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Protein

Frizzled-9

Gene

Fzd9

Organism
Mus musculus (Mouse)
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

GO - Biological processi

  • B cell differentiation Source: MGI
  • canonical Wnt signaling pathway Source: GO_Central
  • learning or memory Source: MGI
  • neuroblast proliferation Source: MGI
  • non-canonical Wnt signaling pathway Source: GO_Central
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-9
Short name:
Fz-9
Short name:
mFz3
Short name:
mFz9
Alternative name(s):
CD_antigen: CD349
Gene namesi
Name:Fzd9
Synonyms:Fzd3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1313278. Fzd9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 230207ExtracellularAdd
BLAST
Transmembranei231 – 25121Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini252 – 26716CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei268 – 28821Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini289 – 31628ExtracellularSequence AnalysisAdd
BLAST
Transmembranei317 – 33721Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini338 – 35619CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei357 – 37721Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini378 – 40124ExtracellularSequence AnalysisAdd
BLAST
Transmembranei402 – 42221Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini423 – 44826CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei449 – 46921Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini470 – 50940ExtracellularSequence AnalysisAdd
BLAST
Transmembranei510 – 53021Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini531 – 59262CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • filopodium membrane Source: MGI
  • integral component of membrane Source: GO_Central
  • perinuclear region of cytoplasm Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 592569Frizzled-9PRO_0000013004Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 101PROSITE-ProRule annotation
Disulfide bondi48 ↔ 94PROSITE-ProRule annotation
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi85 ↔ 123PROSITE-ProRule annotation
Disulfide bondi112 ↔ 153PROSITE-ProRule annotation
Disulfide bondi116 ↔ 140PROSITE-ProRule annotation
Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Ubiquitinated by ZNRF3, leading to its degradation by the proteasome.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ9R216.

PTM databases

PhosphoSiteiQ9R216.

Expressioni

Tissue specificityi

In the embryo, found in the neural tube, trunk skeletal muscle precursors (myotomes), limb skeletal anlagen, craniofacial regions and nephric ducts. In the adult, expression is abundant in heart, brain, testis and skeletal muscle. In the testis, expressed in all spermatogenic cell types. Lower levels in adult lung, liver and kidney. Barely detectable in spleen. Expressed also in chondrocytes.

Developmental stagei

Not detected at embryonic day 7 (E7), weakly at E11 and strongly at E15 and E17. Expression covers the entire neural tube at 9.5 dpc, decreases at 10.5 dpc and becomes detectable only in the lumbar to tail regions at 11.5 dpc. In the somites, expression begins at 10.5 dpc to become up-regulated all along the rostrocaudal trunk axis at 11.5 dpc. In craniofacial territories, expression is first detected at 11.5 dpc in restricted areas of the nose, the maxillar mandibular and second branchial arch anlagen. At 11.5 dpc, predominantly expressed in restricted areas of the nose, dorsally to the eye and in the caudal pharyngeal region.1 Publication

Gene expression databases

BgeeiQ9R216.
CleanExiMM_FZD3.
MM_FZD9.
GenevisibleiQ9R216. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000053551.

Structurei

3D structure databases

ProteinModelPortaliQ9R216.
SMRiQ9R216. Positions 40-156, 198-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 156122FZPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi533 – 5386Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity

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.
GeneTreeiENSGT00760000118864.
HOGENOMiHOG000233236.
HOVERGENiHBG006977.
InParanoidiQ9R216.
KOiK02842.
OMAiNALCMEA.
OrthoDBiEOG7M3J01.
PhylomeDBiQ9R216.
TreeFamiTF317907.

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.

Q9R216-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVPPLLRGA LLLWQLLATG GAALEIGRFD PERGRGPAPC QAMEIPMCRG
60 70 80 90 100
IGYNLTRMPN LLGHTSQGEA AAQLAEFSPL VQYGCHSHLR FFLCSLYAPM
110 120 130 140 150
CTDQVSTPIP ACRPMCEQAR LRCAPIMEQF NFGWPDSLDC ARLPTRNDPH
160 170 180 190 200
ALCMEAPENA TAGPTEPHKG LGMLPVAPRP ARPPGDSAPG PGSGGTCDNP
210 220 230 240 250
EKFQYVEKSR SCAPRCGPGV EVFWSRRDKD FALVWMAVWS ALCFFSTAFT
260 270 280 290 300
VFTFLLEPHR FQYPERPIIF LSMCYNVYSL AFLIRAVAGA QSVACDQEAG
310 320 330 340 350
ALYVIQEGLE NTGCTLVFLL LYYFGMASSL WWVVLTLTWF LAAGKKWGHE
360 370 380 390 400
AIEAHGSYFH MAAWGLPALK TIVVLTLRKV AGDELTGLCY VASMDPAALT
410 420 430 440 450
GFVLVPLSCY LVLGTSFLLT GFVALFHIRK IMKTGGTNTE KLEKLMVKIG
460 470 480 490 500
VFSILYTVPA TCVIVCYVYE RLNMDFWRLR ATEQPCTAAT VPGGRRDCSL
510 520 530 540 550
PGGSVPTVAV FMLKIFMSLV VGITSGVWVW SSKTFQTWQS LCYRKMAAGR
560 570 580 590
ARAKACRTPG GYGRGTHCHY KAPTVVLHMT KTDPSLENPT HL
Length:592
Mass (Da):64,995
Last modified:May 1, 2000 - v1
Checksum:i21B2D4F8CE232965
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661S → P in AAB87503 (Ref. 3) Curated
Sequence conflicti73 – 742QL → HC in BAB32311 (PubMed:16141072).Curated
Sequence conflicti93 – 931L → F in BAB32311 (PubMed:16141072).Curated
Sequence conflicti144 – 1441P → S in CAB44237 (Ref. 4) Curated
Sequence conflicti221 – 2211E → K in CAB44237 (Ref. 4) Curated
Sequence conflicti237 – 2371A → P in CAB44237 (Ref. 4) Curated
Sequence conflicti308 – 3081G → D in AAB87503 (Ref. 3) Curated
Sequence conflicti374 – 3741V → F in CAB44237 (Ref. 4) Curated
Sequence conflicti592 – 5921L → P in BAB32311 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF088850 Genomic DNA. Translation: AAD27789.1.
AK021164 mRNA. Translation: BAB32311.1.
AF033585 mRNA. Translation: AAB87503.2.
Y17709 mRNA. Translation: CAB44237.1.
CCDSiCCDS51661.1.
RefSeqiNP_034376.1. NM_010246.1.
UniGeneiMm.6256.

Genome annotation databases

EnsembliENSMUST00000062572; ENSMUSP00000053551; ENSMUSG00000049551.
GeneIDi14371.
KEGGimmu:14371.
UCSCiuc008zya.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF088850 Genomic DNA. Translation: AAD27789.1.
AK021164 mRNA. Translation: BAB32311.1.
AF033585 mRNA. Translation: AAB87503.2.
Y17709 mRNA. Translation: CAB44237.1.
CCDSiCCDS51661.1.
RefSeqiNP_034376.1. NM_010246.1.
UniGeneiMm.6256.

3D structure databases

ProteinModelPortaliQ9R216.
SMRiQ9R216. Positions 40-156, 198-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000053551.

Protein family/group databases

MEROPSiI93.001.
GPCRDBiSearch...

PTM databases

PhosphoSiteiQ9R216.

Proteomic databases

PRIDEiQ9R216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062572; ENSMUSP00000053551; ENSMUSG00000049551.
GeneIDi14371.
KEGGimmu:14371.
UCSCiuc008zya.2. mouse.

Organism-specific databases

CTDi8326.
MGIiMGI:1313278. Fzd9.

Phylogenomic databases

eggNOGiNOG257258.
GeneTreeiENSGT00760000118864.
HOGENOMiHOG000233236.
HOVERGENiHBG006977.
InParanoidiQ9R216.
KOiK02842.
OMAiNALCMEA.
OrthoDBiEOG7M3J01.
PhylomeDBiQ9R216.
TreeFamiTF317907.

Miscellaneous databases

NextBioi285857.
PROiQ9R216.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R216.
CleanExiMM_FZD3.
MM_FZD9.
GenevisibleiQ9R216. MM.

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

« Hide 'large scale' publications
  1. "Characterization and expression pattern of the frizzled gene Fzd9, the mouse homolog of FZD9 which is deleted in Williams-Beuren syndrome."
    Wang Y.-K., Spoerle R., Paperna T., Schughart K., Francke U.
    Genomics 57:235-248(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
    Strain: 129/SvJ.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic head.
  3. "A novel mouse frizzled gene expressed in early neural development."
    Van Raay T.J., Rasmussen J.T., Rao M.S.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-592.
  4. "Localization of the mouse frizzled gene mFZD3 in the olfactory epithelium and in the vomeronasal organ."
    Calo L., Mimmack M.L., Keverne E.B., Emson P.C.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-592.
    Strain: BALB/c.

Entry informationi

Entry nameiFZD9_MOUSE
AccessioniPrimary (citable) accession number: Q9R216
Secondary accession number(s): O35494, Q9CX16, Q9R2B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Has been first described as FZD3 in literature.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.