Skip Header

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

Q43116

- PDI_RICCO

UniProt

Q43116 - PDI_RICCO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein disulfide-isomerase

Gene
N/A
Organism
Ricinus communis (Castor bean)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei61 – 611NucleophileBy similarity
Sitei62 – 621Contributes to redox potential valueBy similarity
Sitei63 – 631Contributes to redox potential valueBy similarity
Active sitei64 – 641NucleophileBy similarity
Sitei129 – 1291Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei406 – 4061NucleophileBy similarity
Sitei407 – 4071Contributes to redox potential valueBy similarity
Sitei408 – 4081Contributes to redox potential valueBy similarity
Active sitei409 – 4091NucleophileBy similarity
Sitei470 – 4701Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
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

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

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 498475Protein disulfide-isomerasePRO_0000034211Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
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)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 143120Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini339 – 484146Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi495 – 4984Prevents secretion from ERPROSITE-ProRule annotation

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.

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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41385 mRNA. Translation: AAB05641.1 .
PIRi S62626.

3D structure databases

ProteinModelPortali Q43116.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q43116.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.30.10. 3 hits.
InterProi IPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 2 hits.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 4 hits.
TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular characterisation of plant endoplasmic reticulum. Identification of protein disulfide-isomerase as the major reticuloplasmin."
    Coughlan S.J., Hastings C., Winfrey R.J.
    Eur. J. Biochem. 235:215-224(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Hale.

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 26, 2014
This is version 98 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

External Data

Dasty 3