Q20679

PR
Gene name
let-268 (F52H3.1)
Protein name
Multifunctional procollagen lysine hydroxylase and glycosyltransferase
Names
Lethal protein 268
Species
Caenorhabditis elegans
KEGG Pathway
EC number
1.14.11.4: 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)

147-223 (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 Q20679

Entry ID Method Resolution Chain Position Source
AF-Q20679-F1 Predicted AlphaFoldDB

No variants for Q20679

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q20679

No associated diseases with Q20679

3 regional properties for Q20679

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 555 - 729 IPR006620

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
  • Endoplasmic reticulum lumen
  • Endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side
  • Secreted
  • Secreted, extracellular space
  • The majority of the secreted protein is associated with the extracellular matrix
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.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
rough endoplasmic reticulum The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae.

6 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 galactosyltransferase activity Catalysis of the reaction: UDP-galactose + procollagen 5-hydroxy-L-lysine = UDP + procollagen 5-(D-galactosyloxy)-L-lysine.
procollagen glucosyltransferase activity Catalysis of the reaction: UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
procollagen-lysine 5-dioxygenase activity Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
UDP-glucose:glycoprotein glucosyltransferase activity Catalysis of the addition of UDP-glucose on to asparagine-linked (N-linked) oligosaccharides of the form Man7-9GlcNAc2 on incorrectly folded glycoproteins.

3 GO annotations of biological process

Name Definition
collagen biosynthetic process The chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
peptidyl-lysine hydroxylation The hydroxylation of peptidyl-lysine to form peptidyl-hydroxylysine.
protein glycosylation A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A7MB73 CERCAM Probable inactive glycosyltransferase 25 family member 3 Bos taurus (Bovine) PR
P24802 PLOD1 Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 Gallus gallus (Chicken) PR
Q8IPK4 CG31915 Glycosyltransferase 25 family member Drosophila melanogaster (Fruit fly) PR
O60568 PLOD3 Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 Homo sapiens (Human) PR
Q5T4B2 CERCAM Inactive glycosyltransferase 25 family member 3 Homo sapiens (Human) PR
A3KGW5 Cercam Inactive glycosyltransferase 25 family member 3 Mus musculus (Mouse) 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
MRVLPFLLPL IPVLLATTIT DLPELVVVTV ATENTDGLKR LLESAKAFDI NIEVLGLGEK
70 80 90 100 110 120
WNGGDTRIEQ GGGQKIRILS DWIEKYKDAS DTMIMFVDAY DVVFNADSTT ILRKFFEHYS
130 140 150 160 170 180
EKRLLFGAEP FCWPDQSLAP EYPIVEFGKR FLNSGLFMGY GPEMHKILKL KSVEDKDDDQ
190 200 210 220 230 240
LYYTMIYLDE KLRKELNMDL DSMSKIFQNL NGVIEDVELQ FKEDGTPEAY NAAYNTKPLI
250 260 270 280 290 300
VHGNGPSKSH LNYLGNYLGN RWNSQLGCRT CGLEVKESEE VPLIALNLFI SKPIPFIEEV
310 320 330 340 350 360
LQKIAEFDYP KEKIALYIYN NQPFSIKNIQ DFLQKHGKSY YTKRVINGVT EIGDREARNE
370 380 390 400 410 420
AIEWNKARNV EFAFLMDGDA YFSEPKVIKD LIQYSKTYDV GIIAPMIGQP GKLFTNFWGA
430 440 450 460 470 480
IAANGYYARS EDYMAIVKGN RVGYWNVPFI TSAVLFNKEK LEAMKDAYSY NKNLDPDMSM
490 500 510 520 530 540
CKFARDNGHF LYIDNEKYYG FLIVSDEYAE TVTEGKWHPE MWQIFENREL WEARYIHPGY
550 560 570 580 590 600
HKIMEPEHVV DQACPDVYDF PLMSERFCEE LIEEMEGFGR WSDGSNNDKR LAGGYENVPT
610 620 630 640 650 660
RDIHMNQVGF ERQWLYFMDT YVRPVQEKTF IGYYHQPVES NMMFVVRYKP EEQPSLRPHH
670 680 690 700 710 720
DASTFSIDIA LNKKGRDYEG GGVRYIRYNC TVPADEVGYA MMFPGRLTHL HEGLATTKGT
RYIMVSFINP