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Protein

Frizzled-7

Gene

FZD7

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 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
  2. Wnt-activated receptor activity Source: InterPro

GO - Biological processi

  1. multicellular organismal development Source: UniProtKB-KW
  2. 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

Protein family/group databases

MEROPSiI93.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Frizzled-7
Short name:
Fz-7
Short name:
cFz-7
Gene namesi
Name:FZD7
Synonyms:FZ7
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Membrane By similarity; Multi-pass membrane protein By similarity. Cell membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 250219ExtracellularSequence AnalysisAdd
BLAST
Transmembranei251 – 27121Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini272 – 28211CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei283 – 30321Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini304 – 33027ExtracellularSequence AnalysisAdd
BLAST
Transmembranei331 – 35121Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini352 – 37322CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei374 – 39421Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini395 – 41723ExtracellularSequence AnalysisAdd
BLAST
Transmembranei418 – 43821Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini439 – 46426CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei465 – 48521Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini486 – 52136ExtracellularSequence AnalysisAdd
BLAST
Transmembranei522 – 54221Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini543 – 56725CytoplasmicSequence 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 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 567536Frizzled-7PRO_0000012998Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 ↔ 108PROSITE-ProRule annotation
Disulfide bondi55 ↔ 101PROSITE-ProRule annotation
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi92 ↔ 129PROSITE-ProRule annotation
Disulfide bondi118 ↔ 158PROSITE-ProRule annotation
Disulfide bondi122 ↔ 146PROSITE-ProRule annotation
Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO57329.

Expressioni

Tissue specificityi

Expressed broadly in cranial ectoderm. Also expressed in the developing somites and in other cranial placodes, including the olfactory, lens, otic placodes (lateral half of the vesicle) and epibranchial placodes. Low level of expression in all the mesoderm derivatives in the limb buds.

Developmental stagei

First detected as stage 6 in the forming neural tube and somites, but not in trunk surface ectoderm. By stage 8, expression persists in the cranial ectoderm and is up-regulated in the presomptive olfactory placodes. By stages 11-12, expression declines in the neural tube, but not in the cranial ectoderm; in somites, expressed all along the rostral-caudal axis as well as in presegmental mesenchyme caudal to the developing somites. Lens and otic placode expression first visible at stage 12, strongest at stages 13-16. Detected uniformly in ectoderm and mesenchyme of the limb primordia at stage 17. By stage 18, decrease of ectodermal, otic, lens and olfactory placode expression; expression appears in the epibranchial placodes. By stages 22-30, highest levels in the most distal mesoderm of the autopod, in the ventricular zone of the neural tube from the forebrain to the spinal cord, in the dermomyotomes and the tail buds.

Structurei

3D structure databases

ProteinModelPortaliO57329.
SMRiO57329. Positions 45-162.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 161120FZPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi545 – 5506Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity
Motifi565 – 5673PDZ-binding

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

eggNOGiNOG257258.
HOGENOMiHOG000233237.
HOVERGENiHBG006977.
InParanoidiO57329.
KOiK02432.
PhylomeDBiO57329.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026552. FZD7.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF31. PTHR11309:SF31. 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.

O57329-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRPAAGEAGA GLRWLGLAAL LAALLGTPCA AAHHEDKAIS VPDHGFCQPI
60 70 80 90 100
SIPLCTDIAY NQTILPNLLG HTNQEDAGLE VHQFYPLVKV QCSAELKFFL
110 120 130 140 150
CSMYAPVCTV LEQAIPPCRS LCERARQGCE ALMNKFGFQW PERLRCENFP
160 170 180 190 200
VHGAGEICVG QNTSDAPPGP GGAGGRGATA QPTAGYLPDL LTPPQPAAGF
210 220 230 240 250
SFSCPRQLKV PPYLGYRFLG ERDCGAPCEP GRPNGLMYFK EAEVRFARLW
260 270 280 290 300
VGVWSVLCCA STLFTVLTYL VDMRRFSYPE RPIIFLSGCY FMVAVAYAAG
310 320 330 340 350
FLLEERVVCL ERFSEDGYRT VAQGTKKEGC TILFMILYFF GMASSIWWVI
360 370 380 390 400
LSLTWFLAAG MKWGHEAIEA NSQYFHLAAW AVPAVKTITI LAMGQVDGDV
410 420 430 440 450
LSGVCYVGIY SVDSLRGFVL APLFVYLFIG TSFLLAGFVS LFRIRTIMKH
460 470 480 490 500
DGTKTEKLEK LMVRIGVFSV LYTVPATIVV ACYFYEQAFR STWEKTWLLQ
510 520 530 540 550
TCKTYAVPCP SHFAPMSPDF TVFMIKYLMT MIVGITTGFW IWSGKTLQSW
560
RRFYHRLSTG SKGETAV
Length:567
Mass (Da):62,811
Last modified:June 1, 1998 - v1
Checksum:i3EFF0381FC899BC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 352HE → QD in AAF61097. (PubMed:10781956)Curated
Sequence conflicti480 – 4801V → L in AAF61097. (PubMed:10781956)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031831 mRNA. Translation: AAB87969.1.
AF224317 mRNA. Translation: AAF61097.1.
RefSeqiNP_989552.1. NM_204221.2.
UniGeneiGga.110.

Genome annotation databases

GeneIDi374060.
KEGGigga:374060.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031831 mRNA. Translation: AAB87969.1.
AF224317 mRNA. Translation: AAF61097.1.
RefSeqiNP_989552.1. NM_204221.2.
UniGeneiGga.110.

3D structure databases

ProteinModelPortaliO57329.
SMRiO57329. Positions 45-162.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI93.001.
GPCRDBiSearch...

Proteomic databases

PaxDbiO57329.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi374060.
KEGGigga:374060.

Organism-specific databases

CTDi8324.

Phylogenomic databases

eggNOGiNOG257258.
HOGENOMiHOG000233237.
HOVERGENiHBG006977.
InParanoidiO57329.
KOiK02432.
PhylomeDBiO57329.

Miscellaneous databases

NextBioi20813582.
PROiO57329.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026552. FZD7.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF31. PTHR11309:SF31. 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. "Expression of Wnt and Frizzled genes during chick limb bud development."
    Kengaku M., Twombly V., Tabin C.
    Cold Spring Harb. Symp. Quant. Biol. 62:421-429(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Limb bud.
  2. "Characterization of avian frizzled genes in cranial placode development."
    Stark M.R., Biggs J.J., Schoenwolf G.C., Rao M.S.
    Mech. Dev. 93:195-200(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiFZD7_CHICK
AccessioniPrimary (citable) accession number: O57329
Secondary accession number(s): Q9IA04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: June 1, 1998
Last modified: February 4, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.