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Protein

Frizzled-4

Gene

fzd4

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. Activated by Wnt5A.

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Frizzled-4
Short name:
Fz-4
Short name:
Xfz4
Gene namesi
Name:fzd4
Synonyms:fz4
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865153. fzd4.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 208ExtracellularSequence analysisAdd BLAST186
Transmembranei209 – 229Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini230 – 240CytoplasmicSequence analysisAdd BLAST11
Transmembranei241 – 261Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini262 – 288ExtracellularSequence analysisAdd BLAST27
Transmembranei289 – 309Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini310 – 330CytoplasmicSequence analysisAdd BLAST21
Transmembranei331 – 351Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini352 – 375ExtracellularSequence analysisAdd BLAST24
Transmembranei376 – 396Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini397 – 422CytoplasmicSequence analysisAdd BLAST26
Transmembranei423 – 443Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini444 – 463ExtracellularSequence analysisAdd BLAST20
Transmembranei464 – 484Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini485 – 523CytoplasmicSequence analysisAdd BLAST39

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000001298923 – 523Frizzled-4Add BLAST501

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 92PROSITE-ProRule annotation
Disulfide bondi39 ↔ 85PROSITE-ProRule annotation
Glycosylationi45N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi76 ↔ 114PROSITE-ProRule annotation
Disulfide bondi103 ↔ 144PROSITE-ProRule annotation
Disulfide bondi107 ↔ 131PROSITE-ProRule annotation
Glycosylationi130N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Developmental stagei

Expression level remains constant during early development. First localized during gastrulation to the dorsal presumptive neuroectoderm. At the end of gastrulation, detected in the dorso-anterior neuroectoderm. During neurulation, expressed as a band on both sides of the forebrain, and in the trunk lateral plate mesoderm. As development proceeds, expression in the trunk lateral plate mesoderm decreases but persists in the forebrain. Also expressed in the posterior unsegmented somitic mesoderm from late tail-bud stage onward.

Interactioni

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliQ9PT62.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 147FZPROSITE-ProRule annotationAdd BLAST122

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi485 – 490Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity6
Motifi521 – 523PDZ-binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi25 – 28Poly-Glu4

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.
The FZ domain is involved in binding with Wnt ligands.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG006977.
KOiK02354.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiView protein in InterPro
IPR015526. Frizzled/SFRP.
IPR000539. Frizzled/Smoothened_TM.
IPR020067. Frizzled_dom.
IPR036790. Frizzled_dom_sf.
IPR026551. FZD4.
IPR017981. GPCR_2-like.
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF23. PTHR11309:SF23. 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.

Q9PT62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGARSLTLLY LLCCLVVGLI AGFGEEEERS CDPIRITMCQ NLGYNVTKMP
60 70 80 90 100
NLVGHELQAD AELQLTTFTP LIQYGCSSQL QFFLCSVYVP MCTEKINIPI
110 120 130 140 150
GPCGGMCLSV KRRCEPVLKE FGFAWPESLN CSKFPPQNDH NHMCMEGPGD
160 170 180 190 200
DEVPAHSKTP VLPGEDCNSF GPNSDQYTWV KRSMNCVLKC GYDSGLYNRL
210 220 230 240 250
SKEFTDIWMA VWASLCFIST AFTVLTFLID SSRFCYPERP IIFLSMCYNI
260 270 280 290 300
YSIAYIVRLT VGRERISCDF EEAAEPVLIQ EGLKNTGCAI IFLLMYFFGM
310 320 330 340 350
ASSIWWVILT LTWFLAAGLK WGHEAIEMHS SYFHIAAWAI PAVKTIVILI
360 370 380 390 400
MRLVDADELT GLCYVGNQNI DALTGFVVAP LFTYLVIGTL FIAAGLVALF
410 420 430 440 450
KIRSNLQKDG TKTDKLERLM VKIGVFSVLY TVPATCVIAC YFYEVSNWNV
460 470 480 490 500
FRYTADDSNM AVEMLNIFMS LLVGITSGMW IWSAKTLHTW QKCTNRLVNS
510 520
GKVKRKKRVD GWVKPGKGNE TVV
Length:523
Mass (Da):58,741
Last modified:May 1, 2000 - v1
Checksum:iACCA8D2AFBFC6105
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ251750 mRNA. Translation: CAB63117.1.
RefSeqiNP_001083922.1. NM_001090453.1.
UniGeneiXl.460.

Genome annotation databases

GeneIDi399192.
KEGGixla:399192.

Similar proteinsi

Entry informationi

Entry nameiFZD4_XENLA
AccessioniPrimary (citable) accession number: Q9PT62
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: May 1, 2000
Last modified: October 25, 2017
This is version 100 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