Q17770

PR
Gene name
pdi-2 (C07A12.4)
Protein name
Protein disulfide-isomerase 2
Names
PDI 1, Prolyl 4-hydroxylase subunit beta-2
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_C07A12.4
EC number
5.3.4.1: Transposing S-S bonds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

317-387 (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 Q17770

Entry ID Method Resolution Chain Position Source
AF-Q17770-F1 Predicted AlphaFoldDB

No variants for Q17770

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q17770

No associated diseases with Q17770

6 regional properties for Q17770

Type Name Position InterPro Accession
domain Protein disulfide-isomerase, thioredoxin-like domain 28 - 128 IPR005788-1
domain Protein disulfide-isomerase, thioredoxin-like domain 368 - 467 IPR005788-2
domain Thioredoxin domain 10 - 130 IPR013766-1
domain Thioredoxin domain 342 - 470 IPR013766-2
conserved_site Thioredoxin, conserved site 44 - 62 IPR017937-1
conserved_site Thioredoxin, conserved site 385 - 403 IPR017937-2

Functions

Description
EC Number 5.3.4.1 Transposing S-S bonds
Subcellular Localization
  • Endoplasmic reticulum lumen
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.
procollagen-proline 4-dioxygenase complex A protein complex that catalyzes the formation of procollagen trans-4-hydroxy-L-proline and succinate from procollagen L-proline and 2-oxoglutarate, requiring Fe2+ and ascorbate. Contains two alpha subunits that contribute to most parts of the catalytic sites, and two beta subunits that are identical to protein-disulfide isomerase.

2 GO annotations of molecular function

Name Definition
protein disulfide isomerase activity Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
protein-glutamine gamma-glutamyltransferase activity Catalysis of the reaction: protein glutamine + alkylamine = protein N5-alkylglutamine + NH3. This reaction is the formation of the N6-(L-isoglutamyl)-L-lysine isopeptide, resulting in cross-linking polypeptide chains; the gamma-carboxamide groups of peptidyl-glutamine residues act as acyl donors, and the 6-amino-groups of peptidyl-lysine residues act as acceptors, to give intra- and intermolecular N6-(5-glutamyl)lysine cross-links.

6 GO annotations of biological process

Name Definition
endoplasmic reticulum unfolded protein response The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
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.
protein deglutathionylation The protein modification process in which a glutathione molecule is removed from a protein amino acid by breaking a disulfide linkage.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
response to endoplasmic reticulum stress Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q29RV1 PDIA4 Protein disulfide-isomerase A4 Bos taurus (Bovine) PR
Q8N807 PDILT Protein disulfide-isomerase-like protein of the testis Homo sapiens (Human) PR
Q13087 PDIA2 Protein disulfide-isomerase A2 Homo sapiens (Human) PR
Q5WA72 PDIL1-5 Protein disulfide isomerase-like 1-5 Oryza sativa subsp japonica (Rice) PR
A3KPF5 PDIL1-5 Protein disulfide isomerase-like 1-5 Arabidopsis thaliana (Mouse-ear cress) PR
Q66GQ3 PDIL1-6 Protein disulfide isomerase-like 1-6 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MFRLVGLFFL VLGASAAVIE EEENVIVLTK DNFDEVINGN EFILVEFYAP WCGHCKSLAP
70 80 90 100 110 120
EYAKAATQLK EEGSDIKLGK LDATVHGEVS SKFEVRGYPT LKLFRNGKPQ EYNGGRDHDS
130 140 150 160 170 180
IIAWLKKKTG PVAKPLADAD AVKELQESAD VVVIGYFKDT TSDDAKTFLE VAAGIDDVPF
190 200 210 220 230 240
GISTEDAVKS EIELKGEGIV LFKKFDDGRV AFDEKLTQDG LKTWIQANRL ALVSEFTQET
250 260 270 280 290 300
ASVIFGGEIK SHNLLFVSKE SSEFAKLEQE FKNAAKQFKG KVLFVYINTD VEENARIMEF
310 320 330 340 350 360
FGLKKDELPA IRLISLEEDM TKFKPDFEEI TTENISKFTQ NYLDGSVKPH LMSEDIPEDW
370 380 390 400 410 420
DKNPVKILVG KNFEQVARDN TKNVLVEFYA PWCGHCKQLA PTWDKLGEKF ADDESIVIAK
430 440 450 460 470 480
MDSTLNEVED VKIQSFPTIK FFPAGSNKVV DYTGDRTIEG FTKFLETNGK EGAGASEEEK
490
AEEEADEEGH TEL