Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein disulfide-isomerase

Gene

PDI

Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.By similarity

Catalytic activityi

Catalyzes the rearrangement of -S-S- bonds in proteins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei67NucleophileBy similarity1
Sitei68Contributes to redox potential valueBy similarity1
Sitei69Contributes to redox potential valueBy similarity1
Active sitei70NucleophileBy similarity1
Sitei135Lowers pKa of C-terminal Cys of first active siteBy similarity1
Active sitei411NucleophileBy similarity1
Sitei412Contributes to redox potential valueBy similarity1
Sitei413Contributes to redox potential valueBy similarity1
Active sitei414NucleophileBy similarity1
Sitei474Lowers pKa of C-terminal Cys of second active siteBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase (EC:5.3.4.1)
Short name:
PDI
Alternative name(s):
Endosperm protein E-1
Gene namesi
Name:PDI
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
ChainiPRO_000003420826 – 513Protein disulfide-isomeraseAdd BLAST488

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi67 ↔ 70Redox-activePROSITE-ProRule annotation
Glycosylationi282N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi411 ↔ 414Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

IntActiP80284. 1 interactor.
STRINGi4513.MLOC_351.5.

Structurei

3D structure databases

ProteinModelPortaliP80284.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 149Thioredoxin 1PROSITE-ProRule annotationAdd BLAST124
Domaini369 – 488Thioredoxin 2PROSITE-ProRule annotationAdd BLAST120

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi510 – 513Prevents secretion from ERPROSITE-ProRule annotation4

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0190. Eukaryota.
COG0526. LUCA.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80284-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISKVWISL LLALAVVLSA PAARAEEAAA AEEAAAPEAV LTLHADNFDD
60 70 80 90 100
AIGQHPFILV EFYAPWCGHC KSLAPEYEKA AQLLSKHDPA IVLAKVDAND
110 120 130 140 150
EKNKPLAGKY EVQGFPTLKI FRNGGKSIQE YKGPREAEGI VEYLKKQVGP
160 170 180 190 200
ASKEIKAPED ATYLEDGKIH IVGVFTEFSG PEFTNFLEVA EKLRSYYDFG
210 220 230 240 250
HTVHANHLPR GDAAVERPVV RLFKPFDELV VDSKDFDVSA LEKFIDASST
260 270 280 290 300
PKVVIFDKNP DNHPYLLKFF QSNAPKAMLF LNFSTGPFES FKSAYYGAVE
310 320 330 340 350
EFSGKDVKFL IGDIESSQGA FQYFGLKVDQ APLILIQDGD SKKFLKEHVE
360 370 380 390 400
AGQIVAWLKD YFDGKLTPFR KSEPIPEANN EPVKVVVADN VHDVVFKSGK
410 420 430 440 450
NVLIEFYAPW CGHCKKLAPI LDEAAATLQS EEDVVIAKMD ATENDVPGEF
460 470 480 490 500
DVQGYPTLYF VTPSGKKVSY EGGRTADEIV DYIRKNKETA GQAAAATEKA
510
AEPAATEPLK DEL
Length:513
Mass (Da):56,463
Last modified:October 1, 1996 - v2
Checksum:i03BBAE2EE164F972
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33250 mRNA. Translation: AAA70344.1.
L33251 mRNA. Translation: AAA70345.1.
L33252 mRNA. Translation: AAA70346.1.
PIRiT05974.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33250 mRNA. Translation: AAA70344.1.
L33251 mRNA. Translation: AAA70345.1.
L33252 mRNA. Translation: AAA70346.1.
PIRiT05974.

3D structure databases

ProteinModelPortaliP80284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP80284. 1 interactor.
STRINGi4513.MLOC_351.5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0190. Eukaryota.
COG0526. LUCA.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDI_HORVU
AccessioniPrimary (citable) accession number: P80284
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1996
Last modified: February 17, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.