Q60715

PR
Gene name
P4ha1
Protein name
Prolyl 4-hydroxylase subunit alpha-1
Names
4-PH alpha-1, Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:18451
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)

31-102 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q60715

Entry ID Method Resolution Chain Position Source
AF-Q60715-F1 Predicted AlphaFoldDB

18 variants for Q60715

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389043859 8 M>L No EVA
rs235777577 15 S>F No EVA
rs3389101978 87 L>S No EVA
rs3389105502 199 L>R No EVA
rs3389102176 224 A>T No EVA
rs3389100189 241 A>D No EVA
rs3389109625 273 P>S No EVA
rs3389101971 382 K>Q No EVA
rs3389087768 383 S>C No EVA
rs3389101730 384 A>T No EVA
rs3389111632 402 Q>R No EVA
rs3389074563 450 I>F No EVA
rs3389100375 450 I>N No EVA
rs3389100178 459 D>V No EVA
rs3389096646 478 K>Q No EVA
rs3389109643 492 G>W No EVA
rs3389074529 503 C>Y No EVA
rs3389111620 512 V>E No EVA

No associated diseases with Q60715

5 regional properties for Q60715

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
  • Endoplasmic reticulum lumen
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 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.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
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.

2 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 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
P54001 P4ha1 Prolyl 4-hydroxylase subunit alpha-1 Rattus norvegicus (Rat) PR
Q20065 phy-2 Prolyl 4-hydroxylase subunit alpha-2 Caenorhabditis elegans PR
Q9ZW86 P4H1 Prolyl 4-hydroxylase 1 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SZT0 P4H11 Probable prolyl 4-hydroxylase 11 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MIWVVLMMAI LLPQSLAHPG 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 GNLPGVQHKS FLTAEDCFEL GKVAYTEADY
190 200 210 220 230 240
YHTELWMEQA LTQLEEGELS TVDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR
250 260 270 280 290 300
ANGNLVYFEY IMSKEKDANK SASGDQSDQK TAPKKKGIAV DYLPERQKYE MLCRGEGIKM
310 320 330 340 350 360
TPRRQKRLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRL
370 380 390 400 410 420
RRATISNPVT GALETVHYRI 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