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UniProtKB - O93274 (FZD8_XENLA)

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Protein

Frizzled-8

Gene

fzd8

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionDevelopmental protein, G-protein coupled receptor, Receptor, Transducer
Biological processWnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Frizzled-8
Short name:
Fz-8
Short name:
Xfz8
Gene namesi
Name:fzd8
Synonyms:fz8
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Organism-specific databases

XenbaseiXB-GENE-865411. fzd8.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 239ExtracellularSequence analysisAdd BLAST216
Transmembranei240 – 260Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini261 – 271CytoplasmicSequence analysisAdd BLAST11
Transmembranei272 – 292Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini293 – 320ExtracellularSequence analysisAdd BLAST28
Transmembranei321 – 341Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini342 – 377CytoplasmicSequence analysisAdd BLAST36
Transmembranei378 – 398Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini399 – 407ExtracellularSequence analysis9
Transmembranei408 – 428Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini429 – 454CytoplasmicSequence analysisAdd BLAST26
Transmembranei455 – 475Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini476 – 505ExtracellularSequence analysisAdd BLAST30
Transmembranei506 – 526Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini527 – 581CytoplasmicSequence analysisAdd BLAST55

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000001300224 – 581Frizzled-8Add BLAST558

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 89PROSITE-ProRule annotation
Disulfide bondi36 ↔ 82PROSITE-ProRule annotation
Glycosylationi42N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi73 ↔ 111PROSITE-ProRule annotation
Disulfide bondi100 ↔ 141PROSITE-ProRule annotation
Disulfide bondi104 ↔ 128PROSITE-ProRule annotation
Glycosylationi146N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

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

WithEntry#Exp.IntActNotes
FRIEDQ6EHH92EBI-7735236,EBI-7735259

Protein-protein interaction databases

IntActiO93274. 1 interactor.
MINTiMINT-1893946.

Structurei

3D structure databases

ProteinModelPortaliO93274.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 144FZPROSITE-ProRule annotationAdd BLAST121

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 71Palmitate-binding grooveBy similarity8
Regioni88 – 93Wnt-bindingBy similarity6
Regioni140 – 146Wnt-bindingBy similarity7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi529 – 534Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity6
Motifi579 – 581PDZ-binding3

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 helix

Phylogenomic databases

HOVERGENiHBG006977.
KOiK02375.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiView protein in InterPro
IPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR017981. GPCR_2-like.
PANTHERiPTHR11309. PTHR11309. 1 hit.
PfamiView protein in Pfam
PF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
PRINTSiPR00489. FRIZZLED.
SMARTiView protein in SMART
SM00063. FRI. 1 hit.
SM01330. Frizzled. 1 hit.
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiView protein in PROSITE
PS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O93274-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:581
Mass (Da):65,379
Last modified:November 1, 1998 - v1
Checksum:i80890C408AB21E23
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 3MES → MECPY (PubMed:9636083).Curated3
Sequence conflicti7S → L in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti10L → V in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti14W → G in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti20C → S in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti135G → S in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti171G → S in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti175V → A in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti185T → P in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti216I → T in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti237E → D in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti494 – 496PEM → SEG in AAC77361 (PubMed:9636083).Curated3
Sequence conflicti500H → R in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti547A → T in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti565G → A in AAC77361 (PubMed:9636083).Curated1
Sequence conflicti572C → Y in AAC77361 (PubMed:9636083).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017177 mRNA. Translation: AAC31121.1.
AF033110 mRNA. Translation: AAC77361.1.
RefSeqiNP_001079144.1. NM_001085675.1.
NP_001084206.1. NM_001090737.1.
UniGeneiXl.293.
Xl.412.

Genome annotation databases

GeneIDi373690.
399367.
KEGGixla:373690.
xla:399367.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017177 mRNA. Translation: AAC31121.1.
AF033110 mRNA. Translation: AAC77361.1.
RefSeqiNP_001079144.1. NM_001085675.1.
NP_001084206.1. NM_001090737.1.
UniGeneiXl.293.
Xl.412.

3D structure databases

ProteinModelPortaliO93274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO93274. 1 interactor.
MINTiMINT-1893946.

Protein family/group databases

GPCRDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi373690.
399367.
KEGGixla:373690.
xla:399367.

Organism-specific databases

CTDi373690.
399367.
XenbaseiXB-GENE-865411. fzd8.

Phylogenomic databases

HOVERGENiHBG006977.
KOiK02375.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiView protein in InterPro
IPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR017981. GPCR_2-like.
PANTHERiPTHR11309. PTHR11309. 1 hit.
PfamiView protein in Pfam
PF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
PRINTSiPR00489. FRIZZLED.
SMARTiView protein in SMART
SM00063. FRI. 1 hit.
SM01330. Frizzled. 1 hit.
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiView protein in PROSITE
PS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFZD8_XENLA
AccessioniPrimary (citable) accession number: O93274
Secondary accession number(s): Q9YI55
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: November 1, 1998
Last modified: May 10, 2017
This is version 110 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.