Q20065

PR
Gene name
phy-2 (F35G2.4)
Protein name
Prolyl 4-hydroxylase subunit alpha-2
Names
4-PH alpha-2, Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_F35G2.4
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)

229-301 (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 Q20065

Entry ID Method Resolution Chain Position Source
AF-Q20065-F1 Predicted AlphaFoldDB

No variants for Q20065

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q20065

No associated diseases with Q20065

4 regional properties for Q20065

Type Name Position InterPro Accession
domain Oxoglutarate/iron-dependent dioxygenase 401 - 509 IPR005123
domain Prolyl 4-hydroxylase, alpha subunit 325 - 508 IPR006620
domain Prolyl 4-hydroxylase alpha-subunit, N-terminal 22 - 156 IPR013547
domain Prolyl 4-hydroxylase alpha subunit, Fe(2+) 2OG dioxygenase domain 405 - 508 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

2 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.

4 GO annotations of molecular function

Name Definition
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.
peptidyl-proline 4-dioxygenase activity Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl trans-4-hydroxy-L-proline + succinate + CO2.
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
macromolecule modification The covalent alteration of one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological macromolecule, resulting in a change in its properties.
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
P54001 P4ha1 Prolyl 4-hydroxylase subunit alpha-1 Rattus norvegicus (Rat) 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
MRAVLLVCLL AGLAHADLFT AIADLQHMLG AEKDVTTIID QYIEAERARL DDLRRYAHEY
70 80 90 100 110 120
VHRNAHAESV GPEFVTNPIN AYLLIKRLTT EWKKVENIML NNKASTFLKN ITDNRVRSEV
130 140 150 160 170 180
KFPGEEDLSG AATALLRLQD TYSLDTLDLS NGIIGGEKVS NKLSGHDTFE VGRSAYNQKD
190 200 210 220 230 240
YYHCLMWMQV ALVKIENENP PTIEEWEILE YLAYSLYQQG NVRRALSLTK RLAKIAPNHP
250 260 270 280 290 300
RAKGNVKWYE DMLQGKDMVG DLPPIVNKRV EYDGIVERDA YEALCRGEIP PVEPKWKNKL
310 320 330 340 350 360
RCYLKRDKPF LKLAPIKVEI LRFDPLAVLF KNVIHDSEIE VIKELASPKL KRATVQNSKT
370 380 390 400 410 420
GELEHATYRI SKSAWLKGDL DPVIDRVNRR IEDFTNLNQA TSEELQVANY GLGGHYDPHF
430 440 450 460 470 480
DFARKEEKNA FKTLNTGNRI ATVLFYMSQP ERGGATVFNH LGTAVFPSKN DALFWYNLRR
490 500 510 520 530
DGEGDLRTRH AACPVLLGVK WVSNKWIHEK GQEFTRPCGL EEEVQENFIG DLSPYANDP