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Protein

Frizzled-5

Gene

fzd5

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.

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: UniProtKB-KW

GO - Biological processi

  1. camera-type eye development Source: AgBase
  2. neuron development Source: AgBase
  3. regulation of cell differentiation Source: AgBase
  4. regulation of cell proliferation Source: AgBase
  5. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Frizzled-5
Short name:
Fz-5
Short name:
Xfz5
Gene namesi
Name:fzd5
Synonyms:fz5
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865299. fzd5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 220194ExtracellularSequence AnalysisAdd
BLAST
Transmembranei221 – 24121Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini242 – 25716CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei258 – 27821Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini279 – 30123ExtracellularSequence AnalysisAdd
BLAST
Transmembranei302 – 32221Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini323 – 34321CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei344 – 36421Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini365 – 38723ExtracellularSequence AnalysisAdd
BLAST
Transmembranei388 – 40821Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini409 – 43426CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei435 – 45521Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini456 – 48328ExtracellularSequence AnalysisAdd
BLAST
Transmembranei484 – 50421Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini505 – 55955CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 559533Frizzled-5PRO_0000012992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 94PROSITE-ProRule annotation
Disulfide bondi41 ↔ 87PROSITE-ProRule annotation
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi78 ↔ 116PROSITE-ProRule annotation
Disulfide bondi105 ↔ 146PROSITE-ProRule annotation
Disulfide bondi109 ↔ 133PROSITE-ProRule annotation
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed in retina.

Developmental stagei

First detected at the late neurula stage in retinal primordia. Throughout the tailbud stage, expressed exclusively in the neural retina within the optic vesicles. During tadpole stage, expression becomes restricted to the ciliary marginal zone.

Structurei

3D structure databases

ProteinModelPortaliP58421.
SMRiP58421. Positions 31-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 149122FZPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi507 – 5126Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity
Motifi557 – 5593PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi152 – 1576Poly-Thr

Domaini

Lys-Thr-X-X-X-Trp motif interacts with the PDZ doman 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

Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG006977.
KOiK02375.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PfamiPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSiPR00489. FRIZZLED.
SMARTiSM00063. FRI. 1 hit.
[Graphical view]
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P58421-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSFRSGVFA LSFVVLLLDY FAPAQAASKA IVCQEITVPM CKGIGYNHTY
60 70 80 90 100
MPNQFNHDTQ DEAGMEVHQF WPLVVIQCSL DLKFFLCSMY TPICLPDYRK
110 120 130 140 150
PLPPCRSVCE RAKAGCSPLM RKYGFAWPER MNCDRLPEHG DPDTLCMYYN
160 170 180 190 200
WTETTTTLPP THPPKVKTPT SDCDGVCKCR EPFVSITRES HPLYNRIKTG
210 220 230 240 250
QVPNCAMPCF QPYFTQDEKM FVTFWIGLWS ILCFISTFTT VATFLIDMER
260 270 280 290 300
FRYPERPIIF LSACYLFVSI GYVVRLIVGH ENVACNKDHI HYETTGPALC
310 320 330 340 350
TIVFLLIYFF GMASSIWWVI LTFTWFLAAG MKWGNEAIAS YSQYFHMAAW
360 370 380 390 400
LIPSVKSIAV LALSSVDGDP VAGICYVGNQ NLDNLRGFVL APLVVYLFSG
410 420 430 440 450
TMFLLAGFVS LFRIRSVIKQ GGTKTDKLEK LMIRIGIFSV LYTVPATIVV
460 470 480 490 500
ACYIYEQHYR EHWEKTHNCS CPGDKQRYRP DYAVFMLKYL MCLVVGITSG
510 520 530 540 550
VWIWSGKTLE SWKRFTGRCC RNSKPINASA YSEASRALTP RTGLSNLTLP

HKQVPLSHV
Length:559
Mass (Da):63,518
Last modified:December 4, 2001 - v1
Checksum:i581EB243FCB954B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300716 mRNA. Translation: AAK51688.1.
RefSeqiNP_001079217.1. NM_001085748.1.
UniGeneiXl.11966.

Genome annotation databases

GeneIDi373834.
KEGGixla:373834.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300716 mRNA. Translation: AAK51688.1.
RefSeqiNP_001079217.1. NM_001085748.1.
UniGeneiXl.11966.

3D structure databases

ProteinModelPortaliP58421.
SMRiP58421. Positions 31-149.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

GPCRDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi373834.
KEGGixla:373834.

Organism-specific databases

CTDi7855.
XenbaseiXB-GENE-865299. fzd5.

Phylogenomic databases

HOVERGENiHBG006977.
KOiK02375.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PfamiPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSiPR00489. FRIZZLED.
SMARTiSM00063. FRI. 1 hit.
[Graphical view]
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Xenopus frizzled-5: a frizzled family member expressed exclusively in the neural retina of the developing eye."
    Sumanas S., Ekker S.C.
    Mech. Dev. 103:133-136(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiFZD5_XENLA
AccessioniPrimary (citable) accession number: P58421
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2001
Last sequence update: December 4, 2001
Last modified: January 6, 2015
This is version 82 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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 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.