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 Q67UF5

Entry ID Method Resolution Chain Position Source
AF-Q67UF5-F1 Predicted AlphaFoldDB

No variants for Q67UF5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q67UF5

No associated diseases with Q67UF5

6 regional properties for Q67UF5

Type Name Position InterPro Accession
domain Protein disulfide-isomerase, thioredoxin-like domain 35 - 132 IPR005788-1
domain Protein disulfide-isomerase, thioredoxin-like domain 170 - 270 IPR005788-2
domain Thioredoxin domain 12 - 139 IPR013766-1
domain Thioredoxin domain 159 - 276 IPR013766-2
conserved_site Thioredoxin, conserved site 51 - 69 IPR017937-1
conserved_site Thioredoxin, conserved site 187 - 205 IPR017937-2

Functions

Description
EC Number 5.3.4.1 Transposing S-S bonds
Subcellular Localization
  • Endoplasmic reticulum lumen
  • Localizes on the surface of ER-derived type-I protein bodies in the endosperm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
endoplasmic reticulum lumen The volume enclosed by the membranes of the endoplasmic reticulum.

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-disulfide reductase activity Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.

1 GO annotations of biological process

Name Definition
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
Q63081 Pdia6 Protein disulfide-isomerase A6 Rattus norvegicus (Rat) PR
Q10N04 PDIL5-1 Protein disulfide isomerase-like 5-1 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
MRPAVAAALL LVAAAVAASP VSALYSAGSP VLQFNPNNFK SKVLNSNGVV LVEFFAPWCG
70 80 90 100 110 120
HCQQLTPIWE KAAGVLKGVA TVAALDADAH KELAQEYGIR GFPTIKVFVP GKPPVDYQGA
130 140 150 160 170 180
RDVKPIVEFA LSQVKALLRD RLNGKTSAGS GGKKSGGSSE KTEPSASIEL NSQNFDKLVT
190 200 210 220 230 240
KSKDLWIVEF FAPWCGHCKK LAPEWKKAAK NLKGQVKLGH VDCDAEKSLM SKYKVEGFPT
250 260 270 280 290 300
ILVFGADKES PFPYQGARVA SAIESFALEQ LEANAAPPEV SELTGPDAME EKCASAAICF
310 320 330 340 350 360
VSFLPDILDS KAEGRNKYLE LLLSVAEKFK KSPYSFVWTA AGKQADLEKQ VGVGGYGYPA
370 380 390 400 410 420
MVALNVKKGA YAPLRSAFQL DEITEFVKEA GRGGKGNLPL DGTPTIVQSE PWDGKDGEVI
430 440
EEDEFSLEEL MADNSPVNDE L