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Protein

Protein disulfide-isomerase

Gene

PDI

Organism
Triticum aestivum (Wheat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 sitei68NucleophileBy similarity1
Sitei69Contributes to redox potential valueBy similarity1
Sitei70Contributes to redox potential valueBy similarity1
Active sitei71NucleophileBy similarity1
Sitei136Lowers pKa of C-terminal Cys of first active siteBy similarity1
Active sitei412NucleophileBy similarity1
Sitei413Contributes to redox potential valueBy similarity1
Sitei414Contributes to redox potential valueBy similarity1
Active sitei415NucleophileBy similarity1
Sitei475Lowers 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
Gene namesi
Name:PDI
OrganismiTriticum aestivum (Wheat)
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeTriticinaeTriticum
Proteomesi
  • UP000019116 Componenti: Unassembled WGS sequence

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 – 25By similarityAdd BLAST25
ChainiPRO_000003421226 – 515Protein disulfide-isomeraseAdd BLAST490

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi68 ↔ 71Redox-activePROSITE-ProRule annotation
Glycosylationi283N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi412 ↔ 415Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP52589.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 150Thioredoxin 1PROSITE-ProRule annotationAdd BLAST125
Domaini346 – 489Thioredoxin 2PROSITE-ProRule annotationAdd BLAST144

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi512 – 515Prevents 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

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.

P52589-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISKVWISL LLALAVVLSA PAARAEEAAA AEEAAAAPEA VLTLHADNFD
60 70 80 90 100
DAIAKHPFIL VEFYAPWCGH CKSLAPEYEK AAQLLSKHDP AIVLAKVDAN
110 120 130 140 150
DEKNKPLAGK YEVQGFPTLK IFRSGGKNIQ EYKGPREAEG IVEYLKKQVG
160 170 180 190 200
PASKEIKAPE DATYLEDGKI HIVGVFTEFS GTEFTNFLEL AEKLRSDYDF
210 220 230 240 250
GHTVHANHLP RGDAAVERPL VRLFKPFDEL VVDSKDFDVS ALEKFIDASS
260 270 280 290 300
TPKVVTFDKN PDNHPYLLKY FQSNAPKAML FLNFSTGPFE SFKSAYYGAV
310 320 330 340 350
EEFSGKDVKF LIGDIEASQG AFQYNGLKED QAPLILIQDS DSKKFLKEQV
360 370 380 390 400
EAGQIVAWLK DYFDGKLTPF RKSEPIPEAN NEPVKVVVAD NIHDVVFKSA
410 420 430 440 450
KNVLIEFYAP WCGHCKKLAP ILDEAAATLQ SEEDVVIAKI DATANDVPGE
460 470 480 490 500
FDVQGYPTLY FVTPSGKKVS YEGGRTADEI VDYIKKNKET AGQAAAAATE
510
KAAEPAATEP LKDEL
Length:515
Mass (Da):56,533
Last modified:October 1, 1996 - v1
Checksum:i6630AB9A252A96B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11496 mRNA. Translation: AAA19660.1.
PIRiT06262.
UniGeneiTa.2019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11496 mRNA. Translation: AAA19660.1.
PIRiT06262.
UniGeneiTa.2019.

3D structure databases

ProteinModelPortaliP52589.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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_WHEAT
AccessioniPrimary (citable) accession number: P52589
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 17, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.