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O70421

- FZD1_MOUSE

UniProt

O70421 - FZD1_MOUSE

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Protein

Frizzled-1

Gene

Fzd1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. G-protein coupled receptor activity Source: UniProtKB-KW
  2. PDZ domain binding Source: RefGenome
  3. Wnt-activated receptor activity Source: RefGenome
  4. Wnt-protein binding Source: MGI

GO - Biological processi

  1. autocrine signaling Source: Ensembl
  2. axonogenesis Source: RefGenome
  3. brain development Source: RefGenome
  4. canonical Wnt signaling pathway Source: MGI
  5. canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation Source: Ensembl
  6. canonical Wnt signaling pathway involved in osteoblast differentiation Source: Ensembl
  7. cell-cell signaling Source: MGI
  8. epithelial cell differentiation Source: MGI
  9. gonad development Source: RefGenome
  10. G-protein coupled receptor signaling pathway coupled to cGMP nucleotide second messenger Source: RefGenome
  11. hard palate development Source: MGI
  12. lung alveolus development Source: RefGenome
  13. membranous septum morphogenesis Source: MGI
  14. muscular septum morphogenesis Source: MGI
  15. negative regulation of BMP signaling pathway Source: MGI
  16. negative regulation of canonical Wnt signaling pathway Source: MGI
  17. negative regulation of catenin import into nucleus Source: MGI
  18. negative regulation of transcription, DNA-templated Source: MGI
  19. outflow tract morphogenesis Source: MGI
  20. planar cell polarity pathway involved in neural tube closure Source: MGI
  21. positive regulation of protein phosphorylation Source: MGI
  22. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  23. positive regulation of transcription, DNA-templated Source: Ensembl
  24. regulation of transcription from RNA polymerase II promoter Source: RefGenome
  25. response to drug Source: Ensembl
  26. vasculature development Source: RefGenome
  27. ventricular septum morphogenesis Source: MGI
  28. Wnt signaling pathway Source: MGI
  29. Wnt signaling pathway, calcium modulating pathway Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_207044. TCF dependent signaling in response to WNT.
REACT_214043. PCP/CE pathway.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.

Protein family/group databases

MEROPSiI93.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Frizzled-1
Short name:
Fz-1
Short name:
mFz1
Gene namesi
Name:Fzd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1196625. Fzd1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini69 – 317249ExtracellularSequence AnalysisAdd
BLAST
Transmembranei318 – 33821Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini339 – 34911CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei350 – 37021Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini371 – 39727ExtracellularSequence AnalysisAdd
BLAST
Transmembranei398 – 41821Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini419 – 44022CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei441 – 46121Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini462 – 48423ExtracellularSequence AnalysisAdd
BLAST
Transmembranei485 – 50521Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini506 – 53126CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei532 – 55221Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini553 – 59341ExtracellularSequence AnalysisAdd
BLAST
Transmembranei594 – 61421Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini615 – 64228CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical part of cell Source: RefGenome
  2. cell surface Source: Ensembl
  3. cytoplasm Source: RefGenome
  4. integral component of membrane Source: UniProtKB-KW
  5. neuron projection membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 6868Sequence AnalysisAdd
BLAST
Chaini69 – 642574Frizzled-1PRO_0000012974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 172PROSITE-ProRule annotation
Disulfide bondi119 ↔ 165PROSITE-ProRule annotation
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi156 ↔ 193PROSITE-ProRule annotation
Disulfide bondi182 ↔ 222PROSITE-ProRule annotation
Disulfide bondi186 ↔ 210PROSITE-ProRule annotation
Glycosylationi226 – 2261N-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

MaxQBiO70421.
PRIDEiO70421.

PTM databases

PhosphoSiteiO70421.

Expressioni

Tissue specificityi

Expressed in chondrocytes.

Gene expression databases

BgeeiO70421.
CleanExiMM_FZD1.
GenevestigatoriO70421.

Interactioni

Subunit structurei

Interacts with MYOC.By similarity

Protein-protein interaction databases

BioGridi199775. 3 interactions.
IntActiO70421. 4 interactions.
MINTiMINT-1779162.
STRINGi10090.ENSMUSP00000058629.

Structurei

3D structure databases

ProteinModelPortaliO70421.
SMRiO70421. Positions 111-217, 291-633.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini106 – 225120FZPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi620 – 6256Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity
Motifi640 – 6423PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi85 – 906Poly-Pro

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.
InParanoidiO70421.
KOiK02432.
OMAiHGAGELC.
OrthoDBiEOG7M3J01.
TreeFamiTF317907.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026548. FZD1.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF81. PTHR11309:SF81. 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.

O70421-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEEAAPSES RAAGRLSLEL CAEALPGRRE EVGHEDTASH RRPRADPRRW
60 70 80 90 100
ASGLLLLLWL LEAPLLLGVR AQAAGQVSGP GQQAPPPPQP QQSGQQYNGE
110 120 130 140 150
RGISIPDHGY CQPISIPLCT DIAYNQTIMP NLLGHTNQED AGLEVHQFYP
160 170 180 190 200
LVKVQCSAEL KFFLCSMYAP VCTVLEQALP PCRSLCERAR QGCEALMNKF
210 220 230 240 250
GFQWPDTLKC EKFPVHGAGE LCVGQNTSDK GTPTPSLLPE FWTSNPQHGG
260 270 280 290 300
GGYRGGYPGG AGTVERGKFS CPRALRVPSY LNYHFLGEKD CGAPCEPTKV
310 320 330 340 350
YGLMYFGPEE LRFSRTWIGI WSVLCCASTL FTVLTYLVDM RRFSYPERPI
360 370 380 390 400
IFLSGCYTAV AVAYIAGFLL EDRVVCNDKF AEDGARTVAQ GTKKEGCTIL
410 420 430 440 450
FMMLYFFSMA SSIWWVILSL TWFLAAGMKW GHEAIEANSQ YFHLAAWAVP
460 470 480 490 500
AIKTITILAL GQVDGDVLSG VCFVGLNNVD ALRGFVLAPL FVYLFIGTSF
510 520 530 540 550
LLAGFVSLFR IRTIMKHDGT KTEKLEKLMV RIGVFSVLYT VPATIVIACY
560 570 580 590 600
FYEQAFRDQW ERSWVAQSCK SYAIPCPHLQ GGGGVPPHPP MSPDFTVFMI
610 620 630 640
KYLMTLIVGI TSGFWIWSGK TLNSWRKFYT RLTNSKQGET TV
Length:642
Mass (Da):71,127
Last modified:July 27, 2011 - v3
Checksum:i7674583F819014E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221I → M in AAC12873. (PubMed:11334716)Curated
Sequence conflicti246 – 2461P → G in AAC12873. (PubMed:11334716)Curated
Sequence conflicti341 – 3411R → P in AAC12873. (PubMed:11334716)Curated
Sequence conflicti352 – 3521F → S in AAC12873. (PubMed:11334716)Curated
Sequence conflicti393 – 3931K → N in AAC12873. (PubMed:11334716)Curated
Sequence conflicti474 – 4741V → L in AAC12873. (PubMed:11334716)Curated
Sequence conflicti615 – 6151W → R in AAC12873. (PubMed:11334716)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054623 mRNA. Translation: AAC12873.2.
AK143101 mRNA. Translation: BAE25269.1.
CH466600 Genomic DNA. Translation: EDL14633.1.
BC053010 mRNA. Translation: AAH53010.1.
AF005202 mRNA. Translation: AAC01952.1.
CCDSiCCDS19072.1.
RefSeqiNP_067432.2. NM_021457.3.
UniGeneiMm.246003.

Genome annotation databases

EnsembliENSMUST00000054294; ENSMUSP00000058629; ENSMUSG00000044674.
GeneIDi14362.
KEGGimmu:14362.
UCSCiuc008wig.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054623 mRNA. Translation: AAC12873.2 .
AK143101 mRNA. Translation: BAE25269.1 .
CH466600 Genomic DNA. Translation: EDL14633.1 .
BC053010 mRNA. Translation: AAH53010.1 .
AF005202 mRNA. Translation: AAC01952.1 .
CCDSi CCDS19072.1.
RefSeqi NP_067432.2. NM_021457.3.
UniGenei Mm.246003.

3D structure databases

ProteinModelPortali O70421.
SMRi O70421. Positions 111-217, 291-633.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199775. 3 interactions.
IntActi O70421. 4 interactions.
MINTi MINT-1779162.
STRINGi 10090.ENSMUSP00000058629.

Chemistry

GuidetoPHARMACOLOGYi 229.

Protein family/group databases

MEROPSi I93.001.
GPCRDBi Search...

PTM databases

PhosphoSitei O70421.

Proteomic databases

MaxQBi O70421.
PRIDEi O70421.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000054294 ; ENSMUSP00000058629 ; ENSMUSG00000044674 .
GeneIDi 14362.
KEGGi mmu:14362.
UCSCi uc008wig.2. mouse.

Organism-specific databases

CTDi 8321.
MGIi MGI:1196625. Fzd1.

Phylogenomic databases

eggNOGi NOG257258.
GeneTreei ENSGT00760000118864.
HOGENOMi HOG000233236.
HOVERGENi HBG006977.
InParanoidi O70421.
KOi K02432.
OMAi HGAGELC.
OrthoDBi EOG7M3J01.
TreeFami TF317907.

Enzyme and pathway databases

Reactomei REACT_207044. TCF dependent signaling in response to WNT.
REACT_214043. PCP/CE pathway.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.

Miscellaneous databases

ChiTaRSi Fzd1. mouse.
NextBioi 285827.
PROi O70421.
SOURCEi Search...

Gene expression databases

Bgeei O70421.
CleanExi MM_FZD1.
Genevestigatori O70421.

Family and domain databases

Gene3Di 1.10.2000.10. 1 hit.
InterProi IPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026548. FZD1.
IPR017981. GPCR_2-like.
[Graphical view ]
PANTHERi PTHR11309. PTHR11309. 1 hit.
PTHR11309:SF81. PTHR11309:SF81. 1 hit.
Pfami PF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view ]
PRINTSi PR00489. FRIZZLED.
SMARTi SM00063. FRI. 1 hit.
[Graphical view ]
SUPFAMi SSF63501. SSF63501. 1 hit.
PROSITEi PS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of frizzled genes in mouse costochondral chondrocytes."
    Xu L., Tan L., Goldring M.B., Olsen B.R., Li Y.
    Matrix Biol. 20:147-151(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Embryo.
  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: Eye.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  5. Johnson M.A., Greenberg N.M.
    Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-376.
    Tissue: Prostate.

Entry informationi

Entry nameiFZD1_MOUSE
AccessioniPrimary (citable) accession number: O70421
Secondary accession number(s): O08974, Q7TS82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 126 of the entry and version 3 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. 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