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 Q5I0H9

Entry ID Method Resolution Chain Position Source
AF-Q5I0H9-F1 Predicted AlphaFoldDB

1 variants for Q5I0H9

Variant ID(s) Position Change Description Diseaes Association Provenance
rs104955718 198 R>* No EVA

No associated diseases with Q5I0H9

9 regional properties for Q5I0H9

Type Name Position InterPro Accession
domain Thioredoxin domain 132 - 259 IPR013766-1
domain Thioredoxin domain 268 - 378 IPR013766-2
domain Thioredoxin domain 376 - 504 IPR013766-3
conserved_site Thioredoxin, conserved site 295 - 313 IPR017937-1
conserved_site Thioredoxin, conserved site 416 - 434 IPR017937-2
domain Protein disulfide-isomerase A5, N-terminal TRX-like b domain 26 - 137 IPR041865
domain Protein disulfide-isomerase A5, TRX (a) domain 150 - 254 IPR046374-1
domain Protein disulfide-isomerase A5, TRX (a) domain 275 - 377 IPR046374-2
domain Protein disulfide-isomerase A5, TRX (a) domain 396 - 499 IPR046374-3

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

2 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.

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
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.

11 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
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
Q922R8 Pdia6 Protein disulfide-isomerase A6 Mus musculus (Mouse) PR
Q921X9 Pdia5 Protein disulfide-isomerase A5 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
Q10N04 PDIL5-1 Protein disulfide isomerase-like 5-1 Oryza sativa subsp japonica (Rice) PR
Q9MAU6 PDIL2-2 Protein disulfide-isomerase like 2-2 Arabidopsis thaliana (Mouse-ear cress) PR
O48773 PDIL2-3 Protein disulfide-isomerase 2-3 Arabidopsis thaliana (Mouse-ear cress) PR
Q8GYD1 PDIL5-1 Protein disulfide-isomerase 5-1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MARAWGLLLA IGVILPTWLS STKVSSLIER ISDPKDLKKL LRTRNNVLVL YSESEVAAES
70 80 90 100 110 120
HLKLLSTVAQ AVKGQGTICW VDCGDAESRK LCKKMKVDLS PKDKKIELFH YQDGAFHMQY
130 140 150 160 170 180
DRAVTLKSIV AFLKDPKGPP LWEEDPGAKD VVHIDSEKDF RRLLKKEEKP LLMMFYAPWC
190 200 210 220 230 240
SMCKRIMPHF QKAATQVRGH TVLAGMNVYP PEFENIKEEY NVRGYPTICY FEKGRFLFQY
250 260 270 280 290 300
ENYGSTAEDI VEWLKNPQPP QPQVPETPWA DEGGSVYHLT DEDFDQFVKE HSSVLVMFHA
310 320 330 340 350 360
PWCGHCKKMK PEFESAAEVL HGDAESSGVL AAVDATINEA LAERFHISAF PTLKYFKNGE
370 380 390 400 410 420
QQAVPALRTK KKFIEWMQNP EAPPPPEPTW EEQQTSVLHL VGDNFRETLK KKKHTLVMFY
430 440 450 460 470 480
APWCPHCKKV IPHFTATADA FKDDRKIACA AVDCVKDKNQ DLCQQESVKA YPTFHYYHYG
490 500 510
KLVEKYESDR TELGFTSFIR TLREGDLKRL EKRREDL