Q5RAG8

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
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway
pon:100172658
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)

229-310 (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 Q5RAG8

Entry ID Method Resolution Chain Position Source
AF-Q5RAG8-F1 Predicted AlphaFoldDB

No variants for Q5RAG8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5RAG8

No associated diseases with Q5RAG8

5 regional properties for Q5RAG8

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

2 GO annotations of cellular component

Name Definition
endoplasmic reticulum lumen The volume enclosed by the membranes of the endoplasmic reticulum.
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.

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.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIWYILIIGI LLPQSLAHPG FFTSIGQMTD LIHTEKDLVT SLKDYIKAEE DKLEQIKKWA
70 80 90 100 110 120
EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LVLKDMSDGF ISNLTIQRQY
130 140 150 160 170 180
FPNDEDQVGA AKALLRLQDT YNLDTDTISK GNLPGVKHKS FLTAEDCFEL GKVAYTEADY
190 200 210 220 230 240
YHTELWMEQA LRQLDEGEIS TIDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR
250 260 270 280 290 300
ANGNLKYFEY IMAKEKDVNK SASDDQSDQK TTPKKKGVAV DYLPERQKYE MLCRGEGIKM
310 320 330 340 350 360
TPRRQKKLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRL
370 380 390 400 410 420
RRATISNPIT GDLETVHYRI SKSAWLSGYE NPVVSRINMR IQDLTGLDVS TAEELQVANY
430 440 450 460 470 480
GVGGQYEPHF DFARKDEPDA FKELGTGNRI ATWLFYMSDV SAGGATVFPE VGASVWPKKG
490 500 510 520 530
TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE