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O77438 (FRIZ3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Frizzled-3

Short name=dFz3
Gene names
Name:fz3
ORF Names:CG16785
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.1 Ref.2

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Wing, leg and eye imaginal disks. In embryos, expressed is seen in brain, proventriculus, Malpighian tubules, anal plate and visceral mesoderm of parasegment 8.

Developmental stage

Expressed in embryos from stage 11 and in larvae.

Domain

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

Sequence similarities

Belongs to the G-protein coupled receptor Fz/Smo family.

Contains 1 FZ (frizzled) domain.

Sequence caution

The sequence CAA20896.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
G-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from Biological aspect of Ancestor. Source: RefGenome

canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

establishment or maintenance of cell polarity

Inferred from mutant phenotype Ref.1. Source: UniProtKB

gonad development

Inferred from Biological aspect of Ancestor. Source: RefGenome

signal transduction

Inferred from sequence or structural similarity PubMed 10908591. Source: FlyBase

vasculature development

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcell projection

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

integral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionG-protein coupled receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

PDZ domain binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt-activated receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt-protein binding

Inferred from physical interaction PubMed 12205098. Source: FlyBase

transmembrane signaling receptor activity

Inferred from sequence or structural similarity PubMed 10908591. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 581562Frizzled-3
PRO_0000013013

Regions

Topological domain20 – 237218Extracellular Potential
Transmembrane238 – 25821Helical; Name=1; Potential
Topological domain259 – 27012Cytoplasmic Potential
Transmembrane271 – 29121Helical; Name=2; Potential
Topological domain292 – 32130Extracellular Potential
Transmembrane322 – 34221Helical; Name=3; Potential
Topological domain343 – 35917Cytoplasmic Potential
Transmembrane360 – 38021Helical; Name=4; Potential
Topological domain381 – 39313Extracellular Potential
Transmembrane394 – 41421Helical; Name=5; Potential
Topological domain415 – 44228Cytoplasmic Potential
Transmembrane443 – 46321Helical; Name=6; Potential
Topological domain464 – 48825Extracellular Potential
Transmembrane489 – 50921Helical; Name=7; Potential
Topological domain510 – 58172Cytoplasmic Potential
Domain35 – 156122FZ
Motif579 – 5813PDZ-binding
Compositional bias403 – 4108Poly-Leu

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 101 By similarity
Disulfide bond48 ↔ 94 By similarity
Disulfide bond85 ↔ 123 By similarity
Disulfide bond112 ↔ 153 By similarity
Disulfide bond116 ↔ 141 By similarity

Experimental info

Sequence conflict561T → I in BAA84677. Ref.1
Sequence conflict1921A → V in BAA84677. Ref.1
Sequence conflict2761L → P in BAA84677. Ref.1
Sequence conflict3041G → W in AAF45547. Ref.3
Sequence conflict3041G → W in AAM50295. Ref.3
Sequence conflict3761A → V in BAA84677. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O77438 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: 07A8BBFF2A9E3F93

FASTA58163,252
        10         20         30         40         50         60 
MYAASILILH LTWAVATIAA NGAGHNGPVA SGAGPNGLQC QPIAVSACQG LGYNMTALPN 

        70         80         90        100        110        120 
LAGHTNQLEA ELQIAKLVPL IESGCSRRAR FLLCSSLFPL CTPDVPRPVA ACKLLCETVR 

       130        140        150        160        170        180 
GECMENAPPE LMELWPSFLN CDGLPQPEKH ELCMQIPQEV AVPGGSPSGP PTTGSPGVED 

       190        200        210        220        230        240 
HPQTYRFWKS GASPTSDLAG VLCPQNFSGS PFNPEECVPQ CQRDAFHTSS QKKTSETLIL 

       250        260        270        280        290        300 
GLSAVCFVLT LFALVTFWAE PTRFGYPERP VLFLCLCYNL FSVCYLERIV FHNQARMHDV 

       310        320        330        340        350        360 
ELQGRLMRPG CLLTPPCLAS YITTSYLSLC AASWWLIFAL CFYLSSHKKW SSEALEKRSG 

       370        380        390        400        410        420 
LFHVLAWVPP LAPPIAALLL EKVRPSELTG MCYAPGFVEL PALVLLLLGL YFTLRASRSL 

       430        440        450        460        470        480 
LSLQQQLQPT LAHHRFGQIR KRFVLFSLLY FAPTTAGVVA ALCERYADSV PSCSTPDDCL 

       490        500        510        520        530        540 
SPTPLSAWPA LVRIFFQLVG GTLTGLWVWS RKTCESYRNR LGASGTPTSS LMNQSKAAGA 

       550        560        570        580 
LPKKHLYTSG KSMLPTGGIT PLYAGISFHN VPVYNPNQSR V 

« Hide

References

« Hide 'large scale' references
[1]"Dfrizzled-3, a new Drosophila Wnt receptor, acting as an attenuator of Wingless signaling in wingless hypomorphic mutants."
Sato A., Kojima T., Ui-Tei K., Miyata Y., Saigo K.
Development 126:4421-4430(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"The Wingless target gene Dfz3 encodes a new member of the Drosophila Frizzled family."
Sivasankaran R., Calleja M., Morata G., Basler K.
Mech. Dev. 91:427-431(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[3]"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. expand/collapse author list , 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.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"From sequence to chromosome: the tip of the X chromosome of D. melanogaster."
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. expand/collapse author list , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M.
Science 287:2220-2222(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Oregon-R.
[6]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB018565 mRNA. Translation: BAA84677.1.
AF195242 mRNA. Translation: AAF63250.1.
AE014298 Genomic DNA. Translation: AAF45547.1.
AL031583 Genomic DNA. Translation: CAA20896.1. Sequence problems.
AL132792 Genomic DNA. No translation available.
AY119641 mRNA. Translation: AAM50295.1.
PIRT13484.
RefSeqNP_525035.2. NM_080296.2.
UniGeneDm.1697.

3D structure databases

ProteinModelPortalO77438.
SMRO77438. Positions 40-154, 215-518.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid57591. 4 interactions.

Protein family/group databases

GPCRDBSearch...

Proteomic databases

PaxDbO77438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID31023.
KEGGdme:Dmel_CG16785.

Organism-specific databases

CTD31023.
FlyBaseFBgn0027343. fz3.

Phylogenomic databases

eggNOGNOG331834.
InParanoidO77438.
KOK04690.
OrthoDBEOG7X6M0F.
PhylomeDBO77438.

Enzyme and pathway databases

SignaLinkO77438.

Gene expression databases

BgeeO77438.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
InterProIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026554. FZD3_invertebrates.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF84. PTHR11309:SF84. 1 hit.
PfamPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSPR00489. FRIZZLED.
SMARTSM00063. FRI. 1 hit.
[Graphical view]
SUPFAMSSF63501. SSF63501. 1 hit.
PROSITEPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi31023.
NextBio771559.

Entry information

Entry nameFRIZ3_DROME
AccessionPrimary (citable) accession number: O77438
Secondary accession number(s): Q540W1 expand/collapse secondary AC list , Q9I7Z7, Q9NIU0, Q9U902, Q9W5D5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries