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Search results 401 to 500 out of 516 for Ror1

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Type Details Score
Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
22439932 | J:186090
First Author: Yamaguchi T
Year: 2012
Journal: Cancer Cell
Title: NKX2-1/TITF1/TTF-1-Induced ROR1 is required to sustain EGFR survival signaling in lung adenocarcinoma.
Volume: 21
Issue: 3
Pages: 348-61
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UniProt Feature
UniProt Feature
Begin: 30
Description: Inactive tyrosine-protein kinase transmembrane receptor ROR1
Type: chain
End: 937
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Protein
Q9Z139
Organism: Mus musculus/domesticus
Length: 937  
Fragment?: false
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Publication
21487037 | -
First Author: Gentile A
Year: 2011
Journal: Cancer Res
Title: Ror1 is a pseudokinase that is crucial for Met-driven tumorigenesis.
Volume: 71
Issue: 8
Pages: 3132-41
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DO Term
DOID:0080263 | autosomal recessive nonsyndromic deafness 108
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Publication
26725982 | -
 
First Author: Yamaguchi T
Year: 2016
Journal: Nat Commun
Title: ROR1 sustains caveolae and survival signalling as a scaffold of cavin-1 and caveolin-1.
Volume: 7
Pages: 10060
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Strain
MGI:5571499 | C57BL/6-Tg(Igh-ROR1)1Kip
Attribute String: transgenic, mutant strain, coisogenic
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Genotype
Genotype
Symbol: Tg(Igh-ROR1)1Kip/?
Background: C57BL/6-Tg(Igh-ROR1)1Kip
Zygosity: ot
Has Mutant Allele: true
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Strain
MGI:5571574 | B6.Cg-Tg(Igh-ROR1)1Kip Tg(Igh-V186.2-TCL1A)3Cro
Attribute String: congenic, mutant strain, transgenic
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Genotype
Genotype
Symbol: Tg(Igh-ROR1)1Kip/? Tg(Igh-V186.2-TCL1A)3Cro/?
Background: B6.Cg-Tg(Igh-ROR1)1Kip Tg(Igh-V186.2-TCL1A)3Cro
Zygosity: cx
Has Mutant Allele: true
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Publication
25835638 | -
First Author: Shabani M
Year: 2015
Journal: Expert Opin Ther Targets
Title: Receptor tyrosine kinase-like orphan receptor 1: a novel target for cancer immunotherapy.
Volume: 19
Issue: 7
Pages: 941-55
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Publication
25825749 | J:220532
First Author: Cerpa W
Year: 2015
Journal: Proc Natl Acad Sci U S A
Title: RoR2 functions as a noncanonical Wnt receptor that regulates NMDAR-mediated synaptic transmission.
Volume: 112
Issue: 15
Pages: 4797-802
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Publication
18667433 | -
First Author: Nomachi A
Year: 2008
Journal: J Biol Chem
Title: Receptor tyrosine kinase Ror2 mediates Wnt5a-induced polarized cell migration by activating c-Jun N-terminal kinase via actin-binding protein filamin A.
Volume: 283
Issue: 41
Pages: 27973-81
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Protein Domain
IPR016247 | Tyr_kinase_rcpt_ROR
Type: Family
Description: The Ror family of receptor tyrosine kinases consists of two structurally related proteins, Ror1 and Ror2. Ror1 is a pseudokinase that acts as a substrate for the oncogenic tyrosine kinase Met []. It is expressed during development []. It shows no significant expression in normal adult tissues, but it is selectively overexpressed in a number of malignancies []. Ror2 functions as a Wnt receptor required to maintain basal NMDAR-mediated synaptic transmission []. For a time its ligand remained elusive, hence the name receptor tyrosine kinase-like orphan receptor-2 (Ror2). It is now established that Wnt5A acts a ligand for Ror2 [].
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Publication
33357452 | J:302318
First Author: Srivastava S
Year: 2021
Journal: Cancer Cell
Title: Immunogenic Chemotherapy Enhances Recruitment of CAR-T Cells to Lung Tumors and Improves Antitumor Efficacy when Combined with Checkpoint Blockade.
Volume: 39
Issue: 2
Pages: 193-208.e10
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Publication
25068995 | J:217102
 
First Author: Hojjat-Farsangi M
Year: 2014
Journal: Semin Cancer Biol
Title: The receptor tyrosine kinase ROR1--an oncofetal antigen for targeted cancer therapy.
Volume: 29
Pages: 21-31
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Publication
17942487 | -
First Author: Green JL
Year: 2007
Journal: Development
Title: The C. elegans ROR receptor tyrosine kinase, CAM-1, non-autonomously inhibits the Wnt pathway.
Volume: 134
Issue: 22
Pages: 4053-62
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Publication
18848778 | -
First Author: Green JL
Year: 2008
Journal: Trends Cell Biol
Title: Ror receptor tyrosine kinases: orphans no more.
Volume: 18
Issue: 11
Pages: 536-44
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Protein Domain
IPR041775 | Ror-like_CRD
Type: Domain
Description: The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror) proteins, a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2 []. Proteins containing this domain also include CAM-1 from C. elegans. CAM-1 is a ROR receptor tyrosine kinase that inhibits the Wnt pathway [].
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Publication
19910923 | J:156508
First Author: Sato A
Year: 2010
Journal: EMBO J
Title: Wnt5a regulates distinct signalling pathways by binding to Frizzled2.
Volume: 29
Issue: 1
Pages: 41-54
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Publication
27904138 | J:241799
First Author: Yu J
Year: 2017
Journal: Leukemia
Title: Cirmtuzumab inhibits Wnt5a-induced Rac1 activation in chronic lymphocytic leukemia treated with ibrutinib.
Volume: 31
Issue: 6
Pages: 1333-1339
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Publication
10704868 | -
First Author: Kawakami Y
Year: 2000
Journal: Mech Dev
Title: Identification of chick frizzled-10 expressed in the developing limb and the central nervous system.
Volume: 91
Issue: 1-2
Pages: 375-8
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Publication
11142678 | -
First Author: Kawakami Y
Year: 2000
Journal: Dev Growth Differ
Title: Involvement of frizzled-10 in Wnt-7a signaling during chick limb development.
Volume: 42
Issue: 6
Pages: 561-9
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Publication
21343368 | J:170839
First Author: Ye X
Year: 2011
Journal: Development
Title: Genetic mosaic analysis reveals a major role for frizzled 4 and frizzled 8 in controlling ureteric growth in the developing kidney.
Volume: 138
Issue: 6
Pages: 1161-72
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Publication
18681827 | -
First Author: Melchior K
Year: 2008
Journal: Biol Chem
Title: The WNT receptor FZD7 contributes to self-renewal signaling of human embryonic stem cells.
Volume: 389
Issue: 7
Pages: 897-903
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Protein Domain
IPR026553 | FZD3_vertebrates
Type: Family
Description: Frizzleds are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors []. They have important regulatory roles during embryonic development [, ].Frizzleds expose their large N terminus on the extracellular side. The N-terminal, extracellular cysteine-rich domain (CRD) has been implicated as the Wnt binding domain and its structure has been solved []. The cysteine-rich domain of Frizzled (Fz) is shared with other receptor tyrosine kinases that have roles in development including the muscle-specific receptor tyrosine kinase (MuSK), the neuronal specific kinase (NSK2), and ROR1 and ROR2. The cytoplasmic side of many Fz proteins has been shown to interact with the PDZ domains of PSD-95 family members and is thought to have a role in the assembly of signalling complexes. The conserved cytoplasmic motif of Fz, Lys-Thr-X-X-X-Trp, is required for activation of the beta-catenin pathway, and for membrane localisation and phosphorylation of Dsh.In Drosophila melanogaster, the frizzled locus is involved in planar cell polarity, which is the coordination of the cytoskeleton of epidermal cells to produce a parallel array of cuticular hairs and bristles [, ]. In the wild-type wing, all hairs point towards the distal tip [], whereas in Fz mutants, the orientation of individual hairs with respect both to their neighbours and to the organism as a whole is altered. In the developing wing, Fz function is required for cells to respond to the extracellular polarity signal as well as the proximal-distal transmission of an intracellular polarity signal.In Caenorhabditis elegans, protein mom-5 is the equivalent of frizzled [].Three main signaling pathways are activated by agonist-activated Frizzled proteins: the Fz/beta-catenin pathway, the Fz/Ca2+ pathway and the Fz/PCP (planar cell polarity) pathway []. The Wnt/beta-catenin pathway is the best studied signalling pathway involving Fz receptors. In the Wnt/beta-catenin pathway the first downstream cytoplasmic components activated by Fz signalling include Dishevelled (Dsh) and/or its regulatory kinases.This entry represents frizzled-3 from vertebrates.
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Protein Domain
IPR026552 | FZD7
Type: Family
Description: Frizzleds are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors []. They have important regulatory roles during embryonic development [, ].Frizzleds expose their large N terminus on the extracellular side. The N-terminal, extracellular cysteine-rich domain (CRD) has been implicated as the Wnt binding domain and its structure has been solved []. The cysteine-rich domain of Frizzled (Fz) is shared with other receptor tyrosine kinases that have roles in development including the muscle-specific receptor tyrosine kinase (MuSK), the neuronal specific kinase (NSK2), and ROR1 and ROR2. The cytoplasmic side of many Fz proteins has been shown to interact with the PDZ domains of PSD-95 family members and is thought to have a role in the assembly of signalling complexes. The conserved cytoplasmic motif of Fz, Lys-Thr-X-X-X-Trp, is required for activation of the beta-catenin pathway, and for membrane localisation and phosphorylation of Dsh.In Drosophila melanogaster, the frizzled locus is involved in planar cell polarity, which is the coordination of the cytoskeleton of epidermal cells to produce a parallel array of cuticular hairs and bristles [, ]. In the wild-type wing, all hairs point towards the distal tip [], whereas in Fz mutants, the orientation of individual hairs with respect both to their neighbours and to the organism as a whole is altered. In the developing wing, Fz function is required for cells to respond to the extracellular polarity signal as well as the proximal-distal transmission of an intracellular polarity signal.In Caenorhabditis elegans, protein mom-5 is the equivalent of frizzled [].Three main signaling pathways are activated by agonist-activated Frizzled proteins: the Fz/beta-catenin pathway, the Fz/Ca2+ pathway and the Fz/PCP (planar cell polarity) pathway []. The Wnt/beta-catenin pathway is the best studied signalling pathway involving Fz receptors. In the Wnt/beta-catenin pathway the first downstream cytoplasmic components activated by Fz signalling include Dishevelled (Dsh) and/or its regulatory kinases.This entry represents frizzled-7. It is likely to have an important role in the maintenance of embryonic stem cells self-renewal capacity [].
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Protein Domain
IPR026551 | FZD4
Type: Family
Description: Frizzleds are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors []. They have important regulatory roles during embryonic development [, ].Frizzleds expose their large N terminus on the extracellular side. The N-terminal, extracellular cysteine-rich domain (CRD) has been implicated as the Wnt binding domain and its structure has been solved []. The cysteine-rich domain of Frizzled (Fz) is shared with other receptor tyrosine kinases that have roles in development including the muscle-specific receptor tyrosine kinase (MuSK), the neuronal specific kinase (NSK2), and ROR1 and ROR2. The cytoplasmic side of many Fz proteins has been shown to interact with the PDZ domains of PSD-95 family members and is thought to have a role in the assembly of signalling complexes. The conserved cytoplasmic motif of Fz, Lys-Thr-X-X-X-Trp, is required for activation of the beta-catenin pathway, and for membrane localisation and phosphorylation of Dsh.In Drosophila melanogaster, the frizzled locus is involved in planar cell polarity, which is the coordination of the cytoskeleton of epidermal cells to produce a parallel array of cuticular hairs and bristles [, ]. In the wild-type wing, all hairs point towards the distal tip [], whereas in Fz mutants, the orientation of individual hairs with respect both to their neighbours and to the organism as a whole is altered. In the developing wing, Fz function is required for cells to respond to the extracellular polarity signal as well as the proximal-distal transmission of an intracellular polarity signal.In Caenorhabditis elegans, protein mom-5 is the equivalent of frizzled [].Three main signaling pathways are activated by agonist-activated Frizzled proteins: the Fz/beta-catenin pathway, the Fz/Ca2+ pathway and the Fz/PCP (planar cell polarity) pathway []. The Wnt/beta-catenin pathway is the best studied signalling pathway involving Fz receptors. In the Wnt/beta-catenin pathway the first downstream cytoplasmic components activated by Fz signalling include Dishevelled (Dsh) and/or its regulatory kinases.This entry represents frizzled-4. Together with frizzled-8, it has a major role in controlling ureteric growth in the developing kidney [].
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Protein Domain
IPR026549 | FZD10
Type: Family
Description: Frizzleds are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors []. They have important regulatory roles during embryonic development [, ].Frizzleds expose their large N terminus on the extracellular side. The N-terminal, extracellular cysteine-rich domain (CRD) has been implicated as the Wnt binding domain and its structure has been solved []. The cysteine-rich domain of Frizzled (Fz) is shared with other receptor tyrosine kinases that have roles in development including the muscle-specific receptor tyrosine kinase (MuSK), the neuronal specific kinase (NSK2), and ROR1 and ROR2. The cytoplasmic side of many Fz proteins has been shown to interact with the PDZ domains of PSD-95 family members and is thought to have a role in the assembly of signalling complexes. The conserved cytoplasmic motif of Fz, Lys-Thr-X-X-X-Trp, is required for activation of the beta-catenin pathway, and for membrane localisation and phosphorylation of Dsh.In Drosophila melanogaster, the frizzled locus is involved in planar cell polarity, which is the coordination of the cytoskeleton of epidermal cells to produce a parallel array of cuticular hairs and bristles [, ]. In the wild-type wing, all hairs point towards the distal tip [], whereas in Fz mutants, the orientation of individual hairs with respect both to their neighbours and to the organism as a whole is altered. In the developing wing, Fz function is required for cells to respond to the extracellular polarity signal as well as the proximal-distal transmission of an intracellular polarity signal.In Caenorhabditis elegans, protein mom-5 is the equivalent of frizzled [].Three main signaling pathways are activated by agonist-activated Frizzled proteins: the Fz/beta-catenin pathway, the Fz/Ca2+ pathway and the Fz/PCP (planar cell polarity) pathway []. The Wnt/beta-catenin pathway is the best studied signalling pathway involving Fz receptors. In the Wnt/beta-catenin pathway the first downstream cytoplasmic components activated by Fz signalling include Dishevelled (Dsh) and/or its regulatory kinases.This entry represents frizzled-10 [], which may act as a receptor for Wnt-7a [].
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Publication
21665003 | J:178042
First Author: Fröjmark AS
Year: 2011
Journal: Am J Hum Genet
Title: Mutations in Frizzled 6 cause isolated autosomal-recessive nail dysplasia.
Volume: 88
Issue: 6
Pages: 852-860
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Publication
10347172 | -
First Author: Bafico A
Year: 1999
Journal: J Biol Chem
Title: Interaction of frizzled related protein (FRP) with Wnt ligands and the frizzled receptor suggests alternative mechanisms for FRP inhibition of Wnt signaling.
Volume: 274
Issue: 23
Pages: 16180-7
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Publication
19842188 | J:155359
First Author: Stuebner S
Year: 2010
Journal: Dev Dyn
Title: Fzd3 and Fzd6 deficiency results in a severe midbrain morphogenesis defect.
Volume: 239
Issue: 1
Pages: 246-60
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Publication
1334084 | -
First Author: Chan SD
Year: 1992
Journal: J Biol Chem
Title: Two homologs of the Drosophila polarity gene frizzled (fz) are widely expressed in mammalian tissues.
Volume: 267
Issue: 35
Pages: 25202-7
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Publication
10557084 | J:161039
First Author: Gazit A
Year: 1999
Journal: Oncogene
Title: Human frizzled 1 interacts with transforming Wnts to transduce a TCF dependent transcriptional response.
Volume: 18
Issue: 44
Pages: 5959-66
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Protein Domain
IPR026550 | FZD1/2
Type: Family
Description: Frizzleds are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors []. They have important regulatory roles during embryonic development [, ].Frizzleds expose their large N terminus on the extracellular side. The N-terminal, extracellular cysteine-rich domain (CRD) has been implicated as the Wnt binding domain and its structure has been solved []. The cysteine-rich domain of Frizzled (Fz) is shared with other receptor tyrosine kinases that have roles in development including the muscle-specific receptor tyrosine kinase (MuSK), the neuronal specific kinase (NSK2), and ROR1 and ROR2. The cytoplasmic side of many Fz proteins has been shown to interact with the PDZ domains of PSD-95 family members and is thought to have a role in the assembly of signalling complexes. The conserved cytoplasmic motif of Fz, Lys-Thr-X-X-X-Trp, is required for activation of the beta-catenin pathway, and for membrane localisation and phosphorylation of Dsh.In Drosophila melanogaster, the frizzled locus is involved in planar cell polarity, which is the coordination of the cytoskeleton of epidermal cells to produce a parallel array of cuticular hairs and bristles [, ]. In the wild-type wing, all hairs point towards the distal tip [], whereas in Fz mutants, the orientation of individual hairs with respect both to their neighbours and to the organism as a whole is altered. In the developing wing, Fz function is required for cells to respond to the extracellular polarity signal as well as the proximal-distal transmission of an intracellular polarity signal.In Caenorhabditis elegans, protein mom-5 is the equivalent of frizzled [].Three main signaling pathways are activated by agonist-activated Frizzled proteins: the Fz/beta-catenin pathway, the Fz/Ca2+ pathway and the Fz/PCP (planar cell polarity) pathway []. The Wnt/beta-catenin pathway is the best studied signalling pathway involving Fz receptors. In the Wnt/beta-catenin pathway the first downstream cytoplasmic components activated by Fz signalling include Dishevelled (Dsh) and/or its regulatory kinases.This entry represents frizzled-1 and 2. Human frizzled-1 []is a functional partner for certain Wnts in inducing TCF dependent transcription []. Frizzled-2 has been reported to bind Wnt-8 [].
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Protein Domain
IPR015526 | Frizzled/SFRP
Type: Family
Description: Frizzleds are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors []. They have important regulatory roles during embryonic development [, ].Frizzleds expose their large N terminus on the extracellular side. The N-terminal, extracellular cysteine-rich domain (CRD) has been implicated as the Wnt binding domain and its structure has been solved []. The cysteine-rich domain of Frizzled (Fz) is shared with other receptor tyrosine kinases that have roles in development including the muscle-specific receptor tyrosine kinase (MuSK), the neuronal specific kinase (NSK2), and ROR1 and ROR2. The cytoplasmic side of many Fz proteins has been shown to interact with the PDZ domains of PSD-95 family members and is thought to have a role in the assembly of signalling complexes. The conserved cytoplasmic motif of Fz, Lys-Thr-X-X-X-Trp, is required for activation of the beta-catenin pathway, and for membrane localisation and phosphorylation of Dsh.In Drosophila melanogaster, the frizzled locus is involved in planar cell polarity, which is the coordination of the cytoskeleton of epidermal cells to produce a parallel array of cuticular hairs and bristles [, ]. In the wild-type wing, all hairs point towards the distal tip [], whereas in Fz mutants, the orientation of individual hairs with respect both to their neighbours and to the organism as a whole is altered. In the developing wing, Fz function is required for cells to respond to the extracellular polarity signal as well as the proximal-distal transmission of an intracellular polarity signal.In Caenorhabditis elegans, protein mom-5 is the equivalent of frizzled [].Three main signaling pathways are activated by agonist-activated Frizzled proteins: the Fz/beta-catenin pathway, the Fz/Ca2+ pathway and the Fz/PCP (planar cell polarity) pathway []. The Wnt/beta-catenin pathway is the best studied signalling pathway involving Fz receptors. In the Wnt/beta-catenin pathway the first downstream cytoplasmic components activated by Fz signalling include Dishevelled (Dsh) and/or its regulatory kinases.There are secreted forms of Fz, known as soluble or secreted frizzled-related proteins (sFRPS), which function as modulators of Wnt signaling through direct interaction with Wnts []. They consist of only the amino-terminal cysteine rich domain (CRD), but no transmembrane segments. These secreted forms may bind to Wnt proteins in solution and thereby change the activity of Wnts. Such as FRP/FrzB, which consist of the CRD only and can act as secreted antagonists of Wnt signalling.This entry includes both frizzled proteins and secreted frizzled-related proteins (SFRP).
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Protein Domain
IPR026543 | FZD6
Type: Family
Description: Frizzleds are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors []. They have important regulatory roles during embryonic development [, ].Frizzleds expose their large N terminus on the extracellular side. The N-terminal, extracellular cysteine-rich domain (CRD) has been implicated as the Wnt binding domain and its structure has been solved []. The cysteine-rich domain of Frizzled (Fz) is shared with other receptor tyrosine kinases that have roles in development including the muscle-specific receptor tyrosine kinase (MuSK), the neuronal specific kinase (NSK2), and ROR1 and ROR2. The cytoplasmic side of many Fz proteins has been shown to interact with the PDZ domains of PSD-95 family members and is thought to have a role in the assembly of signalling complexes. The conserved cytoplasmic motif of Fz, Lys-Thr-X-X-X-Trp, is required for activation of the beta-catenin pathway, and for membrane localisation and phosphorylation of Dsh.In Drosophila melanogaster, the frizzled locus is involved in planar cell polarity, which is the coordination of the cytoskeleton of epidermal cells to produce a parallel array of cuticular hairs and bristles [, ]. In the wild-type wing, all hairs point towards the distal tip [], whereas in Fz mutants, the orientation of individual hairs with respect both to their neighbours and to the organism as a whole is altered. In the developing wing, Fz function is required for cells to respond to the extracellular polarity signal as well as the proximal-distal transmission of an intracellular polarity signal.In Caenorhabditis elegans, protein mom-5 is the equivalent of frizzled [].Three main signaling pathways are activated by agonist-activated Frizzled proteins: the Fz/beta-catenin pathway, the Fz/Ca2+ pathway and the Fz/PCP (planar cell polarity) pathway []. The Wnt/beta-catenin pathway is the best studied signalling pathway involving Fz receptors. In the Wnt/beta-catenin pathway the first downstream cytoplasmic components activated by Fz signalling include Dishevelled (Dsh) and/or its regulatory kinases.This entry represents Frizzled-6. Frizzled-6 deficiency results in a severe midbrain morphogenesis defect in mice []. In humans, mutations in Frizzled-6 have been described to cause nail dysplasia [].
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Protein Domain
IPR037441 | FZ5_CRD
Type: Domain
Description: Frizzleds are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors []. They have important regulatory roles during embryonic development [, ].Frizzleds expose their large N terminus on the extracellular side. The N-terminal, extracellular cysteine-rich domain (CRD) has been implicated as the Wnt binding domain and its structure has been solved []. The cysteine-rich domain of Frizzled (Fz) is shared with other receptor tyrosine kinases that have roles in development including the muscle-specific receptor tyrosine kinase (MuSK), the neuronal specific kinase (NSK2), and ROR1 and ROR2. The cytoplasmic side of many Fz proteins has been shown to interact with the PDZ domains of PSD-95 family members and is thought to have a role in the assembly of signalling complexes. The conserved cytoplasmic motif of Fz, Lys-Thr-X-X-X-Trp, is required for activation of the beta-catenin pathway, and for membrane localisation and phosphorylation of Dsh.In Drosophila melanogaster, the frizzled locus is involved in planar cell polarity, which is the coordination of the cytoskeleton of epidermal cells to produce a parallel array of cuticular hairs and bristles [, ]. In the wild-type wing, all hairs point towards thedistal tip [], whereas in Fz mutants, the orientation of individual hairs with respect both to their neighbours and to the organism as a whole is altered. In the developing wing, Fz function is required for cells to respond to the extracellular polarity signal as well as the proximal-distal transmission of an intracellular polarity signal.In Caenorhabditis elegans, protein mom-5 is the equivalent of frizzled [].Three main signaling pathways are activated by agonist-activated Frizzled proteins: the Fz/beta-catenin pathway, the Fz/Ca2+ pathway and the Fz/PCP (planar cell polarity) pathway []. The Wnt/beta-catenin pathway is the best studied signalling pathway involving Fz receptors. In the Wnt/beta-catenin pathway the first downstream cytoplasmic components activated by Fz signalling include Dishevelled (Dsh) and/or its regulatory kinases.This entry represents the cysteine-rich Wnt-binding domain (CRD) of Frizzled-5 (Fz5). The cysteine-rich domain (CRD) is an essential extracellular portion of the Fz5 receptor, and is required for binding Wnt proteins [].
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Protein
A0A2I3BR53
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: false
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Protein
Q9CUZ6
Organism: Mus musculus/domesticus
Length: 37  
Fragment?: true
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Protein
A0A2I3BQF8
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
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Publication
2174014 | -
First Author: Adler PN
Year: 1990
Journal: Genetics
Title: Molecular structure of frizzled, a Drosophila tissue polarity gene.
Volume: 126
Issue: 2
Pages: 401-16
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Publication
2493583 | -
First Author: Vinson CR
Year: 1989
Journal: Nature
Title: A Drosophila tissue polarity locus encodes a protein containing seven potential transmembrane domains.
Volume: 338
Issue: 6212
Pages: 263-4
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Publication
17884187 | -
First Author: Schulte G
Year: 2007
Journal: Trends Pharmacol Sci
Title: The Frizzled family of unconventional G-protein-coupled receptors.
Volume: 28
Issue: 10
Pages: 518-25
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Publication
21314612 | -
First Author: Katanaev VL
Year: 2010
Journal: Biochemistry (Mosc)
Title: The Wnt/Frizzled GPCR signaling pathway.
Volume: 75
Issue: 12
Pages: 1428-34
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Publication
9288750 | -
First Author: Rocheleau CE
Year: 1997
Journal: Cell
Title: Wnt signaling and an APC-related gene specify endoderm in early C. elegans embryos.
Volume: 90
Issue: 4
Pages: 707-16
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Publication
10097073 | -
First Author: Hsieh JC
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: Biochemical characterization of Wnt-frizzled interactions using a soluble, biologically active vertebrate Wnt protein.
Volume: 96
Issue: 7
Pages: 3546-51
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Protein
Q8K2P8
Organism: Mus musculus/domesticus
Length: 310  
Fragment?: true
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Protein
Q8BJN8
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: true
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Publication
11452312 | -
First Author: Dann CE
Year: 2001
Journal: Nature
Title: Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains.
Volume: 412
Issue: 6842
Pages: 86-90
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Protein
Q923Z9
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: true
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Protein
Q3TUV1
Organism: Mus musculus/domesticus
Length: 224  
Fragment?: true
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Protein
Q8BKU9
Organism: Mus musculus/domesticus
Length: 381  
Fragment?: false
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Protein
A0A172Q396
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: true
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Protein
Q3UTZ0
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: true
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Protein
Q61086
Organism: Mus musculus/domesticus
Length: 666  
Fragment?: false
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Protein
Q9JIP6
Organism: Mus musculus/domesticus
Length: 570  
Fragment?: false
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Protein
Q8BKG4
Organism: Mus musculus/domesticus
Length: 582  
Fragment?: false
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Protein
O70421
Organism: Mus musculus/domesticus
Length: 642  
Fragment?: false
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Protein
Q61088
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
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Protein
Q9EQD0
Organism: Mus musculus/domesticus
Length: 585  
Fragment?: false
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Protein
Q61089
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
Q61090
Organism: Mus musculus/domesticus
Length: 572  
Fragment?: false
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Protein
Q3V1B2
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
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Protein
Q6P551
Organism: Mus musculus/domesticus
Length: 572  
Fragment?: false
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Protein
Q149J3
Organism: Mus musculus/domesticus
Length: 582  
Fragment?: false
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Protein
Q542J1
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
Q149L3
Organism: Mus musculus/domesticus
Length: 585  
Fragment?: false
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Protein
Q71S95
Organism: Mus musculus/domesticus
Length: 618  
Fragment?: false
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Protein
Q8BKS3
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
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Protein
Q3UYZ0
Organism: Mus musculus/domesticus
Length: 357  
Fragment?: true
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Protein
Q810L8
Organism: Mus musculus/domesticus
Length: 750  
Fragment?: true
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Protein
Q8R382
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
Q8BLL2
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
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Protein
A0A1Y7VK98
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: false
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Protein
A0A1Y7VJK6
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: true
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Protein
Q8K0Q8
Organism: Mus musculus/domesticus
Length: 801  
Fragment?: true
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Protein
Q61091
Organism: Mus musculus/domesticus
Length: 685  
Fragment?: false
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Protein
Q9R216
Organism: Mus musculus/domesticus
Length: 592  
Fragment?: false
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Protein
P56726
Organism: Mus musculus/domesticus
Length: 793  
Fragment?: false
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Protein
Q9Z1N6
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Protein
P97401
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
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Protein
Q8C4U3
Organism: Mus musculus/domesticus
Length: 314  
Fragment?: false
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Protein
Q9WU66
Organism: Mus musculus/domesticus
Length: 314  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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