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Protein

Protein disulfide-isomerase

Gene

PDI

Organism
Medicago sativa (Alfalfa)
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 sitei62NucleophileBy similarity1
Sitei63Contributes to redox potential valueBy similarity1
Sitei64Contributes to redox potential valueBy similarity1
Active sitei65NucleophileBy similarity1
Sitei130Lowers pKa of C-terminal Cys of first active siteBy similarity1
Active sitei407NucleophileBy similarity1
Sitei408Contributes to redox potential valueBy similarity1
Sitei409Contributes to redox potential valueBy similarity1
Active sitei410NucleophileBy similarity1
Sitei471Lowers 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
OrganismiMedicago sativa (Alfalfa)
Taxonomic identifieri3879 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

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 – 24By similarityAdd BLAST24
ChainiPRO_000003420925 – 512Protein disulfide-isomeraseAdd BLAST488

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi62 ↔ 65Redox-activePROSITE-ProRule annotation
Glycosylationi278N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi407 ↔ 410Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP29828.

Structurei

3D structure databases

ProteinModelPortaliP29828.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 144Thioredoxin 1PROSITE-ProRule annotationAdd BLAST120
Domaini357 – 485Thioredoxin 2PROSITE-ProRule annotationAdd BLAST129

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi509 – 512Prevents secretion from ER4

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.

P29828-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKNVAIFGL LFSLLLLVPS QIFAEESSTD AKEFVLTLDN TNFHDTVKKH
60 70 80 90 100
DFIVVEFYAP WCGHCKKLAP EYEKAASILS THEPPVVLAK VDANEEHNKD
110 120 130 140 150
LASENDVKGF PTIKIFRNGG KNIQEYKGPR EAEGIVEYLK KQSGPASTEI
160 170 180 190 200
KSADDATAFV GDNKVVIVGV FPKFSGEEYD NFIALAEKLR SDYDFAHTLN
210 220 230 240 250
AKHLPKGDSS VSGPVVRLFK PFDELFVDSK DFNVEALEKF IEESSTPIVT
260 270 280 290 300
VFNNEPSNHP FVVKFFNSPN AKAMLFINFT TEGAESFKTK YHEVAEQYKQ
310 320 330 340 350
QGVSFLVGDV ESSQGAFQYF GLKEEQVPLI IIQHNDGKKF FKPNLELDQL
360 370 380 390 400
PTWLKAYKDG KVEPFVKSEP IPETNNEPVK VVVGQTLEDV VFKSGKNVLI
410 420 430 440 450
EFYAPWCGHC KQLAPILDEV AVSFQSDADV VIAKLDATAN DIPTDTFDVQ
460 470 480 490 500
GYPTLYFRSA SGKLSQYDGG RTKEDIIEFI EKNKDKTGAA HQEVEQPKAA
510
AQPEAEQPKD EL
Length:512
Mass (Da):57,087
Last modified:April 1, 1993 - v1
Checksum:iE5EC7341A3FF7935
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16L → V in AAA32662 (PubMed:1720555).Curated1
Sequence conflicti395G → A in AAA32662 (PubMed:1720555).Curated1
Sequence conflicti491H → Q in AAA32662 (PubMed:1720555).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11499 mRNA. Translation: CAA77575.1.
M82973 mRNA. Translation: AAA32662.1.
PIRiA41440.
S22479. ISAASS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11499 mRNA. Translation: CAA77575.1.
M82973 mRNA. Translation: AAA32662.1.
PIRiA41440.
S22479. ISAASS.

3D structure databases

ProteinModelPortaliP29828.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP29828.

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_MEDSA
AccessioniPrimary (citable) accession number: P29828
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 5, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.