Q9Z138 · ROR2_MOUSE
- ProteinTyrosine-protein kinase transmembrane receptor ROR2
- GeneRor2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids944 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tyrosine-protein kinase receptor which may be involved in the early formation of the chondrocytes. It seems to be required for cartilage and growth plate development (PubMed:10700181).
Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation. In contrast, has also been shown to have very little tyrosine kinase activity in vitro. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated signaling (By similarity).
Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation. In contrast, has also been shown to have very little tyrosine kinase activity in vitro. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated signaling (By similarity).
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Cofactor
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein kinase transmembrane receptor ROR2
- EC number
- Short namesmROR2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9Z138
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 34-403 | Extracellular | ||||
Sequence: EVEDSEAIDTLGQPDGPDSPLPTLKGYFLNFLEPVNNITIVQGQTAILHCKVAGNPPPNVRWLKNDAPVVQEPRRVIIRKTEYGSRLRIQDLDTTDTGYYQCVATNGLKTITATGVLYVRLGPTHSPNHNFQDDDQEDGFCQPYRGIACARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTQLSDQCSQFAIPSFCHFVFPLCDARSRAPKPRELCRDECEVLENDLCRQEYTIARSNPLILMRLQLPKCEALPMPESPDAANCMRIGIPAERLGRYHQCYNGSGADYRGMASTTKSGHQCQPWALQHPHSHRLSSTEFPELGGGHAYCRNPGGQVEGPWCFTQNKNVRVELCDVPPCSPRDGSKMG | ||||||
Transmembrane | 404-424 | Helical | ||||
Sequence: ILYILVPSIAIPLVIACLFFL | ||||||
Topological domain | 425-944 | Cytoplasmic | ||||
Sequence: VCMCRNKQKASASTPQRRQLMASPSQDMEMPLISQHKQAKLKEISLSTVRFMEELGEDRFGKVYKGHLFGPAPGEPTQAVAIKTLKDKAEGPLREEFRQEAMLRARLQHPNIVCLLGVVTKDQPLSMIFSYCSHGDLHEFLVMRSPHSDVGSTDDDRTVKSALEPPDFVHVVAQIAAGMEFLSSHHVVHKDLATRNVLVYDKLNVRISDLGLFREVYSADYYKLMGNSLLPIRWMSPEAVMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVVEMIRSRQVLPCPDDCPAWVYALMIECWNEFPSRRPRFKDIHSRLRSWGNLSNYNSSAQTSGASNTTQTSSLSTSPVSNVSNARYMAPKQKAQPFPQPQFIPMKGQIRPLVPPAQLYIPVNGYQPVPAYGAYLPNFYPVQIPMQMAPQQVPPQMVPKPSSHHSGSGSTSTGYVTTAPSNTSVADRAALLSEGTEDAQNIAEDVAQSPVQEAEEEEEGSVPETELLGDNDTLQVTEAAHVQLEA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-33 | |||||
Sequence: MARGWVRPSRVPLCARAVWTAAALLLWTPWTAG | ||||||
Chain | PRO_0000024461 | 34-944 | Tyrosine-protein kinase transmembrane receptor ROR2 | |||
Sequence: EVEDSEAIDTLGQPDGPDSPLPTLKGYFLNFLEPVNNITIVQGQTAILHCKVAGNPPPNVRWLKNDAPVVQEPRRVIIRKTEYGSRLRIQDLDTTDTGYYQCVATNGLKTITATGVLYVRLGPTHSPNHNFQDDDQEDGFCQPYRGIACARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTQLSDQCSQFAIPSFCHFVFPLCDARSRAPKPRELCRDECEVLENDLCRQEYTIARSNPLILMRLQLPKCEALPMPESPDAANCMRIGIPAERLGRYHQCYNGSGADYRGMASTTKSGHQCQPWALQHPHSHRLSSTEFPELGGGHAYCRNPGGQVEGPWCFTQNKNVRVELCDVPPCSPRDGSKMGILYILVPSIAIPLVIACLFFLVCMCRNKQKASASTPQRRQLMASPSQDMEMPLISQHKQAKLKEISLSTVRFMEELGEDRFGKVYKGHLFGPAPGEPTQAVAIKTLKDKAEGPLREEFRQEAMLRARLQHPNIVCLLGVVTKDQPLSMIFSYCSHGDLHEFLVMRSPHSDVGSTDDDRTVKSALEPPDFVHVVAQIAAGMEFLSSHHVVHKDLATRNVLVYDKLNVRISDLGLFREVYSADYYKLMGNSLLPIRWMSPEAVMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVVEMIRSRQVLPCPDDCPAWVYALMIECWNEFPSRRPRFKDIHSRLRSWGNLSNYNSSAQTSGASNTTQTSSLSTSPVSNVSNARYMAPKQKAQPFPQPQFIPMKGQIRPLVPPAQLYIPVNGYQPVPAYGAYLPNFYPVQIPMQMAPQQVPPQMVPKPSSHHSGSGSTSTGYVTTAPSNTSVADRAALLSEGTEDAQNIAEDVAQSPVQEAEEEEEGSVPETELLGDNDTLQVTEAAHVQLEA | ||||||
Glycosylation | 70 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 83↔135 | |||||
Sequence: CKVAGNPPPNVRWLKNDAPVVQEPRRVIIRKTEYGSRLRIQDLDTTDTGYYQC | ||||||
Disulfide bond | 174↔239 | |||||
Sequence: CQPYRGIACARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTQLSDQCSQFAIPSFCHFVFPLC | ||||||
Disulfide bond | 182↔232 | |||||
Sequence: CARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTQLSDQCSQFAIPSFC | ||||||
Glycosylation | 188 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 223↔264 | |||||
Sequence: CSQFAIPSFCHFVFPLCDARSRAPKPRELCRDECEVLENDLC | ||||||
Disulfide bond | 252↔300 | |||||
Sequence: CRDECEVLENDLCRQEYTIARSNPLILMRLQLPKCEALPMPESPDAANC | ||||||
Disulfide bond | 256↔286 | |||||
Sequence: CEVLENDLCRQEYTIARSNPLILMRLQLPKC | ||||||
Disulfide bond | 316↔394 | |||||
Sequence: CYNGSGADYRGMASTTKSGHQCQPWALQHPHSHRLSSTEFPELGGGHAYCRNPGGQVEGPWCFTQNKNVRVELCDVPPC | ||||||
Glycosylation | 318 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 337↔377 | |||||
Sequence: CQPWALQHPHSHRLSSTEFPELGGGHAYCRNPGGQVEGPWC | ||||||
Disulfide bond | 365↔389 | |||||
Sequence: CRNPGGQVEGPWCFTQNKNVRVELC | ||||||
Modified residue | 646 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | ||||||
Modified residue | 785 | Asymmetric dimethylarginine | ||||
Sequence: R |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
From 9.5 to 11.5 dpc, expressed in the branchial arches, otic vesicle, limb buds, somites, craniofacial mesenchyme and tail buds. At 14.5 dpc, expressed in the developing tongue, nasal cavity, palate, adrenal gland, in the forebrain, dorsal root ganglia and in the somites. At 14.5 dpc, also detected in lung, rib cartilage, kidney and intestine (at protein level).
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 55-145 | Ig-like C2-type | ||||
Sequence: PTLKGYFLNFLEPVNNITIVQGQTAILHCKVAGNPPPNVRWLKNDAPVVQEPRRVIIRKTEYGSRLRIQDLDTTDTGYYQCVATNGLKTIT | ||||||
Domain | 169-303 | FZ | ||||
Sequence: QEDGFCQPYRGIACARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTQLSDQCSQFAIPSFCHFVFPLCDARSRAPKPRELCRDECEVLENDLCRQEYTIARSNPLILMRLQLPKCEALPMPESPDAANCMRI | ||||||
Domain | 316-394 | Kringle | ||||
Sequence: CYNGSGADYRGMASTTKSGHQCQPWALQHPHSHRLSSTEFPELGGGHAYCRNPGGQVEGPWCFTQNKNVRVELCDVPPC | ||||||
Domain | 473-746 | Protein kinase | ||||
Sequence: VRFMEELGEDRFGKVYKGHLFGPAPGEPTQAVAIKTLKDKAEGPLREEFRQEAMLRARLQHPNIVCLLGVVTKDQPLSMIFSYCSHGDLHEFLVMRSPHSDVGSTDDDRTVKSALEPPDFVHVVAQIAAGMEFLSSHHVVHKDLATRNVLVYDKLNVRISDLGLFREVYSADYYKLMGNSLLPIRWMSPEAVMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVVEMIRSRQVLPCPDDCPAWVYALMIECWNEFPSRRPRFKDIHSRL | ||||||
Region | 757-779 | Disordered | ||||
Sequence: SSAQTSGASNTTQTSSLSTSPVS | ||||||
Region | 850-879 | Disordered | ||||
Sequence: QVPPQMVPKPSSHHSGSGSTSTGYVTTAPS | ||||||
Compositional bias | 856-879 | Polar residues | ||||
Sequence: VPKPSSHHSGSGSTSTGYVTTAPS | ||||||
Region | 898-929 | Disordered | ||||
Sequence: QNIAEDVAQSPVQEAEEEEEGSVPETELLGDN | ||||||
Compositional bias | 908-923 | Acidic residues | ||||
Sequence: PVQEAEEEEEGSVPET |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length944
- Mass (Da)105,005
- Last updated2011-07-27 v2
- Checksum03B00784CFFF4489
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 110 | in Ref. 1; BAA75481 | ||||
Sequence: I → V | ||||||
Sequence conflict | 242 | in Ref. 1; BAA75481 | ||||
Sequence: R → C | ||||||
Sequence conflict | 372 | in Ref. 1; BAA75481 | ||||
Sequence: V → M | ||||||
Sequence conflict | 398 | in Ref. 1; BAA75481 | ||||
Sequence: D → Y | ||||||
Sequence conflict | 612 | in Ref. 1; BAA75481 | ||||
Sequence: V → C | ||||||
Compositional bias | 856-879 | Polar residues | ||||
Sequence: VPKPSSHHSGSGSTSTGYVTTAPS | ||||||
Sequence conflict | 897 | in Ref. 1; BAA75481 | ||||
Sequence: A → V | ||||||
Compositional bias | 908-923 | Acidic residues | ||||
Sequence: PVQEAEEEEEGSVPET |
Keywords
- Technical term