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P04785 (PDIA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase

Short name=PDI
EC=5.3.4.1
Alternative name(s):
Cellular thyroid hormone-binding protein
Prolyl 4-hydroxylase subunit beta
Gene names
Name:P4hb
Synonyms:Pdia1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP By similarity.

Catalytic activity

Catalyzes the rearrangement of -S-S- bonds in proteins.

Subunit structure

Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1 By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity. Melanosome By similarity. Cell membrane; Peripheral membrane protein Potential. Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces By similarity.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Caution

Was originally (Ref.3 and Ref.4) thought to be identical to thyroxine deiodinase but this was later shown (Ref.8) to be incorrect.

Ontologies

Keywords
   Cellular componentCell membrane
Endoplasmic reticulum
Membrane
   DomainRedox-active center
Repeat
Signal
   Molecular functionChaperone
Isomerase
   PTMAcetylation
Disulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

peptidyl-proline hydroxylation to 4-hydroxy-L-proline

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from mutant phenotype Ref.5. Source: GOC

regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to endoplasmic reticulum stress

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentendoplasmic reticulum

Inferred from Biological aspect of Ancestor. Source: RefGenome

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

procollagen-proline 4-dioxygenase complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprocollagen-proline 4-dioxygenase activity

Inferred from electronic annotation. Source: Ensembl

protein disulfide isomerase activity

Inferred from mutant phenotype Ref.5. Source: RGD

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

protein heterodimerization activity

Inferred from physical interaction PubMed 11830580. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.3
Chain20 – 509490Protein disulfide-isomerase
PRO_0000034199

Regions

Domain20 – 136117Thioredoxin 1
Domain335 – 477143Thioredoxin 2
Motif506 – 5094Prevents secretion from ER

Sites

Active site551Nucleophile By similarity
Active site581Nucleophile By similarity
Active site3991Nucleophile By similarity
Active site4021Nucleophile By similarity
Site561Contributes to redox potential value By similarity
Site571Contributes to redox potential value By similarity
Site1221Lowers pKa of C-terminal Cys of first active site By similarity
Site4001Contributes to redox potential value By similarity
Site4011Contributes to redox potential value By similarity
Site4631Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue2021N6-acetyllysine By similarity
Modified residue2241N6-succinyllysine By similarity
Modified residue2731N6-succinyllysine By similarity
Disulfide bond55 ↔ 58Redox-active By similarity
Disulfide bond399 ↔ 402Redox-active By similarity

Experimental info

Sequence conflict39 – 402AL → P in CAA26675. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P04785 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 3056107F5E8B1B54

FASTA50956,951
        10         20         30         40         50         60 
MLSRALLCLA LAWAARVGAD ALEEEDNVLV LKKSNFAEAL AAHNYLLVEF YAPWCGHCKA 

        70         80         90        100        110        120 
LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG YPTIKFFKNG DTASPKEYTA 

       130        140        150        160        170        180 
GREADDIVNW LKKRTGPAAT TLSDTAAAES LVDSSEVTVI GFFKDAGSDS AKQFLLAAEA 

       190        200        210        220        230        240 
VDDIPFGITS NSDVFSKYQL DKDGVVLFKK FDEGRNNFEG EITKEKLLDF IKHNQLPLVI 

       250        260        270        280        290        300 
EFTEQTAPKI FGGEIKTHIL LFLPKSVSDY DGKLSNFKKA AEGFKGKILF IFIDSDHTDN 

       310        320        330        340        350        360 
QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITQFCHHFLE GKIKPHLMSQ 

       370        380        390        400        410        420 
ELPEDWDKQP VKVLVGKNFE EVAFDEKKNV FVEFYAPWCG HCKQLAPIWD KLGETYKDHE 

       430        440        450        460        470        480 
NIVIAKMDST ANEVEAVKVH SFPTLKFFPA SADRTVIDYN GERTLDGFKK FLESGGQDGA 

       490        500 
GDNDDLDLEE ALEPDMEEDD DQKAVKDEL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin."
Edman J.C., Ellis L., Blacher R.W., Roth R.A., Rutter W.J.
Nature 317:267-270(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[3]"Identification of protein disulfide isomerase and calreticulin as autoimmune antigens in LEC strain of rats."
Yokoi T., Nagayama S., Kajiwara R., Kawaguchi Y., Horiuchi R., Kamataki T.
Biochim. Biophys. Acta 1158:339-344(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-34.
Strain: LEC.
Tissue: Liver.
[4]"Nucleotide sequence of rat liver iodothyronine 5'-monodeiodinase (5' MD): its identity with the protein disulfide isomerase."
Boado R.J., Campbell D.A., Chopra I.J.
Biochem. Biophys. Res. Commun. 155:1297-1304(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-509.
Tissue: Liver.
[5]"Enzyme binding-inhibiting assay for iodothyronine 5'-monodeiodinase (5'-MD) and its application to isolation of complementary deoxyribonucleic acid clones for the 5'-MD in rat liver."
Boado R.J., Chopra I.J., Flink I.L., Campbell D.A.
Endocrinology 123:1264-1273(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 129-394.
Tissue: Liver.
[6]Lubec G., Afjehi-Sadat L., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 233-249; 288-302 AND 341-352, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
[7]"Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites."
Noiva R., Freedman R.B., Lennarz W.J.
J. Biol. Chem. 268:19210-19217(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 471-494.
[8]"Rat liver type I iodothyronine deiodinase is not identical to protein disulfide isomerase."
Schoenmakers C.H.H., Pigmans I.G.A.J., Hawkins H.C., Freedman R.B., Visser T.J.
Biochem. Biophys. Res. Commun. 162:857-868(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT PROTEIN IS NOT IDENTICAL TO THYROXINE DEIODINASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21018 mRNA. Translation: AAA40620.1.
BC061857 mRNA. Translation: AAH61857.1.
X02918 mRNA. Translation: CAA26675.1.
M21476 mRNA. Translation: AAA40619.1.
PIRISRTSS. A24595.
S68028.
RefSeqNP_037130.1. NM_012998.1.
UniGeneRn.4234.

3D structure databases

ProteinModelPortalP04785.
SMRP04785. Positions 20-359, 370-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247538. 1 interaction.
IntActP04785. 1 interaction.
MINTMINT-4996344.
STRING10116.ENSRNOP00000051841.

PTM databases

PhosphoSiteP04785.

Proteomic databases

PaxDbP04785.
PRIDEP04785.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000054958; ENSRNOP00000051841; ENSRNOG00000036689.
GeneID25506.
KEGGrno:25506.

Organism-specific databases

CTD5034.
RGD3244. P4hb.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00740000115202.
HOGENOMHOG000162459.
HOVERGENHBG005920.
InParanoidP04785.
KOK09580.
OMACHHFLEG.
OrthoDBEOG7VHSX1.
PhylomeDBP04785.
TreeFamTF106381.

Gene expression databases

GenevestigatorP04785.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio606925.
PROP04785.

Entry information

Entry namePDIA1_RAT
AccessionPrimary (citable) accession number: P04785
Secondary accession number(s): P13700
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families