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Protein

Frizzled-3

Gene

Fzd3

Organism
Mus musculus (Mouse)
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. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Plays a role in controlling early axon growth and guidance processes necessary for the formation of a subset of central and peripheral major fiber tracts. Required for the development of major fiber tracts in the central nervous system, including: the anterior commissure, the corpus callosum, the thalamocortical, corticothalamic and nigrostriatal tracts, the corticospinal tract, the fasciculus retroflexus, the mammillothalamic tract, the medial lemniscus, and ascending fiber tracts from the spinal cord to the brain. In the peripheral nervous system, controls axon growth in distinct populations of cranial and spinal motor neurons, including the facial branchimotor nerve, the hypoglossal nerve, the phrenic nerve, and motor nerves innervating dorsal limbs. Involved in the migration of cranial neural crest cells. May also be implicated in the transmission of sensory information from the trunk and limbs to the brain. Controls commissural sensory axons guidance after midline crossing along the anterior-posterior axis in the developing spinal cord in a Wnt-dependent signaling pathway. Together with FZD6, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle in a beta-catenin-dependent manner.7 Publications

GO - Molecular functioni

  • G-protein coupled receptor activity Source: UniProtKB-KW
  • PDZ domain binding Source: MGI
  • Wnt-activated receptor activity Source: ParkinsonsUK-UCL
  • Wnt-protein binding Source: MGI

GO - Biological processi

  • canonical Wnt signaling pathway Source: MGI
  • cell proliferation in midbrain Source: MGI
  • commissural neuron axon guidance Source: MGI
  • dopaminergic neuron axon guidance Source: ParkinsonsUK-UCL
  • establishment of planar polarity Source: MGI
  • hair follicle development Source: BHF-UCL
  • inner ear morphogenesis Source: MGI
  • midbrain development Source: MGI
  • negative regulation of execution phase of apoptosis Source: UniProtKB
  • negative regulation of mitotic cell cycle, embryonic Source: UniProtKB
  • neural tube closure Source: MGI
  • neuron migration Source: MGI
  • planar cell polarity pathway involved in axon guidance Source: ParkinsonsUK-UCL
  • positive regulation of neuroblast proliferation Source: UniProtKB
  • post-anal tail morphogenesis Source: MGI
  • serotonergic neuron axon guidance Source: ParkinsonsUK-UCL
  • sympathetic ganglion development Source: UniProtKB
  • Wnt signaling pathway, planar cell polarity pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Neurogenesis, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiR-MMU-4086398. Ca2+ pathway.
R-MMU-4608870. Asymmetric localization of PCP proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Frizzled-3
Short name:
Fz-3
Short name:
mFz3
Gene namesi
Name:Fzd3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:108476. Fzd3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 205183ExtracellularSequence analysisAdd
BLAST
Transmembranei206 – 22621Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini227 – 23711CytoplasmicSequence analysisAdd
BLAST
Transmembranei238 – 25821Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini259 – 28830ExtracellularSequence analysisAdd
BLAST
Transmembranei289 – 30921Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini310 – 32819CytoplasmicSequence analysisAdd
BLAST
Transmembranei329 – 34921Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini350 – 37425ExtracellularSequence analysisAdd
BLAST
Transmembranei375 – 39521Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini396 – 42025CytoplasmicSequence analysisAdd
BLAST
Transmembranei421 – 44121Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini442 – 47736ExtracellularSequence analysisAdd
BLAST
Transmembranei478 – 49821Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini499 – 666168CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical part of cell Source: MGI
  • apical plasma membrane Source: MGI
  • axon Source: BHF-UCL
  • cell surface Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • dendrite Source: BHF-UCL
  • filopodium tip Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • lateral plasma membrane Source: MGI
  • neuronal cell body Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Neonate knockout mice have a curly tail, flexed lower limbs, breathe irregularly and typically die within 30 min of birth. Central nervous system (CNS) shows severe defects in the development of several major axon tracts, including: a nearly complete absence of the three early most prominent axon tracts in the brain and the ventral branch of the trigeminal nerve, absence of subcortical and striatal axons, the anterior commissure, misrouting of thalamocortical axons, a nearly complete absence of the corticospinal tract, the fasciculus retroflexus, and the mammillothalamic tract, poor fasciculation of the medial lemniscus and a disorganization of axon bundles in the reticular formation, severe defect in the asymmetric rostrocaudal orientation of dopaminergic and serotonergic axons, a large reduction or complete absence of ascending spinal axon tracts in the braistem, midbrain and thalamus, peripheral nerves defect in several motor neurons, such as in the VIIth and XIIth cranial motor nerves, the phrenic nerve, and the spinal motor nerve which failed to form connections with their respective targets and display also aberrant migration of a subpopulation of cranial neural crest cells (PubMed:12351730, PubMed:24347548, PubMed:24799694). Neonate knockout mice show fewer S-phase proliferating neuroblasts, premature cell cycle exit and enhanced apoptosis in early-stage superior cervical ganglia (SCGs), and in some cases, complete absence of sympathetic innervation of several peripheral targets (PubMed:21325504). Display also impaired rostral turning by growth cones of spinal cord commissural sensory axons (PubMed:14671310). FZD3 and FZD6 double knockout embryos have a curled tail, exhibit defects in neural tube and eyelids closure, in the orientation of hair bundles on inner-ear sensory cells and die at birth (PubMed:16495441). The following conditional knockout mice display the corresponding phenotypes: dopaminergic neuron-specific shows a defect in the orientation and growth of midbrain dopaminergic axons with an absence of striatum innervation; retinal ganglion cell (RGC)-specific displays a misrouting of a subset of optic tract axons and a lack of the medial terminal nucleus (MTN) innervation; neocortex neuron-specific displays a total absence of the posterior part of the anterior commissure and aberrant axon trajectories appearing in the external capsule; ventral telencephalon neuron-specific shows corticothalamic, thalamocortical and corticospinal tracts defect to various extent; telencephalon neuron-specific exhibits the full spectrum of axon defects seen in the classical null mutant knockout mice; cholinergic neuron-specific shows an absence of cholinergic fiber tracts passing through the striatum, a defective caudal migration of neurons of the VIIth motor nucleus and a loss of motor innervation to the face, a decrease in motor innervation of the tongue by the XIIth nerve and a complete loss of cholinergic neurons in the vomeronasal organ; oligodendrocyte neuron-specific leads to the complete spectrum of motor neuron phenotypes shown by the classical mutant knockout mice; caudal and upper thorax region-specific leads to a loss of motor innervation and an atrophy of anterior compartment muscles in the lower hindlimb by the deep peroneal nerve and a nearly absence in ascending spinal sensory axons in the brainstem, midbrain and thalamus altering the ability to transmit sensory information from the trunk and limbs to the brain in postnatal life (PubMed:24347548, PubMed:24799694).6 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 666644Frizzled-3PRO_0000012983Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 89PROSITE-ProRule annotation
Disulfide bondi36 ↔ 82PROSITE-ProRule annotation
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence analysis
Disulfide bondi73 ↔ 110PROSITE-ProRule annotation
Disulfide bondi99 ↔ 133PROSITE-ProRule annotation
Disulfide bondi103 ↔ 127PROSITE-ProRule annotation
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence analysis
Glycosylationi356 – 3561N-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

MaxQBiQ61086.
PaxDbiQ61086.
PRIDEiQ61086.

PTM databases

iPTMnetiQ61086.
PhosphoSiteiQ61086.

Expressioni

Tissue specificityi

Expressed in the cortex, diencephalon, rostral brainstem and little or no staining is seen in the striatum or cerebellum. Expressed in both hair cells and supporting cells in the utricle, saccule, cristae and the organ of Corti in the inner ear (at protein level). Highly expressed in the CNS. In skin, it is restricted to the epidermis and to the developing hair follicle.4 Publications

Developmental stagei

Expressed throughout the developing central nervous system (CNS). Expressed in the cortex, diencephalon, and brainstem, with the most intense staining in the striatum and trigeminal ganglia at 18 dpc (at protein level). First detected in discrete foci in the developing epidermis of 13 days old embryos, later in the hair follicle placodes of 15 days old embryos. Expressed in the ventral and lateral margins of the spinal cord from 9.5 to 13.5 dpc, where post-crossing commissural axons project longitudinally. Expressed in superior sympathetic cervical ganglia (SCG) at 14.5 and 16.5 dpc, a stage when the SCG is comprised primarily of proliferating sympathetic neuroblasts. In 17 days embryos and 1 day old newborn, expression is limited to suprabasal keratinocytes and is not seen in pelage follicles until 3 days postpartum. In 7 days old neonatal skin, expression occurs throughout the epidermis and in the outer cell layers of hair follicles.4 Publications

Gene expression databases

BgeeiQ61086.
CleanExiMM_FZD3.
GenevisibleiQ61086. MM.

Interactioni

Subunit structurei

Interacts with VANGL2.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199776. 1 interaction.
MINTiMINT-4997253.
STRINGi10090.ENSMUSP00000115325.

Structurei

3D structure databases

ProteinModelPortaliQ61086.
SMRiQ61086. Positions 28-136, 182-507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 136114FZPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi502 – 5076Lys-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

eggNOGiKOG3577. Eukaryota.
ENOG410XRC8. LUCA.
GeneTreeiENSGT00760000118864.
HOGENOMiHOG000233237.
HOVERGENiHBG006977.
InParanoidiQ61086.
KOiK02329.
OMAiMAMSWIV.
OrthoDBiEOG7M3J01.
PhylomeDBiQ61086.
TreeFamiTF317907.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026553. FZD3_vertebrates.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF22. PTHR11309:SF22. 1 hit.
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.

Q61086-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSWIVFDL WLLTVFLGQI GGHSLFSCEP ITLRMCQDLP YNTTFMPNLL
60 70 80 90 100
NHYDQQTAAL AMEPFHPMVN LDCSRDFRPF LCALYAPICM EYGRVTLPCR
110 120 130 140 150
RLCQRAYSEC SKLMEMFGVP WPEDMECSRF PDCDEPYPRL VDLNLVGDPT
160 170 180 190 200
EGAPVAVQRD YGFWCPRELK IDPDLGYSFL HVRDCSPPCP NMYFRREELS
210 220 230 240 250
FARYFIGLIS IICLSATLFT FLTFLIDVTR FRYPERPIIF YAVCYMMVSL
260 270 280 290 300
IFFIGFLLED RVACNASSPA QYKASTVTQG SHNKACTMLF MVLYFFTMAG
310 320 330 340 350
SVWWVILTIT WFLAAVPKWG SEAIEKKALL FHASAWGIPG TLTIILLAMN
360 370 380 390 400
KIEGDNISGV CFVGLYDVDA LRYFVLAPLC LYVVVGVSLL LAGIISLNRV
410 420 430 440 450
RIEIPLEKEN QDKLVKFMIR IGVFSILYLV PLLVVIGCYF YEQAYRGIWE
460 470 480 490 500
TTWIQERCRE YHIPCPYQVT QMSRPDLILF LMKYLMALIV GIPSIFWVGS
510 520 530 540 550
KKTCFEWASF FHGRRKKEIV NESRQVLQEP DFAQSLLRDP NTPIIRKSRG
560 570 580 590 600
TSTQGTSTHA SSTQLAMVDD QRSKAGSVHS KVSSYHGSLH RSRDGRYTPC
610 620 630 640 650
SYRGMEERLP HGSMSRLTDH SRHSSSHRLN EQSRHSSIRD LSNNPMTHIT
660
HGTSMNRVIE EDGTSA
Length:666
Mass (Da):76,208
Last modified:November 1, 1996 - v1
Checksum:i0920038B79A73335
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43205 mRNA. Translation: AAC52429.1.
CCDSiCCDS27212.1.
RefSeqiNP_067433.1. NM_021458.2.
UniGeneiMm.214687.
Mm.404299.

Genome annotation databases

EnsembliENSMUST00000131309; ENSMUSP00000115325; ENSMUSG00000007989.
GeneIDi14365.
KEGGimmu:14365.
UCSCiuc007ujb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43205 mRNA. Translation: AAC52429.1.
CCDSiCCDS27212.1.
RefSeqiNP_067433.1. NM_021458.2.
UniGeneiMm.214687.
Mm.404299.

3D structure databases

ProteinModelPortaliQ61086.
SMRiQ61086. Positions 28-136, 182-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199776. 1 interaction.
MINTiMINT-4997253.
STRINGi10090.ENSMUSP00000115325.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiQ61086.
PhosphoSiteiQ61086.

Proteomic databases

MaxQBiQ61086.
PaxDbiQ61086.
PRIDEiQ61086.

Protocols and materials databases

DNASUi14365.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000131309; ENSMUSP00000115325; ENSMUSG00000007989.
GeneIDi14365.
KEGGimmu:14365.
UCSCiuc007ujb.2. mouse.

Organism-specific databases

CTDi7976.
MGIiMGI:108476. Fzd3.

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
ENOG410XRC8. LUCA.
GeneTreeiENSGT00760000118864.
HOGENOMiHOG000233237.
HOVERGENiHBG006977.
InParanoidiQ61086.
KOiK02329.
OMAiMAMSWIV.
OrthoDBiEOG7M3J01.
PhylomeDBiQ61086.
TreeFamiTF317907.

Enzyme and pathway databases

ReactomeiR-MMU-4086398. Ca2+ pathway.
R-MMU-4608870. Asymmetric localization of PCP proteins.

Miscellaneous databases

PROiQ61086.
SOURCEiSearch...

Gene expression databases

BgeeiQ61086.
CleanExiMM_FZD3.
GenevisibleiQ61086. MM.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026553. FZD3_vertebrates.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF22. PTHR11309:SF22. 1 hit.
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

  1. "A large family of putative transmembrane receptors homologous to the product of the Drosophila tissue polarity gene frizzled."
    Wang Y., Macke J.P., Abella B.S., Andreasson K., Worley P., Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.
    J. Biol. Chem. 271:4468-4476(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Protein kinase C is differentially stimulated by Wnt and Frizzled homologs in a G-protein-dependent manner."
    Sheldahl L.C., Park M., Malbon C.C., Moon R.T.
    Curr. Biol. 9:695-698(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: WNT-MEDIATED PKC ACTIVATION.
  3. "Characterization of mouse frizzled-3 expression in hair follicle development and identification of the human homolog in keratinocytes."
    Hung B.S., Wang X.-Q., Cam G.R., Rothnagel J.A.
    J. Invest. Dermatol. 116:940-946(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  4. "Frizzled-3 is required for the development of major fiber tracts in the rostral CNS."
    Wang Y., Thekdi N., Smallwood P.M., Macke J.P., Nathans J.
    J. Neurosci. 22:8563-8573(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. "Anterior-posterior guidance of commissural axons by Wnt-frizzled signaling."
    Lyuksyutova A.I., Lu C.C., Milanesio N., King L.A., Gu o N., Wang Y., Nathans J., Tessier-Lavigne M., Zou Y.
    Science 302:1984-1988(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
  6. "Axonal growth and guidance defects in Frizzled3 knock-out mice: a comparison of diffusion tensor magnetic resonance imaging, neurofilament staining, and genetically directed cell labeling."
    Wang Y., Zhang J., Mori S., Nathans J.
    J. Neurosci. 26:355-364(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The role of Frizzled3 and Frizzled6 in neural tube closure and in the planar polarity of inner-ear sensory hair cells."
    Wang Y., Guo N., Nathans J.
    J. Neurosci. 26:2147-2156(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms for planar cell polarity in mammals."
    Montcouquiol M., Sans N., Huss D., Kach J., Dickman J.D., Forge A., Rachel R.A., Copeland N.G., Jenkins N.A., Bogani D., Murdoch J., Warchol M.E., Wenthold R.J., Kelley M.W.
    J. Neurosci. 26:5265-5275(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VANGL2.
  9. "Frizzled3 is required for neurogenesis and target innervation during sympathetic nervous system development."
    Armstrong A., Ryu Y.K., Chieco D., Kuruvilla R.
    J. Neurosci. 31:2371-2381(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
  10. "Frizzled3 controls axonal development in distinct populations of cranial and spinal motor neurons."
    Hua Z.L., Smallwood P.M., Nathans J.
    Elife 2:E01482-E01482(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUTS.
  11. "Frizzled3 is required for the development of multiple axon tracts in the mouse central nervous system."
    Hua Z.L., Jeon S., Caterina M.J., Nathans J.
    Proc. Natl. Acad. Sci. U.S.A. 111:E3005-E3005(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUTS.

Entry informationi

Entry nameiFZD3_MOUSE
AccessioniPrimary (citable) accession number: Q61086
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 140 of the entry and version 1 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

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.