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 Q1RMU3

Entry ID Method Resolution Chain Position Source
AF-Q1RMU3-F1 Predicted AlphaFoldDB

24 variants for Q1RMU3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs435633383 21 F>V No EVA
rs443129649 23 T>P No EVA
rs478310888 107 S>L No EVA
rs478687100 124 D>E No EVA
rs451391994 205 V>I No EVA
rs437835480 206 S>A No EVA
rs475947776 228 T>I No EVA
rs457935106 293 C>* No EVA
rs444311863 294 R>G No EVA
rs449982538 305 Q>E No EVA
rs436386326 309 F>C No EVA
rs468285287 316 N>S No EVA
rs459552468 324 A>D No EVA
rs479616006 324 A>S No EVA
rs445842113 329 E>D No EVA
rs477131672 331 E>Q No EVA
rs457612594 332 W>* No EVA
rs457612594 332 W>L No EVA
rs463486415 332 W>R No EVA
rs474623461 336 R>G No EVA
rs441510535 341 H>P No EVA
rs472728461 347 A>V No EVA
rs479876675 361 R>G No EVA
rs460366489 362 R>G No EVA

No associated diseases with Q1RMU3

5 regional properties for Q1RMU3

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 - 154 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 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.

3 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.
procollagen-proline 4-dioxygenase activity Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2.

1 GO annotations of biological process

Name Definition
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
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
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
MIWYILVVGI 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 GDLPGVKHKS FLTVEDCFEL GKVAYTEADY
190 200 210 220 230 240
YHTELWMEQA LRQLDEGEVS TVDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR
250 260 270 280 290 300
ANGNLKYFEY IMAKEKDANK SSSDDQSDQK TTLKKKGAAV DYLPERQKYE MLCRGEGIKM
310 320 330 340 350 360
TPRRQKKLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE VVKDLAKPRL
370 380 390 400 410 420
RRATISNPIT GDLETVHYRI SKSAWLSGYE NPVVSRINMR IQDLTGLDVS TAEELQVANY
430 440 450 460 470 480
GVGGQYEPHF DFARKDEPDA FKELGTGNRI ATWLFYMSDV LAGGATVFPE VGASVWPKKG
490 500 510 520 530
TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE