pass membrane protein. Cell
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed, especially in the eye anlage,
CC otic vesicle and developing somites.
CC -!- DEVELOPMENTAL STAGE: Minimal expression in oocytes and embryos prior to
CC mid-blastula transition. Readily detected in the presomitic tissue from
CC late gastrulae. By neurula stages, somitic expression is broader and
CC also appears in developing neural structures and other anterior
CC structures (eye anlage). By late neurula, the posterior expression is
CC condensed into two stripes on each side, expression in the anterior
CC tissues remains high in the developing eye. During tailbud stages,
CC expression is still high in the eye vesicle, otic vesicle and other
CC anterior regions, as well as the presomitic mesoderm. In the tadpole,
CC highly expressed in the head, eye and otic vesicle, branchial arches
CC and midportion of the somites.
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; AF139165; AAF06359.1; -; mRNA.
DR EMBL; BC110756; AAI10757.1; -; mRNA.
DR RefSeq; NP_001083829.1; NM_001090360.1.
DR AlphaFoldDB; Q9PUU6; -.
DR SMR; Q9PUU6; -.
DR DNASU; 399141; -.
DR GeneID; 399141; -.
DR KEGG; xla:399141; -.
DR CTD; 399141; -.
DR Xenbase; XB-GENE-865666; fzd2.S.
DR OMA; CEHYRSS; -.
DR OrthoDB; 330751at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 399141; Expressed in internal ear and 19 other tissues.
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; 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; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..551
FT /note="Frizzled-2"
FT /id="PRO_0000012981"
FT TOPO_DOM 27..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..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..400
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..505
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..152
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT MOTIF 529..534
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 549..551
FT /note="PDZ-binding"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 46..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 83..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 109..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 113..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 551 AA; 62462 MW; 3F29F16B8EE6E007 CRC64;
MQGVTRASIL LIIYHLFTLS LGQLHGEKGI SVPEHGFCQP ISIPLCTDIA YNQTIMPNLL
GHTNQEDAGL EVHQFYPLVK VQCSSELRFF LCSMYAPVCT VLEQAIPPCR SICERARHGC
EALMNKFGFQ WPERLRCENF PRHGAEQICV GQNHSEDGGP TLLTTSPPHH GTPGPPIYAT
LDHPFHCPRV LKVPSYLNYR FLGEKDCAAP CEPTKSDGFM FFSQDEIRFA RIWILIWSVL
CCASTFITVT TYLVDMQRFR YPERPIIFLS GCYTMVSVAY IAGFVLGDKV VCNEGFSEDG
YKTVVQGTKK EGCTILFMML YFFSMASSIW WVILSLTWFL AAGMKWGHEA IEANSQYFHL
AAWAVPAVKT ITILAMGQID GDLLSGVCFV GLNNIDPLRG FVLAPLFVYL FIGTSFLLAG
FVSLFRIRTI MKHDGTKTEK LERLMVRIGV FSVLYTVPAT IVIACYFYEQ AFREHWERSW
VSQNCKSLAI PCPLQYTPRM TPDFTVYMIK YLMTLIVGIT SGFWIWSGKT LHSWRKFYTR
LTNSKHGETT V
