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 P24802

Entry ID Method Resolution Chain Position Source
AF-P24802-F1 Predicted AlphaFoldDB

No variants for P24802

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P24802

No associated diseases with P24802

4 regional properties for P24802

Type Name Position InterPro Accession
conserved_site Procollagen-lysine 5-dioxygenase, conserved site 658 - 665 IPR001006
domain Oxoglutarate/iron-dependent dioxygenase 639 - 730 IPR005123
domain Prolyl 4-hydroxylase, alpha subunit 556 - 729 IPR006620
domain Isopenicillin N synthase-like, Fe(2+) 2OG dioxygenase domain 643 - 729 IPR044861

Functions

Description
EC Number 1.14.11.4 With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Subcellular Localization
  • Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side
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).
rough endoplasmic reticulum membrane The lipid bilayer surrounding the rough 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-lysine 5-dioxygenase activity Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.

1 GO annotations of biological process

Name Definition
peptidyl-lysine hydroxylation The hydroxylation of peptidyl-lysine to form peptidyl-hydroxylysine.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O60568 PLOD3 Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 Homo sapiens (Human) PR
Q20679 let-268 Multifunctional procollagen lysine hydroxylase and glycosyltransferase Caenorhabditis elegans PR
Q3ED68 ICU11 2-oxoglutarate and iron-dependent oxygenase domain-containing protein ICU11 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MVPPAVLLPW VVLPLLGVQG GSGSKQEENL LVLTVATKQT EGFRRFRRSA QFFNYKIQVL
70 80 90 100 110 120
GLDEEWKGGD DKKPAGGGQK VRLLKSALKQ HADKEDLVIL FIESYDVLFA SGPTELLKKF
130 140 150 160 170 180
KQAKSKVVFS AENYIYPDRK LEAKYPPVRD GKRFLGSGGF IGYAPNLKKL VEEWKGKDDD
190 200 210 220 230 240
SDQLFYTKIF LDPEKRENIN ISLDHRSRIF QNLNGALDEV VLKFENARVR ARNLLYDTLP
250 260 270 280 290 300
VIIHGNGPTK LQLNYLGNYI PQIWTFETGC TVCDEGLRSL TGIKDEALPM ILIGIFIEQP
310 320 330 340 350 360
TPFLSQFFLR LRNLHYPKQR IQIFIHNHEE HHSMQVDSFV KEHSKEYLAM KVIGPDDEVE
370 380 390 400 410 420
NAEARNLGMD LCRKDPDCDY YFSLDAEVVL KNTETLRILI EQNKSVIAPL VSRHEKLWSN
430 440 450 460 470 480
FWGALSPDGY YARSEDYVDI VQRRRVGLWN VPYISSVYMV KGKVLRSELD EGDLFHGGKL
490 500 510 520 530 540
DADMAFCHNV RNQGVFMYLT NRHQFGHILS LENYQTTHLH NDLWQIFSNP EDWREKYIHE
550 560 570 580 590 600
NYTAALKGKL VEMPCPDVYW FPIFTDTACD ELVEEMEHYG KWSTGDNTDS RIQGGYENVP
610 620 630 640 650 660
TIDIHMNQIG FEREWYKFLL DYIAPITEKL YPGYYTKTQF ELAFVVRYKP DEQPSLMPHH
670 680 690 700 710 720
DASTFTINIA LNRVGIDYEG GGCRFLRYNC SIRAPRKGWT LMHPGRLTHY HEGLPTTKGT
RYIAVSFIDP