FZ10A_XENLA
ID FZ10A_XENLA Reviewed; 586 AA.
AC Q9DEB5;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Frizzled-10-A;
DE Short=Fz-10A;
DE Short=Xfz10-A;
DE Flags: Precursor;
GN Name=fzd10-a; Synonyms=fz10a;
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=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, stomach,
CC kidney, eye, skeletal muscle and skin.
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; AB046534; BAB19017.1; -; mRNA.
DR RefSeq; NP_001080925.1; NM_001087456.1.
DR AlphaFoldDB; Q9DEB5; -.
DR SMR; Q9DEB5; -.
DR GeneID; 387604; -.
DR KEGG; xla:387604; -.
DR CTD; 387604; -.
DR Xenbase; XB-GENE-865370; fzd10.L.
DR OrthoDB; 509772at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 387604; Expressed in liver and 15 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 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 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..586
FT /note="Frizzled-10-A"
FT /id="PRO_0000013008"
FT TOPO_DOM 27..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..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..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..156
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 161..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 531..536
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 584..586
FT /note="PDZ-binding"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 48..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 85..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 112..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 116..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 586 AA; 65579 MW; A71B5BEF5BDCCEA5 CRC64;
MDVSGVTGLL RGTALLLVLA AALCSAISSI NPDRSGDGRC QAIEIPMCKD IGYNMTRMPN
LMGHENQKEA AIQLHEFAPL VEYGCHSHLK FFLCSLYAPM CTEQVSTPIP ACRVMCEQAR
LKCSPIMEQF NFKWPDSLDC SKLPNKNDPN YLCMEAPNNG TDETPRGSSM LPPIFRPQRP
SSGHEIYPKD PTSRSSCENS GKFHHVEKSA SCAPLCSSSV DVYWSKDDKK FAFIWIAIWS
ILCFFSSAFT VLTFLVDPLR FKYPERPIIF LSMCYCVYSV GYIIRLFAGA DSIACDRDSG
QLYVIQEGLE STGCTIVFLI LYYFGMASSL WWVILTLTWF LAAGKKWGHE AIEANSSYFH
LAAWAIPAVK TIMILVMRRV AGDELTGVCY VGSMDVNALT GFVLIPLACY LIIGTSFILS
GFVALFHIRR VMKTGGENTD KLEKLMVRIG VFSVLYTVPA TCVIACYFYE RLNMDFWKIL
ATQDKCKMDS QTKTLDCTMT SSIPAVEIFM VKIFMLLVVG ITSGMWIWTS KTVQSWQNVF
SKRLKKRNRS KPASVITSAG IYKKPQHPPK VHHGKYESAL QSPTCV
