O08721 · UNC5A_RAT
- ProteinNetrin receptor UNC5A
- GeneUnc5a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids898 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for netrin required for axon guidance (PubMed:10399920, PubMed:9126742).
Functions in the netrin signaling pathway and promotes neurite outgrowth in response to NTN1 (PubMed:19755150).
Mediates axon repulsion of neuronal growth cones in the developing nervous system in response to netrin (PubMed:10399920).
Axon repulsion in growth cones may be mediated by its association with DCC that may trigger signaling for repulsion (PubMed:10399920).
It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (PubMed:11387206, PubMed:12598531).
Functions in the netrin signaling pathway and promotes neurite outgrowth in response to NTN1 (PubMed:19755150).
Mediates axon repulsion of neuronal growth cones in the developing nervous system in response to netrin (PubMed:10399920).
Axon repulsion in growth cones may be mediated by its association with DCC that may trigger signaling for repulsion (PubMed:10399920).
It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (PubMed:11387206, PubMed:12598531).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 396-397 | Cleavage; by caspase-3 | ||||
Sequence: DS |
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 | membrane raft | |
Cellular Component | neuron projection membrane | |
Cellular Component | neuronal cell body membrane | |
Cellular Component | plasma membrane | |
Molecular Function | netrin receptor activity | |
Biological Process | anterior/posterior axon guidance | |
Biological Process | apoptotic process | |
Biological Process | axon guidance | |
Biological Process | netrin-activated signaling pathway | |
Biological Process | neuron projection development |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNetrin receptor UNC5A
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionO08721
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: The interaction with PRKCABP regulates its surface expression and leads to its removal from the surface of neurons and growth cones (PubMed:14672991).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 26-361 | Extracellular | ||||
Sequence: QQSATVANPVPGANPDLLPHFLVEPEDVYIVKNKPVLLVCKAVPATQIFFKCNGEWVRQVDHVIERSTDSSSGLPTMEVRINVSRQQVEKVFGLEEYWCQCVAWSSSGTTKSQKAYIRIAYLRKNFEQEPLAKEVSLEQGIVLPCRPPEGIPPAEVEWLRNEDLVDPSLDPNVYITREHSLVVRQARLADTANYTCVAKNIVARRRSTSAAVIVYVNGGWSTWTEWSVCSASCGRGWQKRSRSCTNPAPLNGGAFCEGQNVQKTACATLCPVDGSWSSWSKWSACGLDCTHWRSRECSDPAPRNGGEECRGADLDTRNCTSDLCLHTASCPEDVAL | ||||||
Transmembrane | 362-382 | Helical | ||||
Sequence: YIGLVAVAVCLFLLLLALGLI | ||||||
Topological domain | 383-898 | Cytoplasmic | ||||
Sequence: YCRKKEGLDSDVADSSILTSGFQPVSIKPSKADNPHLLTIQPDLSTTTTTYQGSLCSRQDGPSPKFQLSNGHLLSPLGSGRHTLHHSSPTSEAEDFVSRLSTQNYFRSLPRGTSNMAYGTFNFLGGRLMIPNTGISLLIPPDAIPRGKIYEIYLTLHKPEDVRLPLAGCQTLLSPVVSCGPPGVLLTRPVILAMDHCGEPSPDSWSLRLKKQSCEGSWEDVLHLGEESPSHLYYCQLEAGACYVFTEQLGRFALVGEALSVAATKRLRLLLFAPVACTSLEYNIRVYCLHDTHDALKEVVQLEKQLGGQLIQEPRVLHFKDSYHNLRLSIHDVPSSLWKSKLLVSYQEIPFYHIWNGTQQYLHCTFTLERINASTSDLACKVWVWQVEGDGQSFNINFNITKDTRFAELLALESEGGVPALVGPSAFKIPFLIRQKIIASLDPPCSRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLGQLAAAVAGLGQPDAGLFTVSEAEC |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 896-898 | Abolishes interaction with PRKCABP. | ||||
Sequence: Missing |
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MAVRPGLWPVLLGIVLAAWLRGSGA | ||||||
Chain | PRO_0000036070 | 26-898 | Netrin receptor UNC5A | |||
Sequence: QQSATVANPVPGANPDLLPHFLVEPEDVYIVKNKPVLLVCKAVPATQIFFKCNGEWVRQVDHVIERSTDSSSGLPTMEVRINVSRQQVEKVFGLEEYWCQCVAWSSSGTTKSQKAYIRIAYLRKNFEQEPLAKEVSLEQGIVLPCRPPEGIPPAEVEWLRNEDLVDPSLDPNVYITREHSLVVRQARLADTANYTCVAKNIVARRRSTSAAVIVYVNGGWSTWTEWSVCSASCGRGWQKRSRSCTNPAPLNGGAFCEGQNVQKTACATLCPVDGSWSSWSKWSACGLDCTHWRSRECSDPAPRNGGEECRGADLDTRNCTSDLCLHTASCPEDVALYIGLVAVAVCLFLLLLALGLIYCRKKEGLDSDVADSSILTSGFQPVSIKPSKADNPHLLTIQPDLSTTTTTYQGSLCSRQDGPSPKFQLSNGHLLSPLGSGRHTLHHSSPTSEAEDFVSRLSTQNYFRSLPRGTSNMAYGTFNFLGGRLMIPNTGISLLIPPDAIPRGKIYEIYLTLHKPEDVRLPLAGCQTLLSPVVSCGPPGVLLTRPVILAMDHCGEPSPDSWSLRLKKQSCEGSWEDVLHLGEESPSHLYYCQLEAGACYVFTEQLGRFALVGEALSVAATKRLRLLLFAPVACTSLEYNIRVYCLHDTHDALKEVVQLEKQLGGQLIQEPRVLHFKDSYHNLRLSIHDVPSSLWKSKLLVSYQEIPFYHIWNGTQQYLHCTFTLERINASTSDLACKVWVWQVEGDGQSFNINFNITKDTRFAELLALESEGGVPALVGPSAFKIPFLIRQKIIASLDPPCSRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLGQLAAAVAGLGQPDAGLFTVSEAEC | ||||||
Disulfide bond | 65↔126 | |||||
Sequence: CKAVPATQIFFKCNGEWVRQVDHVIERSTDSSSGLPTMEVRINVSRQQVEKVFGLEEYWCQC | ||||||
Disulfide bond | 77↔124 | |||||
Sequence: CNGEWVRQVDHVIERSTDSSSGLPTMEVRINVSRQQVEKVFGLEEYWC | ||||||
Glycosylation | 107 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 170↔221 | |||||
Sequence: CRPPEGIPPAEVEWLRNEDLVDPSLDPNVYITREHSLVVRQARLADTANYTC | ||||||
Glycosylation | 218 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 245 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 248 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 251 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Disulfide bond | 254↔291 | |||||
Sequence: CSASCGRGWQKRSRSCTNPAPLNGGAFCEGQNVQKTAC | ||||||
Disulfide bond | 258↔295 | |||||
Sequence: CGRGWQKRSRSCTNPAPLNGGAFCEGQNVQKTACATLC | ||||||
Disulfide bond | 269↔281 | |||||
Sequence: CTNPAPLNGGAFC | ||||||
Glycosylation | 301 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 304 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Disulfide bond | 310↔344 | |||||
Sequence: CGLDCTHWRSRECSDPAPRNGGEECRGADLDTRNC | ||||||
Disulfide bond | 314↔349 | |||||
Sequence: CTHWRSRECSDPAPRNGGEECRGADLDTRNCTSDLC | ||||||
Disulfide bond | 322↔334 | |||||
Sequence: CSDPAPRNGGEEC | ||||||
Glycosylation | 343 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Phosphorylated on cytoplasmic tyrosine residues (By similarity).
Phosphorylated by PKC in vitro
Phosphorylated by PKC in vitro
Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis.
The two extracellular TSRs of UNC5A contain WxxWxxWxxC motifs that can be C-mannosylated on all tryptophans. DPY19L1 preferentially mannosylates the first two tryptophans and DPY19L3 prefers the third. C-mannosylation by DPY19L1 is required for transport of UNC5A from the endoplasmic reticulum to the cell surface.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Mainly expressed in regions of differentiating neurons. Expressed at early stages of neural tube development in the ventral spinal cord. In developing hindbrain, it colocalizes with a number of cranial motor neuron subpopulations from embryonic E11 to E14, while DCC is expressed by motor neurons at E12. Also expressed in non-neural structures, such as the basal plane of the hindbrain and midbrain, in the developing hypothalamus, thalamus and in the pallidum.
Interaction
Subunit
Homodimer and homooligomer (PubMed:19755150).
Interacts with the cytoplasmic part of DCC (PubMed:10399920).
Interacts with MAGED1 (PubMed:12598531).
Interacts with PRKCABP, possibly mediating some interaction with PKC (PubMed:14672991).
Interacts (via extracellular domain) with FLRT2 (via extracellular domain) (By similarity).
Interacts (via extracellular domain) with FLRT3 (via extracellular domain) (By similarity).
Interacts with the cytoplasmic part of DCC (PubMed:10399920).
Interacts with MAGED1 (PubMed:12598531).
Interacts with PRKCABP, possibly mediating some interaction with PKC (PubMed:14672991).
Interacts (via extracellular domain) with FLRT2 (via extracellular domain) (By similarity).
Interacts (via extracellular domain) with FLRT3 (via extracellular domain) (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 44-141 | Ig-like | ||||
Sequence: PHFLVEPEDVYIVKNKPVLLVCKAVPATQIFFKCNGEWVRQVDHVIERSTDSSSGLPTMEVRINVSRQQVEKVFGLEEYWCQCVAWSSSGTTKSQKAY | ||||||
Domain | 155-238 | Ig-like C2-type | ||||
Sequence: PLAKEVSLEQGIVLPCRPPEGIPPAEVEWLRNEDLVDPSLDPNVYITREHSLVVRQARLADTANYTCVAKNIVARRRSTSAAVI | ||||||
Domain | 242-296 | TSP type-1 1 | ||||
Sequence: NGGWSTWTEWSVCSASCGRGWQKRSRSCTNPAPLNGGAFCEGQNVQKTACATLCP | ||||||
Domain | 298-350 | TSP type-1 2 | ||||
Sequence: DGSWSSWSKWSACGLDCTHWRSRECSDPAPRNGGEECRGADLDTRNCTSDLCL | ||||||
Domain | 497-640 | ZU5 | ||||
Sequence: NMAYGTFNFLGGRLMIPNTGISLLIPPDAIPRGKIYEIYLTLHKPEDVRLPLAGCQTLLSPVVSCGPPGVLLTRPVILAMDHCGEPSPDSWSLRLKKQSCEGSWEDVLHLGEESPSHLYYCQLEAGACYVFTEQLGRFALVGEA | ||||||
Region | 661-679 | Interaction with DCC | ||||
Sequence: SLEYNIRVYCLHDTHDALK | ||||||
Domain | 817-897 | Death | ||||
Sequence: QKIIASLDPPCSRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLGQLAAAVAGLGQPDAGLFTVSEAE |
Domain
The ZU5 domain mediates the interaction with MAGED1, which participates in the induction of apoptosis.
Sequence similarities
Belongs to the unc-5 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length898
- Mass (Da)98,841
- Last updated1997-07-01 v1
- Checksum7A3CBCB9E7ACA135
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JZN2 | A0A0G2JZN2_RAT | Unc5a | 842 | ||
A0A8I5YBB0 | A0A8I5YBB0_RAT | Unc5a | 898 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U87305 EMBL· GenBank· DDBJ | AAB57678.1 EMBL· GenBank· DDBJ | mRNA |