UniProtKB - O93274 (FZD8_XENLA)
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Protein
Frizzled-8
Gene
fzd8
Organism
Xenopus laevis (African clawed frog)
Status
Functioni
Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Activation by Wnt8, Wnt5A or Wnt3A induces expression of beta-catenin target genes. Displays an axis-inducing activity.1 Publication
GO - Molecular functioni
- G-protein coupled receptor activity Source: UniProtKB-KW
GO - Biological processi
- canonical Wnt signaling pathway Source: BHF-UCL
- multicellular organism development Source: UniProtKB-KW
- positive regulation of DNA binding transcription factor activity Source: BHF-UCL
Keywordsi
Molecular function | Developmental protein, G-protein coupled receptor, Receptor, Transducer |
Biological process | Wnt signaling pathway |
Names & Taxonomyi
Protein namesi | Recommended name: Frizzled-8Short name: Fz-8 Short name: Xfz8 |
Gene namesi | Name:fzd8 Synonyms:fz8 |
Organismi | Xenopus laevis (African clawed frog) |
Taxonomic identifieri | 8355 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Organism-specific databases
Xenbasei | XB-GENE-865411. fzd8. |
Subcellular locationi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 24 – 239 | ExtracellularSequence analysisAdd BLAST | 216 | |
Transmembranei | 240 – 260 | Helical; Name=1Sequence analysisAdd BLAST | 21 | |
Topological domaini | 261 – 271 | CytoplasmicSequence analysisAdd BLAST | 11 | |
Transmembranei | 272 – 292 | Helical; Name=2Sequence analysisAdd BLAST | 21 | |
Topological domaini | 293 – 320 | ExtracellularSequence analysisAdd BLAST | 28 | |
Transmembranei | 321 – 341 | Helical; Name=3Sequence analysisAdd BLAST | 21 | |
Topological domaini | 342 – 377 | CytoplasmicSequence analysisAdd BLAST | 36 | |
Transmembranei | 378 – 398 | Helical; Name=4Sequence analysisAdd BLAST | 21 | |
Topological domaini | 399 – 407 | ExtracellularSequence analysis | 9 | |
Transmembranei | 408 – 428 | Helical; Name=5Sequence analysisAdd BLAST | 21 | |
Topological domaini | 429 – 454 | CytoplasmicSequence analysisAdd BLAST | 26 | |
Transmembranei | 455 – 475 | Helical; Name=6Sequence analysisAdd BLAST | 21 | |
Topological domaini | 476 – 505 | ExtracellularSequence analysisAdd BLAST | 30 | |
Transmembranei | 506 – 526 | Helical; Name=7Sequence analysisAdd BLAST | 21 | |
Topological domaini | 527 – 581 | CytoplasmicSequence analysisAdd BLAST | 55 |
Keywords - Cellular componenti
Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 23 | Sequence analysisAdd BLAST | 23 | |
ChainiPRO_0000013002 | 24 – 581 | Frizzled-8Add BLAST | 558 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 28 ↔ 89 | PROSITE-ProRule annotation | ||
Disulfide bondi | 36 ↔ 82 | PROSITE-ProRule annotation | ||
Glycosylationi | 42 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 73 ↔ 111 | PROSITE-ProRule annotation | ||
Disulfide bondi | 100 ↔ 141 | PROSITE-ProRule annotation | ||
Disulfide bondi | 104 ↔ 128 | PROSITE-ProRule annotation | ||
Glycosylationi | 146 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Keywords - PTMi
Disulfide bond, GlycoproteinExpressioni
Developmental stagei
First expressed at high levels in the late blastula stages. At early gastrula, expressed in the deep cells of the Spemann organizer prior to involution of the dorsal blastopore lip. Detected in presumptive neurectoderm as gastrulation proceeds. Becomes restricted to the anterior ectoderm by the end of gastrulation. At neurula stages, localized in the most anterior region of the embryo, mainly in the anterior ectoderm including telencephalic and cement gland regions.
Interactioni
Subunit structurei
Interacts with lypd6 and the interaction is strongly enhanced by wnt3a (PubMed:23987510).1 Publication
Binary interactionsi
With | Entry | #Exp. | IntAct | Notes |
---|---|---|---|---|
FRIED | Q6EHH9 | 2 | EBI-7735236,EBI-7735259 |
Protein-protein interaction databases
IntActi | O93274. 1 interactor. |
MINTi | O93274. |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 24 – 144 | FZPROSITE-ProRule annotationAdd BLAST | 121 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 64 – 71 | Palmitate-binding grooveBy similarity | 8 | |
Regioni | 88 – 93 | Wnt-bindingBy similarity | 6 | |
Regioni | 140 – 146 | Wnt-bindingBy similarity | 7 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 529 – 534 | Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity | 6 | |
Motifi | 579 – 581 | PDZ-binding | 3 |
Domaini
Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.By similarity
The FZ domain is involved in binding with Wnt ligands.By similarity
Sequence similaritiesi
Belongs to the G-protein coupled receptor Fz/Smo family.Curated
Keywords - Domaini
Signal, Transmembrane, Transmembrane helixPhylogenomic databases
HOVERGENi | HBG006977. |
KOi | K02375. |
Family and domain databases
Gene3Di | 1.10.2000.10. 1 hit. |
InterProi | View protein in InterPro IPR015526. Frizzled/SFRP. IPR000539. Frizzled/Smoothened_TM. IPR020067. Frizzled_dom. IPR036790. Frizzled_dom_sf. IPR017981. GPCR_2-like. |
PANTHERi | PTHR11309. PTHR11309. 1 hit. |
Pfami | View protein in Pfam PF01534. Frizzled. 1 hit. PF01392. Fz. 1 hit. |
PRINTSi | PR00489. FRIZZLED. |
SMARTi | View protein in SMART SM00063. FRI. 1 hit. SM01330. Frizzled. 1 hit. |
SUPFAMi | SSF63501. SSF63501. 1 hit. |
PROSITEi | View protein in PROSITE PS50038. FZ. 1 hit. PS50261. G_PROTEIN_RECEP_F2_4. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O93274-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MESLSLSLLL LVSWLQGSQC AAAKELSCQE ITVPLCKDIG YNYTYMPNQF
60 70 80 90 100
NHDTQDEAGM EVHQFWPLVV IHCSPDLKFF LCSMYTPICL EDYKKPLPPC
110 120 130 140 150
RSVCERARAG CAPLMRQYGF AWPDRMRCDR LPEQGNPDTL CMDYYNRTEQ
160 170 180 190 200
TTAAPSHPEP PKPPARSVPK GRTRVEPPRS RSRATGCESG CQCRAPMVQV
210 220 230 240 250
SNERHPLYNR VRTGQIPNCA MPCHNPFFSP EERTFTEFWI GLWSVLCFAS
260 270 280 290 300
TFATVSTFLI DMERFKYPER PIIFLSACYL LVSTGYLIRL IAGHEKVACS
310 320 330 340 350
RGELDLEHII HYETTGPALC TLVFLLIYFF GMASSIWWVI LSLTWFLAAG
360 370 380 390 400
MKWGNEAIAG YSQYFHLAAW LVPSIKSIAV LALSSVDGDP VAGICFVGNQ
410 420 430 440 450
NLDNLRGFVL APLVIYLFIG SMFLLAGFVS LFRIRSVIKQ GGTKTDKLEK
460 470 480 490 500
LMIRIGIFSV LYTVPATIVV ACFFYEQHNR QGWEVAHNCN SCQPEMAQPH
510 520 530 540 550
RPDYAVFMLK YFMCLVVGIT SGVWIWSGKT LESWRAFCTR CCWGSKATGG
560 570 580
SMYSDVSTGL TWRSGTGSSV SCPKQMPLSQ V
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 1 – 3 | MES → MECPY (PubMed:9636083).Curated | 3 | |
Sequence conflicti | 7 | S → L in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 10 | L → V in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 14 | W → G in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 20 | C → S in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 135 | G → S in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 171 | G → S in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 175 | V → A in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 185 | T → P in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 216 | I → T in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 237 | E → D in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 494 – 496 | PEM → SEG in AAC77361 (PubMed:9636083).Curated | 3 | |
Sequence conflicti | 500 | H → R in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 547 | A → T in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 565 | G → A in AAC77361 (PubMed:9636083).Curated | 1 | |
Sequence conflicti | 572 | C → Y in AAC77361 (PubMed:9636083).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF017177 mRNA. Translation: AAC31121.1. AF033110 mRNA. Translation: AAC77361.1. |
RefSeqi | NP_001079144.1. NM_001085675.1. NP_001084206.1. NM_001090737.1. |
UniGenei | Xl.293. Xl.412. |
Genome annotation databases
GeneIDi | 373690. 399367. |
KEGGi | xla:373690. xla:399367. |
Similar proteinsi
Entry informationi
Entry namei | FZD8_XENLA | |
Accessioni | O93274Primary (citable) accession number: O93274 Secondary accession number(s): Q9YI55 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 5, 2001 |
Last sequence update: | November 1, 1998 | |
Last modified: | February 28, 2018 | |
This is version 114 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |