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

2 structures for Q12404

Entry ID Method Resolution Chain Position Source
3ED3 X-ray 200 A A/B 23-310 PDB
AF-Q12404-F1 Predicted AlphaFoldDB

10 variants for Q12404

Variant ID(s) Position Change Description Diseaes Association Provenance
s15-853001 26 D>N No SGRP
s15-852721 119 K>M No SGRP
s15-852711 122 D>E No SGRP
s15-852655 141 T>N No SGRP
s15-852620 153 I>V No SGRP
s15-852424 218 M>T No SGRP
s15-852422 219 N>H No SGRP
s15-852170 303 P>S No SGRP
s15-852167 304 I>F No SGRP
s15-852157 307 N>I No SGRP

No associated diseases with Q12404

2 regional properties for Q12404

Type Name Position InterPro Accession
domain Thioredoxin domain 13 - 158 IPR013766
conserved_site Thioredoxin, conserved site 51 - 69 IPR017937

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.
fungal-type vacuole A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure.

3 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-disulfide reductase (glutathione) activity Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
protein-disulfide reductase activity Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.

2 GO annotations of biological process

Name Definition
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
Q15084 PDIA6 Protein disulfide-isomerase A6 Homo sapiens (Human) PR
Q922R8 Pdia6 Protein disulfide-isomerase A6 Mus musculus (Mouse) PR
Q63081 Pdia6 Protein disulfide-isomerase A6 Rattus norvegicus (Rat) PR
Q67UF5 PDIL2-3 Protein disulfide isomerase-like 2-3 Oryza sativa subsp japonica (Rice) PR
O48773 PDIL2-3 Protein disulfide-isomerase 2-3 Arabidopsis thaliana (Mouse-ear cress) PR
Q9MAU6 PDIL2-2 Protein disulfide-isomerase like 2-2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MLFLNIIKLL LGLFIMNEVK AQNFYDSDPH ISELTPKSFD KAIHNTNYTS LVEFYAPWCG
70 80 90 100 110 120
HCKKLSSTFR KAAKRLDGVV QVAAVNCDLN KNKALCAKYD VNGFPTLMVF RPPKIDLSKP
130 140 150 160 170 180
IDNAKKSFSA HANEVYSGAR TLAPIVDFSL SRIRSYVKKF VRIDTLGSLL RKSPKLSVVL
190 200 210 220 230 240
FSKQDKISPV YKSIALDWLG KFDFYSISNK KLKQLTDMNP TYEKTPEIFK YLQKVIPEQR
250 260 270 280 290 300
QSDKSKLVVF DADKDKFWEY EGNSINKNDI SKFLRDTFSI TPNEGPFSRR SEYIAYLKTG
310
KKPIKKNHSS SGNKHDEL