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Protein

Frizzled-2

Gene

fz2

Organism
Drosophila melanogaster (Fruit fly)
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. Required to coordinate the cytoskeletons of epidermal cells to produce a parallel array of cuticular hairs and bristles.1 Publication

GO - Molecular functioni

  • G-protein coupled receptor activity Source: UniProtKB-KW
  • PDZ domain binding Source: FlyBase
  • transmembrane signaling receptor activity Source: FlyBase
  • Wnt-activated receptor activity Source: FlyBase
  • Wnt-protein binding Source: UniProtKB

GO - Biological processi

  • axon extension Source: FlyBase
  • axon guidance Source: FlyBase
  • cell migration Source: FlyBase
  • chaeta morphogenesis Source: FlyBase
  • female gonad development Source: FlyBase
  • G-protein coupled receptor signaling pathway Source: FlyBase
  • imaginal disc-derived wing margin morphogenesis Source: FlyBase
  • motor neuron axon guidance Source: FlyBase
  • receptor-mediated endocytosis Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • regulation of hemocyte proliferation Source: FlyBase
  • retinal ganglion cell axon guidance Source: FlyBase
  • salivary gland morphogenesis Source: FlyBase
  • signal transduction Source: FlyBase
  • synapse organization Source: FlyBase
  • synaptic target inhibition Source: FlyBase
  • Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

SignaLinkiQ9VVX3.

Protein family/group databases

TCDBi9.A.14.16.2. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Frizzled-2
Short name:
dFz2
Gene namesi
Name:fz2
ORF Names:CG9739
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0016797. fz2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 315293ExtracellularSequence analysisAdd
BLAST
Transmembranei316 – 33621Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini337 – 35216CytoplasmicSequence analysisAdd
BLAST
Transmembranei353 – 37321Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini374 – 39724ExtracellularSequence analysisAdd
BLAST
Transmembranei398 – 41821Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini419 – 43921CytoplasmicSequence analysisAdd
BLAST
Transmembranei440 – 46021Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini461 – 48222ExtracellularSequence analysisAdd
BLAST
Transmembranei483 – 50321Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini504 – 53431CytoplasmicSequence analysisAdd
BLAST
Transmembranei535 – 55521Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini556 – 58429ExtracellularSequence analysisAdd
BLAST
Transmembranei585 – 60521Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini606 – 69489CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endocytic vesicle Source: FlyBase
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: FlyBase
  • nucleus Source: FlyBase
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 694672Frizzled-2PRO_0000013012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi64 ↔ 125PROSITE-ProRule annotation
Disulfide bondi72 ↔ 118PROSITE-ProRule annotation
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence analysis
Disulfide bondi109 ↔ 147PROSITE-ProRule annotation
Disulfide bondi136 ↔ 177PROSITE-ProRule annotation
Disulfide bondi140 ↔ 164PROSITE-ProRule annotation
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9VVX3.
PRIDEiQ9VVX3.

Expressioni

Developmental stagei

Expression starts at stage 6 in all cells between 15 and 70 per cent of egg length, including the invaginating cells of the ventral furrow. Stripe pattern is emerging by early stage 8. From stage 9 and continuing throughout embryogenesis, expression is seen in the developing CNS. At stage 10, expressed in 15 stripes in the presumptive head and trunk regions, in the posterior midgut primordium, in a subset of cells of anterior midgut invagination and in the procephalic lobe. At stage 12, expression declines in epidermis and increases in the midgut and visceral mesoderm. At stage 17, only expressed in the CNS, hindgut and dorsal vessel.

Gene expression databases

BgeeiQ9VVX3.
ExpressionAtlasiQ9VVX3. differential.
GenevisibleiQ9VVX3. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
GripQ9W4503EBI-118222,EBI-149374

GO - Molecular functioni

  • PDZ domain binding Source: FlyBase
  • Wnt-protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi65366. 8 interactions.
DIPiDIP-17196N.
IntActiQ9VVX3. 59 interactions.
MINTiMINT-893633.
STRINGi7227.FBpp0303228.

Structurei

3D structure databases

ProteinModelPortaliQ9VVX3.
SMRiQ9VVX3. Positions 64-179, 267-620.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 180122FZPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi608 – 6136Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity
Motifi692 – 6943PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi187 – 22539Gly-richAdd
BLAST

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.

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
ENOG410XRC8. LUCA.
GeneTreeiENSGT00760000118864.
InParanoidiQ9VVX3.
KOiK02375.
OrthoDBiEOG7M3J01.
PhylomeDBiQ9VVX3.

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. 2 hits.
PfamiPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSiPR00489. FRIZZLED.
SMARTiSM00063. FRI. 1 hit.
SM01330. Frizzled. 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.

Q9VVX3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHNRLKVLI LGLVLLLTSC RADGPLHSAD HGMGGMGMGG HGLDASPAPG
60 70 80 90 100
YGVPVIPKDP NLRCEEITIP MCRGIGYNMT SFPNEMNHET QDEAGLEVHQ
110 120 130 140 150
FWPLVEIKCS PDLKFFLCSM YTPICLEDYH KPLPVCRSVC ERARSGCAPI
160 170 180 190 200
MQQYSFEWPE RMACEHLPLH GDPDNLCMEQ PSYTEAGSGG SSGGSGGSGS
210 220 230 240 250
GSGSGGKRKQ GGSGSGGSGA GGSSGSTSTK PCRGRNSKNC QNPQGEKASG
260 270 280 290 300
KECSCSCRSP LIFLGKEQLL QQQSQMPMMH HPHHWYMNLT VQRIAGVPNC
310 320 330 340 350
GIPCKGPFFS NDEKDFAGLW IALWSGLCFC STLMTLTTFI IDTERFKYPE
360 370 380 390 400
RPIVFLSACY FMVAVGYLSR NFLQNEEIAC DGLLLRESST GPHSCTLVFL
410 420 430 440 450
LTYFFGMASS IWWVILSFTW FLAAGLKWGN EAITKHSQYF HLAAWLIPTV
460 470 480 490 500
QSVAVLLLSA VDGDPILGIC YVGNLNPDHL KTFVLAPLFV YLVIGTTFLM
510 520 530 540 550
AGFVSLFRIR SVIKQQGGVG AGVKADKLEK LMIRIGIFSV LYTVPATIVI
560 570 580 590 600
GCYLYEAAYF EDWIKALACP CAQVKGPGKK PLYSVLMLKY FMALAVGITS
610 620 630 640 650
GVWIWSGKTL ESWRRFWRRL LGAPDRTGAN QALIKQRPPI PHPYAGSGMG
660 670 680 690
MPVGSAAGSL LATPYTQAGG ASVASTSHHH LHHHVLKQPA ASHV
Length:694
Mass (Da):75,451
Last modified:May 1, 2000 - v1
Checksum:i6C510F13CBAFB096
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551V → A in AAC47273 (PubMed:8717036).Curated
Sequence conflicti417 – 4171S → T in AAC47273 (PubMed:8717036).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65589 Genomic DNA. Translation: AAC47273.1.
AE014296 Genomic DNA. Translation: AAF49184.1.
AE014296 Genomic DNA. Translation: ABW08569.1.
BT023785 mRNA. Translation: AAZ41794.1.
PIRiS71786.
RefSeqiNP_001097643.1. NM_001104173.3.
NP_001137971.1. NM_001144499.3.
NP_001262036.1. NM_001275107.1.
NP_001262038.1. NM_001275109.1.
NP_524155.1. NM_079431.2.
NP_730389.1. NM_168787.3.
UniGeneiDm.2524.

Genome annotation databases

EnsemblMetazoaiFBtr0075028; FBpp0074795; FBgn0016797.
FBtr0075029; FBpp0074796; FBgn0016797.
FBtr0112890; FBpp0111803; FBgn0016797.
FBtr0299586; FBpp0288861; FBgn0016797.
FBtr0330194; FBpp0303227; FBgn0016797.
FBtr0332735; FBpp0304981; FBgn0016797.
GeneIDi40090.
KEGGidme:Dmel_CG9739.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65589 Genomic DNA. Translation: AAC47273.1.
AE014296 Genomic DNA. Translation: AAF49184.1.
AE014296 Genomic DNA. Translation: ABW08569.1.
BT023785 mRNA. Translation: AAZ41794.1.
PIRiS71786.
RefSeqiNP_001097643.1. NM_001104173.3.
NP_001137971.1. NM_001144499.3.
NP_001262036.1. NM_001275107.1.
NP_001262038.1. NM_001275109.1.
NP_524155.1. NM_079431.2.
NP_730389.1. NM_168787.3.
UniGeneiDm.2524.

3D structure databases

ProteinModelPortaliQ9VVX3.
SMRiQ9VVX3. Positions 64-179, 267-620.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65366. 8 interactions.
DIPiDIP-17196N.
IntActiQ9VVX3. 59 interactions.
MINTiMINT-893633.
STRINGi7227.FBpp0303228.

Protein family/group databases

TCDBi9.A.14.16.2. the g-protein-coupled receptor (gpcr) family.
GPCRDBiSearch...

Proteomic databases

PaxDbiQ9VVX3.
PRIDEiQ9VVX3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075028; FBpp0074795; FBgn0016797.
FBtr0075029; FBpp0074796; FBgn0016797.
FBtr0112890; FBpp0111803; FBgn0016797.
FBtr0299586; FBpp0288861; FBgn0016797.
FBtr0330194; FBpp0303227; FBgn0016797.
FBtr0332735; FBpp0304981; FBgn0016797.
GeneIDi40090.
KEGGidme:Dmel_CG9739.

Organism-specific databases

CTDi40090.
FlyBaseiFBgn0016797. fz2.

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
ENOG410XRC8. LUCA.
GeneTreeiENSGT00760000118864.
InParanoidiQ9VVX3.
KOiK02375.
OrthoDBiEOG7M3J01.
PhylomeDBiQ9VVX3.

Enzyme and pathway databases

SignaLinkiQ9VVX3.

Miscellaneous databases

GenomeRNAii40090.
NextBioi816938.
PROiQ9VVX3.

Gene expression databases

BgeeiQ9VVX3.
ExpressionAtlasiQ9VVX3. differential.
GenevisibleiQ9VVX3. DM.

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. 2 hits.
PfamiPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSiPR00489. FRIZZLED.
SMARTiSM00063. FRI. 1 hit.
SM01330. Frizzled. 1 hit.
[Graphical view]
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new member of the frizzled family from Drosophila functions as a Wingless receptor."
    Bhanot P., Brink M., Samos C.H., Hsieh J.C., Wang Y., Macke J.P., Andrew D., Nathans J., Nusse R.
    Nature 382:225-230(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH WG THROUGH FZ DOMAIN.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. "Biochemical characterization of Wnt-frizzled interactions using a soluble, biologically active vertebrate Wnt protein."
    Hsieh J.C., Rattner A., Smallwood P.M., Nathans J.
    Proc. Natl. Acad. Sci. U.S.A. 96:3546-3551(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiFRIZ2_DROME
AccessioniPrimary (citable) accession number: Q9VVX3
Secondary accession number(s): A8JNV7
, Q494J1, Q94916, Q9VVX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  3. 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.