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Protein

Protein disulfide-isomerase

Gene
N/A
Organism
Ricinus communis (Castor bean)
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 sitei61NucleophileBy similarity1
Sitei62Contributes to redox potential valueBy similarity1
Sitei63Contributes to redox potential valueBy similarity1
Active sitei64NucleophileBy similarity1
Sitei129Lowers pKa of C-terminal Cys of first active siteBy similarity1
Active sitei406NucleophileBy similarity1
Sitei407Contributes to redox potential valueBy similarity1
Sitei408Contributes to redox potential valueBy similarity1
Active sitei409NucleophileBy similarity1
Sitei470Lowers 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
OrganismiRicinus communis (Castor bean)
Taxonomic identifieri3988 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000003421124 – 498Protein disulfide-isomeraseAdd BLAST475

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi41N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi61 ↔ 64Redox-activePROSITE-ProRule annotation
Disulfide bondi406 ↔ 409Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ43116.

Structurei

3D structure databases

ProteinModelPortaliQ43116.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 143Thioredoxin 1PROSITE-ProRule annotationAdd BLAST120
Domaini339 – 484Thioredoxin 2PROSITE-ProRule annotationAdd BLAST146

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi495 – 498Prevents 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

KOiK09580.

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.

Q43116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFRGSIWY CIFVLSLIAV AISAAESEEE QSSVLTLDST NFTDTISKHD
60 70 80 90 100
FIVVEFYAPW CGHCKKLRPE YEKAASILKS HDIPVVLAKV DANEEANKEL
110 120 130 140 150
ATQYDIKGFP TLKILRNGGK SIQEYKGPRE ADGIAEYLKK QSGPASVEIK
160 170 180 190 200
STEAANTFIG DKKIFIVGVF PKFSGEEYEN YMSVADKLRS DYEFGHTLDA
210 220 230 240 250
KHLPQGESSV TGPVVRLFKP FDELFVDFKD FNVDALEKFV EESSMPVVTV
260 270 280 290 300
FNSDPSNHPF VIKFFNSPDA KAMLFMNFNG EAADSIKSKY QEVAHQFKGE
310 320 330 340 350
GIILLLGDVE ASQGAFQYFG LKEDQVPLII IQTNDGQKYL KANLEPDHIA
360 370 380 390 400
PWVKAYKEGK VQAYRKSEPI PEVNNEPVKV VVADTLQDIV FNSGKNVLLE
410 420 430 440 450
FYAPWCGHCK QLAPILDEVA VSYKSDADIV IAKLDATAND IPSDTFDVRG
460 470 480 490
YPTVYFRSAS GKVEQYDGDR TKDDIISFIE KNRDKAAQQE SANGKDEL
Length:498
Mass (Da):55,561
Last modified:November 1, 1996 - v1
Checksum:iD556492D78F955D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41385 mRNA. Translation: AAB05641.1.
PIRiS62626.
RefSeqiNP_001310686.1. NM_001323757.1.

Genome annotation databases

GeneIDi8281065.
KEGGircu:8281065.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41385 mRNA. Translation: AAB05641.1.
PIRiS62626.
RefSeqiNP_001310686.1. NM_001323757.1.

3D structure databases

ProteinModelPortaliQ43116.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ43116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8281065.
KEGGircu:8281065.

Phylogenomic databases

KOiK09580.

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_RICCO
AccessioniPrimary (citable) accession number: Q43116
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 100 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.