SubmitCancel

Skip Header

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

Q12730

- PDI_ASPNG

UniProt

Q12730 - PDI_ASPNG

(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
pdiA, pdi1
Organism
Aspergillus niger
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 sitei54 – 541Nucleophile By similarity
Sitei55 – 551Contributes to redox potential value By similarity
Sitei56 – 561Contributes to redox potential value By similarity
Active sitei57 – 571Nucleophile By similarity
Sitei117 – 1171Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei389 – 3891Nucleophile By similarity
Sitei390 – 3901Contributes to redox potential value By similarity
Sitei391 – 3911Contributes to redox potential value By similarity
Active sitei392 – 3921Nucleophile By similarity
Sitei456 – 4561Lowers pKa of C-terminal Cys of second active site By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. 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
Gene namesi
Name:pdiA
Synonyms:pdi1
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed prediction
Add
BLAST
Chaini21 – 515495Protein disulfide-isomerase
PRO_0000034213Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 57Redox-active By similarity
Disulfide bondi389 ↔ 392Redox-active By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliQ12730.
SMRiQ12730. Positions 231-471.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 132112Thioredoxin 1
Add
BLAST
Domaini339 – 470132Thioredoxin 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi512 – 5154Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Contains 2 thioredoxin domains.

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR001393. Calsequestrin.
IPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
PRINTSiPR00312. CALSEQUESTRN.
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 1 hit.
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.

Q12730-1 [UniParc]FASTAAdd to Basket

« Hide

MRSFAPWLVS LLGASAVVAA ADTESDVISL DQDTFESFMN EHGLVLAEFF    50
APWCGHCKAL APKYEEAATE LKAKNIPLVK VDCTAEEDLC RSQGVEGYPT 100
LKIFRGVDSS KPYQGARQTE SIVSYMIKQS LPAVSSVNEE NLEEIKTMDK 150
IVVIGYIPSD DQETYQAFEK YAESQRDNYL FAATDDAAIA KSEGVEQPSI 200
VLYKDFDEKK AVYDGEIEQE AIHSWVKSAS TPLVGEIGPE TYSGYIGAGV 250
PLAYIFAETK EEREKYTEDF KPIAQKHKGA INIATIDAKM FGAHAGNLNL 300
DSQKFPAFAI QDPAKNAKYP YDQAKELNAD EVEKFIQDVL DGKVEPSIKS 350
EPVPESQEGP VTVVVAHSYK DLVIDNDKDV LLEFYAPWCG HCKALAPKYD 400
ELAALYADHP DLAAKVTIAK IDATANDVPD PITGFPTLRL YPAGAKDSPI 450
EYSGSRTVED LANFVKENGK HNVDALNVAS EETQEGGDVT EAAPSATEAE 500
TPAATDDEKA EHDEL 515
Length:515
Mass (Da):56,292
Last modified:November 1, 1997 - v1
Checksum:i2B0058B788400AD9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98797 Genomic DNA. Translation: CAA67332.1.
X89449 mRNA. Translation: CAA61619.1.
PIRiS57942.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98797 Genomic DNA. Translation: CAA67332.1 .
X89449 mRNA. Translation: CAA61619.1 .
PIRi S57942.

3D structure databases

ProteinModelPortali Q12730.
SMRi Q12730. Positions 231-471.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0526.

Family and domain databases

Gene3Di 3.40.30.10. 3 hits.
InterProi IPR001393. Calsequestrin.
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 ]
PRINTSi PR00312. CALSEQUESTRN.
SUPFAMi SSF52833. SSF52833. 4 hits.
TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and characterisation of a gene encoding protein disulphide isomerase, pdiA, from Aspergillus niger."
    Ngiam C., Jeenes D.J., Archer D.B.
    Curr. Genet. 31:133-138(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
  2. Malpricht S.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Entry informationi

Entry nameiPDI_ASPNG
AccessioniPrimary (citable) accession number: Q12730
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi