FZ10B_XENLA
ID FZ10B_XENLA Reviewed; 580 AA.
AC Q9W742;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Frizzled-10-B;
DE Short=Fz-10B;
DE Short=Xfz10-B;
DE AltName: Full=Frizzled-9;
DE Short=Fz-9;
DE Short=Xfz9;
DE Flags: Precursor;
GN Name=fzd10-b; Synonyms=fz10b, fz9;
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].
RX PubMed=10446283; DOI=10.1016/s0925-4773(99)00117-3;
RA Wheeler G.N., Hoppler S.;
RT "Two novel Xenopus frizzled genes expressed in developing heart and
RT brain.";
RL Mech. Dev. 86:203-207(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=11097845; DOI=10.1006/bbrc.2000.3808;
RA Moriwaki J., Kajita E., Kirikoshi H., Koike J., Sagara N., Yasuhiko Y.,
RA Saitoh T., Hirai M., Katoh M., Shiokawa K.;
RT "Isolation of Xenopus frizzled-10A and frizzled-10B genomic clones and
RT their expression in adult tissues and embryos.";
RL Biochem. Biophys. Res. Commun. 278:377-384(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. Activated by Wnt8.
CC Could have an antagonizing activity in the morphogenesis during
CC development.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, lung, brain, testis, heart and
CC ovary.
CC -!- DEVELOPMENTAL STAGE: Expressed from blastula stage, peak expression at
CC late gastrula stage. Expression localizes in neural fold at neurula
CC stage; in the dorsal region of midbrain, hindbrain and spinal cord at
CC tadpole stage.
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; AF159107; AAD44332.1; -; mRNA.
DR EMBL; AB046535; BAB19018.1; -; mRNA.
DR RefSeq; NP_001080926.1; NM_001087457.1.
DR AlphaFoldDB; Q9W742; -.
DR SMR; Q9W742; -.
DR DNASU; 387605; -.
DR GeneID; 387605; -.
DR KEGG; xla:387605; -.
DR CTD; 387605; -.
DR Xenbase; XB-GENE-6253606; fzd10.S.
DR OMA; YVGNQDI; -.
DR OrthoDB; 509772at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 387605; Expressed in pancreas and 16 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042813; F:Wnt receptor activity; IEA:InterPro.
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; IPR026549; FZD10.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF86; PTHR11309:SF86; 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 Calcium; Cell membrane; Developmental protein; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Metal-binding;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..580
FT /note="Frizzled-10-B"
FT /id="PRO_0000013009"
FT TOPO_DOM 21..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..501
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..150
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 173..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 525..530
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 578..580
FT /note="PDZ-binding"
FT COMPBIAS 177..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 48
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 34..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 42..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 79..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 106..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 110..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 580 AA; 65106 MW; E404658CECD76697 CRC64;
MEPRVVTALL LSLAAALCSG ISSINPDRSG EGRCQAIEIP MCKDIGYNMT RMPNLMGHEN
QKEAAIQLHE FAPLVEYGCH SHLKFFLCSL YAPMCTEQVS TPIPACRVMC EQARLKCSPI
MEQFNFKWPD SLDCSKLPNK NDPNYLCMEA PNNGTDEAPR SSSILPPIFR PQRPNSGHEM
YPKDPKGRSS CENSGKFHHV EKSASCAPLC SSSVDVYWSK NDKKFAFIWI AIWSLLCFFS
SAFTVLTFLV DPLRFKYPER PIIFLSMCYC VYSVGYIIRL FAGADSIACD RDSGQLYVIQ
EGLESTGCTI VFLILYYFGM ASSLWWVILT LTWFLAAGKK WGHEAIEANS SYFHLAAWAI
PAVKTIMILV MRRVAGDELT GVCYVGSMDV NALTGFVLIP LACYLIIGTS FILSGFVALF
HIRRVMKTGG ENTDKLEKLM VRIGVFSVLY TVPATCVIAC YFYERLNMDF WKILATQDKC
KMDSQTKTLD CTMTSSIPAV EIFMVKIFML LVVGITSGMW IWTSKTVQSW QNVFSKSLKK
RNRNKPASVI TSAGIYKKPQ QPPKIHHGKY ESALRSPTCV
