P54001
Gene name |
P4ha1 (P4ha) |
Protein name |
Prolyl 4-hydroxylase subunit alpha-1 |
Names |
4-PH alpha-1, Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1 |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:64475 |
EC number |
1.14.11.2: With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P54001
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P54001-F1 | Predicted | AlphaFoldDB |
No variants for P54001
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P54001 | |||||
No associated diseases with P54001
5 regional properties for P54001
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Oxoglutarate/iron-dependent dioxygenase | 411 - 519 | IPR005123 |
| domain | Prolyl 4-hydroxylase, alpha subunit | 335 - 518 | IPR006620 |
| domain | Prolyl 4-hydroxylase alpha-subunit, N-terminal | 24 - 155 | IPR013547 |
| repeat | Tetratricopeptide repeat | 205 - 238 | IPR019734 |
| domain | Prolyl 4-hydroxylase alpha subunit, Fe(2+) 2OG dioxygenase domain | 415 - 518 | IPR044862 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.11.2 | With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum lumen | The volume enclosed by the membranes of the endoplasmic reticulum. |
| procollagen-proline 4-dioxygenase complex | A protein complex that catalyzes the formation of procollagen trans-4-hydroxy-L-proline and succinate from procollagen L-proline and 2-oxoglutarate, requiring Fe2+ and ascorbate. Contains two alpha subunits that contribute to most parts of the catalytic sites, and two beta subunits that are identical to protein-disulfide isomerase. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| identical protein binding | Binding to an identical protein or proteins. |
| iron ion binding | Binding to an iron (Fe) ion. |
| L-ascorbic acid binding | Binding to L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species. |
| procollagen-proline 4-dioxygenase activity | Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| collagen fibril organization | Any process that determines the size and arrangement of collagen fibrils within an extracellular matrix. |
| peptidyl-proline hydroxylation | The hydroxylation of peptidyl-proline to form peptidyl-hydroxyproline. |
| peptidyl-proline hydroxylation to 4-hydroxy-L-proline | The modification of peptidyl-proline to form 4-hydroxy-L-proline; catalyzed by procollagen-proline,2-oxoglutarate-4-dioxygenase. |
8 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q1RMU3 | P4HA1 | Prolyl 4-hydroxylase subunit alpha-1 | Bos taurus (Bovine) | PR |
| P16924 | P4HA1 | Prolyl 4-hydroxylase subunit alpha-1 | Gallus gallus (Chicken) | PR |
| O15460 | P4HA2 | Prolyl 4-hydroxylase subunit alpha-2 | Homo sapiens (Human) | PR |
| P13674 | P4HA1 | Prolyl 4-hydroxylase subunit alpha-1 | Homo sapiens (Human) | PR |
| Q60715 | P4ha1 | Prolyl 4-hydroxylase subunit alpha-1 | Mus musculus (Mouse) | PR |
| Q20065 | phy-2 | Prolyl 4-hydroxylase subunit alpha-2 | Caenorhabditis elegans | PR |
| Q9SZT0 | P4H11 | Probable prolyl 4-hydroxylase 11 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9ZW86 | P4H1 | Prolyl 4-hydroxylase 1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIWGVLMMGI | LLPQCSAHPG | FFTSIGQMTD | LIHNEKDLVT | SLKDYIKAEE | DKLEQIKKWA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EKLDRLTSTA | TKDPEGFVGH | PVNAFKLMKR | LNTEWSELEN | LILKDMSDGF | ISNLTIQRQY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FPNDEDQVGA | AKALFRLQDT | YNLDTNTISK | GNLPGVKHKS | FLTAEDCFEL | GKVAYTEADY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YHTELWMEQA | LMQLEEGEMS | TVDKVSVLDY | LSYAVYQQGD | LDKALLLTKK | LLELDPEHQR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ANGNLVYFEY | IMSKEKDANK | SASGDQSDQK | TTPKKKGIAV | DYLPERQKYE | MLCRGEGIKM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TPRRQKRLFC | RYHDGNRNPK | FILAPAKQED | EWDKPRIIRF | HDIISDAEIE | IVKDLAKPRL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SRATVHDPET | GKLTTAQYRV | SKSAWLSGYE | DPVVSRINMR | IQDLTGLDVS | TAEELQVANY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GVGGQYEPHF | DFARKDEPDA | FRELGTGNRI | ATWLFYMSDV | SAGGATVFPE | VGASVWPKKG |
| 490 | 500 | 510 | 520 | 530 | |
| TAVFWYNLFA | SGEGDYSTRH | AACPVLVGNK | WVSNKWLHER | GQEFRRPCTL | SELE |