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 Q63081

Entry ID Method Resolution Chain Position Source
AF-Q63081-F1 Predicted AlphaFoldDB

No variants for Q63081

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q63081

No associated diseases with Q63081

6 regional properties for Q63081

Type Name Position InterPro Accession
domain Protein disulfide-isomerase, thioredoxin-like domain 30 - 125 IPR005788-1
domain Protein disulfide-isomerase, thioredoxin-like domain 165 - 263 IPR005788-2
domain Thioredoxin domain 19 - 133 IPR013766-1
domain Thioredoxin domain 151 - 287 IPR013766-2
conserved_site Thioredoxin, conserved site 47 - 65 IPR017937-1
conserved_site Thioredoxin, conserved site 182 - 200 IPR017937-2

Functions

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

7 GO annotations of cellular component

Name Definition
endoplasmic reticulum chaperone complex A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
endoplasmic reticulum lumen The volume enclosed by the membranes of the endoplasmic reticulum.
endoplasmic reticulum-Golgi intermediate compartment A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
melanosome A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
smooth endoplasmic reticulum The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.

3 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
protein disulfide isomerase activity Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
protein-disulfide reductase activity Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.

5 GO annotations of biological process

Name Definition
negative regulation of IRE1-mediated unfolded protein response Any process that stops, prevents or reduces the frequency, rate or extent of the IRE1-mediated unfolded protein response.
platelet activation A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug.
platelet aggregation The adhesion of one platelet to one or more other platelets via adhesion molecules.
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.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q12404 MPD1 Protein disulfide-isomerase MPD1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q2KIL5 PDIA5 Protein disulfide-isomerase A5 Bos taurus (Bovine) PR
Q8N807 PDILT Protein disulfide-isomerase-like protein of the testis Homo sapiens (Human) PR
Q15084 PDIA6 Protein disulfide-isomerase A6 Homo sapiens (Human) PR
Q921X9 Pdia5 Protein disulfide-isomerase A5 Mus musculus (Mouse) PR
Q922R8 Pdia6 Protein disulfide-isomerase A6 Mus musculus (Mouse) PR
Q5I0H9 Pdia5 Protein disulfide-isomerase A5 Rattus norvegicus (Rat) PR
Q10N04 PDIL5-1 Protein disulfide isomerase-like 5-1 Oryza sativa subsp japonica (Rice) PR
Q67UF5 PDIL2-3 Protein disulfide isomerase-like 2-3 Oryza sativa subsp japonica (Rice) PR
Q8GYD1 PDIL5-1 Protein disulfide-isomerase 5-1 Arabidopsis thaliana (Mouse-ear cress) 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
MARLVLGLVS CTFFLAVSAL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF YAPWCGHCQR
70 80 90 100 110 120
LTPEWKKAAS ALKDVVKVGA VNADKHQSLG GQYGVQGFPT IKIFGANKNK PEDYQGGRTG
130 140 150 160 170 180
EAIVDAALSA LRQLVKDRLG GRSGGYSSGK QGRGDSSSKK DVVELTDDTF DKNVLDSEDV
190 200 210 220 230 240
WMVEFYAPWC GHCKNLEPEW AAAATEVKEQ TKGKVKLAAV DATVNQVLAS RYGIKGFPTI
250 260 270 280 290 300
KIFQKGESPV DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKKT CEEHQLCVVA
310 320 330 340 350 360
VLPHILDTGA TGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQYELENALG IGGFGYPAMA
370 380 390 400 410 420
AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG GSFPNITPRE PWDGKDGELP
430
VEDDIDLSDV ELDDLEKDEL