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Protein

Frizzled

Gene

fz

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

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
Alternative name(s):
Frizzled-1
Short name:
dFz1
Gene namesi
Name:fz
ORF Names:GJ11377
OrganismiDrosophila virilis (Fruit fly)
Taxonomic identifieri7244 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophila
Proteomesi
  • UP000008792 Componenti: Unassembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0014841. Dvir\fz.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini18 – 248ExtracellularSequence analysisAdd BLAST231
Transmembranei249 – 269Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini270 – 279CytoplasmicSequence analysis10
Transmembranei280 – 300Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini301 – 342ExtracellularSequence analysisAdd BLAST42
Transmembranei343 – 363Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini364 – 379CytoplasmicSequence analysisAdd BLAST16
Transmembranei380 – 400Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini401 – 424ExtracellularSequence analysisAdd BLAST24
Transmembranei425 – 445Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini446 – 470CytoplasmicSequence analysisAdd BLAST25
Transmembranei471 – 491Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini492 – 531ExtracellularSequence analysisAdd BLAST40
Transmembranei532 – 552Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini553 – 580CytoplasmicSequence analysisAdd BLAST28

GO - Cellular componenti

  • cell cortex Source: EnsemblMetazoa
  • endosome Source: EnsemblMetazoa
  • integral component of membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000022418118 – 580FrizzledAdd BLAST563

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi53 ↔ 114PROSITE-ProRule annotation
Disulfide bondi61 ↔ 107PROSITE-ProRule annotation
Glycosylationi67N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi98 ↔ 134PROSITE-ProRule annotation
Disulfide bondi124 ↔ 163PROSITE-ProRule annotation
Disulfide bondi128 ↔ 151PROSITE-ProRule annotation
Glycosylationi167N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Gene expression databases

BgeeiFBgn0014841.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi7244.FBpp0225794.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini48 – 166FZPROSITE-ProRule annotationAdd BLAST119

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi555 – 560Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity6
Motifi578 – 580PDZ-bindingBy similarity3

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

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
ENOG410XRC8. LUCA.
InParanoidiQ24760.
KOiK02432.
OMAiKTLNSWR.
OrthoDBiEOG091G0N5M.
PhylomeDBiQ24760.

Family and domain databases

InterProiView protein in InterPro
IPR015526. Frizzled/SFRP.
IPR000539. Frizzled/Smoothened_TM.
IPR020067. Frizzled_dom.
IPR026552. FZD7.
IPR017981. GPCR_2-like.
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF123. PTHR11309:SF123. 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.

Q24760-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLQPLLLLL LPALLQSAQR YDQTPLDASS YYRSDLTGSS ASSLDGFPHH
60 70 80 90 100
NRCEPITISI CKNIPYNMTI MPNLIGHTKQ EEAGLEVHQF APLVKIGCSA
110 120 130 140 150
DLQLFLCSLY VPVCTILERP IPPCRSLCES ARVCETLMKT YNFNWPENLE
160 170 180 190 200
CSKFPVHGGE DLCVAENTTA SSSTPAPTRS APKVTTRKHQ ISVDSPHRNI
210 220 230 240 250
GFVCPVQLKT PLGMGYELKV GGKDLHDCGA PCHAMFFPER ERTVLRYWVG
260 270 280 290 300
SWAAICVASC LFTVLTFLID SSRFRYPERA IVFLAVCYLV VGCAYVAGLG
310 320 330 340 350
AGDSVSCREP FPPPVKLGRL QMMSTITQGH RQTTACTVLF MALYFCCMAA
360 370 380 390 400
FAWWSCLAFA WFLAAGLKWG HEAIENKSHL FHLVAWAVPA LQTISVLALA
410 420 430 440 450
KVEGDILSGV CFVGQLDTHS LGGFLILPLC IYLSIGALFL LAGFISLFRI
460 470 480 490 500
RTVMKTDGKR TDKLERLMLR IGFFSGLFIL PALGLLGCLF YEYYNFDEWM
510 520 530 540 550
IQWHRDICKP FSIPCPAARP PGTPEARPIF QIYMVKYLCS MLVGVTSSVW
560 570 580
LYSSKTMVSW RNFVERLQGK EPRTRAQAYV
Length:580
Mass (Da):64,709
Last modified:February 22, 2012 - v3
Checksum:iA70793856213CD13
GO

Sequence cautioni

The sequence AAB38383 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11L → M in AAB38383 (PubMed:8770598).Curated1
Sequence conflicti19 – 26QRYDQTPL → TIDTV in AAB38383 (PubMed:8770598).Curated8
Sequence conflicti259S → T in AAB38383 (PubMed:8770598).Curated1
Sequence conflicti482A → G in AAB38383 (PubMed:8770598).Curated1
Sequence conflicti506D → H in AAB38383 (PubMed:8770598).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43163 mRNA. Translation: AAB38383.1. Different initiation.
L43340 Genomic DNA. No translation available.
L43341 Genomic DNA. No translation available.
L43342 Genomic DNA. No translation available.
L43343 Genomic DNA. No translation available.
L43344 Genomic DNA. No translation available.
CH940647 Genomic DNA. Translation: EDW70732.1.
RefSeqiXP_002048390.2. XM_002048354.2.

Genome annotation databases

EnsemblMetazoaiFBtr0227302; FBpp0225794; FBgn0014841.
GeneIDi6624400.
KEGGidvi:Dvir_GJ11377.

Entry informationi

Entry nameiFRIZ_DROVI
AccessioniPrimary (citable) accession number: Q24760
Secondary accession number(s): B4LIE5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: February 22, 2012
Last modified: August 30, 2017
This is version 114 of the entry and version 3 of the sequence. See 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