Q9ZW86 · P4H1_ARATH
- ProteinProlyl 4-hydroxylase 1
- GeneP4H1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids283 (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 proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxylates preferentially prolines in second positions in the -Pro-Pro-Gly-triplets. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins. Can hydroxylate collagen-like peptides and hypoxia-inducible transcription factor peptides.
Miscellaneous
Plants over-expressing P4H1 show absence of trichome on leaf and petal surfaces, increased root hair and reduction in seed size.
Catalytic activity
- 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Fe2+ ion per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
130 μM | 2-oxoglutarate | |||||
2 μM | poly(L-proline) polypeptides of 5-10 kDa | |||||
0.2 μM | poly(L-proline) polypeptides of 10-20 kDa | |||||
60 μM | (Ala-Thr-Pro-Pro-Pro-Val)3 peptide present in arabinogalactan protein | |||||
10 μM | Ser-Pro-Pro-Pro-Pro-Val-Ser-Pro-Pro-Pro-Val-Ser-Pro-Pro-Pro-Pro-Val peptide present in extensin protein | |||||
40 μM | Ser-Pro-Pro-Pro-Val-Tyr-Lys-Ser-Pro-Pro-Pro-Pro-Val-Lys-His-Tyr-Ser-Pro-Pro-Pro-Val peptide present in extensin protein | |||||
60 μM | (Pro-Pro-Gly)10 | |||||
120 μM | (Pro-Pro-Gly)5 | |||||
100 μM | (Ala-Pro-Gly)5 | |||||
280 μM | (Pro-Ala-Gly)5 |
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi cis cisterna | |
Molecular Function | iron ion binding | |
Molecular Function | L-ascorbic acid binding | |
Molecular Function | procollagen-proline 4-dioxygenase activity | |
Biological Process | peptidyl-proline hydroxylation to 4-hydroxy-L-proline |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProlyl 4-hydroxylase 1
- EC number
- Short namesAtP4H-1 ; AtP4H1
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9ZW86
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-6 | Cytoplasmic | ||||
Sequence: MAPAMK | ||||||
Transmembrane | 7-27 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: IVFGLLTFVTVGMVIGSLLQL | ||||||
Topological domain | 28-283 | Lumenal | ||||
Sequence: AFINRLEDSYGTGFPSLRGLRGQNTRYLRDVSRWANDKDAELLRIGNVKPEVVSWSPRIIVLHDFLSPEECEYLKAIARPRLQVSTVVDVKTGKGVKSDVRTSSGMFLTHVERSYPIIQAIEKRIAVFSQVPAENGELIQVLRYEPQQFYKPHHDYFADTFNLKRGGQRVATMLMYLTDDVEGGETYFPLAGDGDCTCGGKIMKGISVKPTKGDAVLFWSMGLDGQSDPRSIHGGCEVLSGEKWSATKWMRQKATS |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 180 | Reduces activity more than 500-fold. | ||||
Sequence: H → A | ||||||
Mutagenesis | 180 | Reduces activity more than 500-fold. | ||||
Sequence: H → E | ||||||
Mutagenesis | 182 | Reduces activity more than 500-fold. | ||||
Sequence: D → A | ||||||
Mutagenesis | 182 | Reduces activity more than 500-fold. | ||||
Sequence: D → E | ||||||
Mutagenesis | 260 | Reduces activity more than 500-fold. | ||||
Sequence: H → A | ||||||
Mutagenesis | 260 | Reduces activity more than 500-fold. | ||||
Sequence: H → E | ||||||
Mutagenesis | 270 | Reduces activity more than 500-fold. | ||||
Sequence: K → A | ||||||
Mutagenesis | 270 | Reduces activity more than 500-fold. | ||||
Sequence: K → R | ||||||
Mutagenesis | 272 | Reduces activity 6-fold. | ||||
Sequence: S → A | ||||||
Mutagenesis | 278 | Reduces activity more than 500-fold. | ||||
Sequence: R → A | ||||||
Mutagenesis | 278 | Reduces activity 4-fold. | ||||
Sequence: R → H |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000429335 | 1-283 | Prolyl 4-hydroxylase 1 | |||
Sequence: MAPAMKIVFGLLTFVTVGMVIGSLLQLAFINRLEDSYGTGFPSLRGLRGQNTRYLRDVSRWANDKDAELLRIGNVKPEVVSWSPRIIVLHDFLSPEECEYLKAIARPRLQVSTVVDVKTGKGVKSDVRTSSGMFLTHVERSYPIIQAIEKRIAVFSQVPAENGELIQVLRYEPQQFYKPHHDYFADTFNLKRGGQRVATMLMYLTDDVEGGETYFPLAGDGDCTCGGKIMKGISVKPTKGDAVLFWSMGLDGQSDPRSIHGGCEVLSGEKWSATKWMRQKATS |
Proteomic databases
Expression
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 162-279 | Fe2OG dioxygenase | ||||
Sequence: NGELIQVLRYEPQQFYKPHHDYFADTFNLKRGGQRVATMLMYLTDDVEGGETYFPLAGDGDCTCGGKIMKGISVKPTKGDAVLFWSMGLDGQSDPRSIHGGCEVLSGEKWSATKWMRQ |
Sequence similarities
Belongs to the P4HA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length283
- Mass (Da)31,530
- Last updated1999-05-01 v1
- ChecksumC4C02FBDB29D3F24
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8AZF5 | A0A1P8AZF5_ARATH | AT-P4H-1 | 191 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC004450 EMBL· GenBank· DDBJ | AAC64297.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC006224 EMBL· GenBank· DDBJ | AAM15158.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC10206.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK117688 EMBL· GenBank· DDBJ | BAC42340.1 EMBL· GenBank· DDBJ | mRNA | ||
BT006098 EMBL· GenBank· DDBJ | AAP04083.1 EMBL· GenBank· DDBJ | mRNA |