Q3U0K8 · OGFD1_MOUSE
- ProteinProlyl 3-hydroxylase OGFOD1
- GeneOgfod1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids545 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-62' of small ribosomal subunit uS12 (RPS23), thereby regulating protein translation termination efficiency. Involved in stress granule formation.
Catalytic activity
- 2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 = [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Fe2+ ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 155 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 157 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 169 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 218 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 230 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic stress granule | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Molecular Function | iron ion binding | |
Molecular Function | L-ascorbic acid binding | |
Molecular Function | peptidyl-proline 3-dioxygenase activity | |
Molecular Function | peptidyl-proline dioxygenase activity | |
Biological Process | cell population proliferation | |
Biological Process | protein hydroxylation | |
Biological Process | regulation of translational termination | |
Biological Process | stress granule assembly |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProlyl 3-hydroxylase OGFOD1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3U0K8
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000288975 | 1-545 | Prolyl 3-hydroxylase OGFOD1 | |||
Sequence: MNGKRPADPGPARPMKKGKKQVSAEFSDAVTEEILRKQVAEAWSCRTPFSHEAIALDMDPFLHCVIPNFIQSQDFLEGLHKELLSLDFHEKYNDLYKFQQSDDLKNRKEPHISALRKLMFEDFRAWLSKVSGIDLEPTIDMSCAKYEFTDALLCHDDELEGRRIAFILYLVPSWDRDLGGTLDLYDTDEHLQPKQIVKSLIPSWNKLVFFEVSPVSFHQVSEVLSEETSRLSISGWFYGPSLTRPPTYFEPPIPRNPHIPQDHEILYEWINPAYLEMDYQMQIQEEFEERSEILLKEFLKPEKFAEVCEALEKGDVEWKSHGPPNKRFYEKAEENNLPDVLKECMGLFRSEALFLLLSNLTGLKLHFLAPSEDDETEEKGEGETASAAAGTEEGTSRRPSGPENNQVAAGSHSQENGEQADPEAQEEEAKKESSVPMCQGELRRWKTGHYTLVHDNTKTEFALDLFLYCGCEGWEPEYGGFTSYIAKGEDEELLIVNPENNSLALVYRDRETLRFVKHINHRSLEQSKAFPSRSGFWDFAFIYYE |
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-23 | Disordered | ||||
Sequence: MNGKRPADPGPARPMKKGKKQVS | ||||||
Domain | 137-239 | Fe2OG dioxygenase | ||||
Sequence: PTIDMSCAKYEFTDALLCHDDELEGRRIAFILYLVPSWDRDLGGTLDLYDTDEHLQPKQIVKSLIPSWNKLVFFEVSPVSFHQVSEVLSEETSRLSISGWFYG | ||||||
Region | 371-437 | Disordered | ||||
Sequence: SEDDETEEKGEGETASAAAGTEEGTSRRPSGPENNQVAAGSHSQENGEQADPEAQEEEAKKESSVPM | ||||||
Compositional bias | 389-418 | Polar residues | ||||
Sequence: AGTEEGTSRRPSGPENNQVAAGSHSQENGE |
Sequence similarities
Belongs to the TPA1 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q3U0K8-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length545
- Mass (Da)62,734
- Last updated2005-10-11 v1
- Checksum92F376ABC86CB410
Q3U0K8-2
- Name2
- Differences from canonical
- 220-262: Missing
Q3U0K8-3
- Name3
- Differences from canonical
- 52-52: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D3YTU2 | D3YTU2_MOUSE | Ogfod1 | 530 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 1; BAE38717 | ||||
Sequence: A → V | ||||||
Sequence conflict | 48 | in Ref. 1; BAE38717 | ||||
Sequence: P → S | ||||||
Alternative sequence | VSP_025853 | 52 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 58 | in Ref. 1; BAE38717 | ||||
Sequence: M → V | ||||||
Sequence conflict | 80 | in Ref. 1; BAE38717 | ||||
Sequence: H → Q | ||||||
Alternative sequence | VSP_025854 | 220-262 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 389-418 | Polar residues | ||||
Sequence: AGTEEGTSRRPSGPENNQVAAGSHSQENGE | ||||||
Sequence conflict | 397 | in Ref. 1; BAE38717 | ||||
Sequence: R → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK156765 EMBL· GenBank· DDBJ | BAE33844.1 EMBL· GenBank· DDBJ | mRNA | ||
AK164189 EMBL· GenBank· DDBJ | BAE37671.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166343 EMBL· GenBank· DDBJ | BAE38717.1 EMBL· GenBank· DDBJ | mRNA | ||
BC040267 EMBL· GenBank· DDBJ | AAH40267.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK122532 EMBL· GenBank· DDBJ | BAC65814.1 EMBL· GenBank· DDBJ | mRNA |