Q9ULW2 · FZD10_HUMAN
- ProteinFrizzled-10
- GeneFZD10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids581 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for Wnt proteins. Functions in the canonical Wnt/beta-catenin signaling pathway (By similarity).
The canonical Wnt/beta-catenin signaling pathway 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 (Probable)
The canonical Wnt/beta-catenin signaling pathway 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 (Probable)
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | cytoplasm | |
Cellular Component | nucleoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | G protein-coupled receptor activity | |
Molecular Function | Wnt receptor activity | |
Molecular Function | Wnt-protein binding | |
Biological Process | canonical Wnt signaling pathway | |
Biological Process | cellular response to retinoic acid | |
Biological Process | neuron differentiation | |
Biological Process | non-canonical Wnt signaling pathway | |
Biological Process | positive regulation of JNK cascade | |
Biological Process | regulation of actin cytoskeleton organization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFrizzled-10
- Short namesFz-10; hFz10
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9ULW2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-225 | Extracellular | ||||
Sequence: ISSMDMERPGDGKCQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHGHLRFFLCSLYAPMCTEQVSTPIPACRVMCEQARLKCSPIMEQFNFKWPDSLDCRKLPNKNDPNYLCMEAPNNGSDEPTRGSGLFPPLFRPQRPHSAQEHPLKDGGPGRGGCDNPGKFHHVEKSASCAPLCTPGVDVYWSREDKR | ||||||
Transmembrane | 226-246 | Helical; Name=1 | ||||
Sequence: FAVVWLAIWAVLCFFSSAFTV | ||||||
Topological domain | 247-262 | Cytoplasmic | ||||
Sequence: LTFLIDPARFRYPERP | ||||||
Transmembrane | 263-283 | Helical; Name=2 | ||||
Sequence: IIFLSMCYCVYSVGYLIRLFA | ||||||
Topological domain | 284-311 | Extracellular | ||||
Sequence: GAESIACDRDSGQLYVIQEGLESTGCTL | ||||||
Transmembrane | 312-332 | Helical; Name=3 | ||||
Sequence: VFLVLYYFGMASSLWWVVLTL | ||||||
Topological domain | 333-351 | Cytoplasmic | ||||
Sequence: TWFLAAGKKWGHEAIEANS | ||||||
Transmembrane | 352-372 | Helical; Name=4 | ||||
Sequence: SYFHLAAWAIPAVKTILILVM | ||||||
Topological domain | 373-393 | Extracellular | ||||
Sequence: RRVAGDELTGVCYVGSMDVNA | ||||||
Transmembrane | 394-414 | Helical; Name=5 | ||||
Sequence: LTGFVLIPLACYLVIGTSFIL | ||||||
Topological domain | 415-443 | Cytoplasmic | ||||
Sequence: SGFVALFHIRRVMKTGGENTDKLEKLMVR | ||||||
Transmembrane | 444-464 | Helical; Name=6 | ||||
Sequence: IGLFSVLYTVPATCVIACYFY | ||||||
Topological domain | 465-502 | Extracellular | ||||
Sequence: ERLNMDYWKILAAQHKCKMNNQTKTLDCLMAASIPAVE | ||||||
Transmembrane | 503-523 | Helical; Name=7 | ||||
Sequence: IFMVKIFMLLVVGITSGMWIW | ||||||
Topological domain | 524-581 | Cytoplasmic | ||||
Sequence: TSKTLQSWQQVCSRRLKKKSRRKPASVITSGGIYKKAQHPQKTHHGKYEIPAQSPTCV |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 804 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-20 | UniProt | |||||
Sequence: MQRPGPRLWLVLQVMGSCAA | |||||||
Chain | PRO_0000013005 | 21-581 | UniProt | Frizzled-10 | |||
Sequence: ISSMDMERPGDGKCQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHGHLRFFLCSLYAPMCTEQVSTPIPACRVMCEQARLKCSPIMEQFNFKWPDSLDCRKLPNKNDPNYLCMEAPNNGSDEPTRGSGLFPPLFRPQRPHSAQEHPLKDGGPGRGGCDNPGKFHHVEKSASCAPLCTPGVDVYWSREDKRFAVVWLAIWAVLCFFSSAFTVLTFLIDPARFRYPERPIIFLSMCYCVYSVGYLIRLFAGAESIACDRDSGQLYVIQEGLESTGCTLVFLVLYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIEANSSYFHLAAWAIPAVKTILILVMRRVAGDELTGVCYVGSMDVNALTGFVLIPLACYLVIGTSFILSGFVALFHIRRVMKTGGENTDKLEKLMVRIGLFSVLYTVPATCVIACYFYERLNMDYWKILAAQHKCKMNNQTKTLDCLMAASIPAVEIFMVKIFMLLVVGITSGMWIWTSKTLQSWQQVCSRRLKKKSRRKPASVITSGGIYKKAQHPQKTHHGKYEIPAQSPTCV | |||||||
Disulfide bond | 34↔95 | UniProt | |||||
Sequence: CQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHGHLRFFLCSLYAPMC | |||||||
Disulfide bond | 42↔88 | UniProt | |||||
Sequence: CKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHGHLRFFLC | |||||||
Glycosylation | 48 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 79↔117 | UniProt | |||||
Sequence: CHGHLRFFLCSLYAPMCTEQVSTPIPACRVMCEQARLKC | |||||||
Disulfide bond | 106↔147 | UniProt | |||||
Sequence: CRVMCEQARLKCSPIMEQFNFKWPDSLDCRKLPNKNDPNYLC | |||||||
Disulfide bond | 110↔134 | UniProt | |||||
Sequence: CEQARLKCSPIMEQFNFKWPDSLDC | |||||||
Glycosylation | 153 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 485 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 553 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 577 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated by ZNRF3, leading to its degradation by the proteasome.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highest levels in the placenta and fetal kidney, followed by fetal lung and brain. In adult brain, abundantly expressed in the cerebellum, followed by cerebral cortex, medulla and spinal cord; very low levels in total brain, frontal lobe, temporal lobe and putamen. Weak expression detected in adult brain, heart, lung, skeletal muscle, pancreas, spleen and prostate.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with WNT7B (By similarity).
Interacts with MYOC (PubMed:19188438).
Interacts with MYOC (PubMed:19188438).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9ULW2 | CCNDBP1 O95273 | 3 | EBI-8803802, EBI-748961 | |
BINARY | Q9ULW2 | CYSRT1 A8MQ03 | 3 | EBI-8803802, EBI-3867333 | |
BINARY | Q9ULW2 | HILPDA Q9Y5L2 | 2 | EBI-8803802, EBI-8803836 | |
BINARY | Q9ULW2 | KRTAP1-1 Q07627 | 3 | EBI-8803802, EBI-11959885 | |
BINARY | Q9ULW2 | KRTAP10-8 P60410 | 3 | EBI-8803802, EBI-10171774 | |
BINARY | Q9ULW2 | NOTCH2NLC P0DPK4 | 3 | EBI-8803802, EBI-22310682 | |
BINARY | Q9ULW2 | P4HB P07237 | 3 | EBI-8803802, EBI-395883 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-150 | FZ | ||||
Sequence: PGDGKCQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHGHLRFFLCSLYAPMCTEQVSTPIPACRVMCEQARLKCSPIMEQFNFKWPDSLDCRKLPNKNDPNYLCMEA | ||||||
Motif | 526-531 | Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members | ||||
Sequence: KTLQSW | ||||||
Region | 560-581 | Disordered | ||||
Sequence: AQHPQKTHHGKYEIPAQSPTCV | ||||||
Motif | 579-581 | PDZ-binding | ||||
Sequence: TCV |
Domain
Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.
The FZ domain is involved in binding with Wnt ligands.
Sequence similarities
Belongs to the G-protein coupled receptor Fz/Smo family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length581
- Mass (Da)65,336
- Last updated2000-05-01 v1
- ChecksumE9B7E51FA7C87B26
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F5H450 | F5H450_HUMAN | FZD10 | 454 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB027464 EMBL· GenBank· DDBJ | BAA84093.1 EMBL· GenBank· DDBJ | mRNA | ||
BC074997 EMBL· GenBank· DDBJ | AAH74997.1 EMBL· GenBank· DDBJ | mRNA | ||
BC074998 EMBL· GenBank· DDBJ | AAH74998.1 EMBL· GenBank· DDBJ | mRNA |