Q60716 · P4HA2_MOUSE
- ProteinProlyl 4-hydroxylase subunit alpha-2
- GeneP4ha2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids537 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Catalytic activity
- 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]This reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Fe2+ ion per subunit.
Activity regulation
Inhibited by poly(L-proline) only at very high concentrations.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
12 μM | 2-oxoglutarate |
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | procollagen-proline 4-dioxygenase complex | |
Molecular Function | iron ion binding | |
Molecular Function | L-ascorbic acid binding | |
Molecular Function | procollagen-proline 4-dioxygenase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProlyl 4-hydroxylase subunit alpha-2
- EC number
- Short names4-PH alpha-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ60716
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MKLQVLVLVLLMSWFGVLSWVQA | ||||||
Chain | PRO_0000022727 | 24-537 | Prolyl 4-hydroxylase subunit alpha-2 | |||
Sequence: EFFTSIGHMTDLIYAEKDLVQSLKEYILVEEAKLAKIKSWASKMEALTSRSAADPEGYLAHPVNAYKLVKRLNTDWPALGDLVLQDASAGFVANLSVQRQFFPTDEDESGAARALMRLQDTYKLDPDTISRGELPGTKYQAMLSVDDCFGLGRSAYNEGDYYHTVLWMEQVLKQLDAGEEATVTKSLVLDYLSYAVFQLGDLHRAVELTRRLLSLDPSHERAGGNLRYFERLLEEERGKSLSNQTDAGLATQENLYERPTDYLPERDVYESLCRGEGVKLTPRRQKKLFCRYHHGNRVPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPKLARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVANYGMGGQYEPHFDFSRSDDEDAFKRLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKKGTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGTTEVD | ||||||
Glycosylation | 117 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 266 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 482 | N6-succinyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at least in brain, heart and lung.
Gene expression databases
Interaction
Subunit
Heterotetramer of two alpha-2 chains and two beta chains (P4HB) (the beta chain is the multi-functional PDI), where P4HB plays the role of a structural subunit; this tetramer catalyzes the formation of 4-hydroxyproline in collagen.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 209-242 | TPR | ||||
Sequence: SLVLDYLSYAVFQLGDLHRAVELTRRLLSLDPSH | ||||||
Domain | 414-522 | Fe2OG dioxygenase | ||||
Sequence: TAELLQVANYGMGGQYEPHFDFSRSDDEDAFKRLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKKGTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHE |
Sequence similarities
Belongs to the P4HA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q60716-1
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.
- NameIIb
- Synonymsalpha(II)
- Length537
- Mass (Da)61,002
- Last updated1996-11-01 v1
- ChecksumC47D976C75E82518
Q60716-2
- NameIIa
- Differences from canonical
- 438-453: SDDEDAFKRLGTGNRV → RPFDSGLKTEGNRL
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_004507 | 438-453 | in isoform IIa | |||
Sequence: SDDEDAFKRLGTGNRV → RPFDSGLKTEGNRL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U16163 EMBL· GenBank· DDBJ | AAC52198.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ314858 EMBL· GenBank· DDBJ | CAC85690.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ314858 EMBL· GenBank· DDBJ | CAC85691.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC018411 EMBL· GenBank· DDBJ | AAH18411.1 EMBL· GenBank· DDBJ | mRNA |