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P04785

- PDIA1_RAT

UniProt

P04785 - PDIA1_RAT

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Protein
Protein disulfide-isomerase
Gene
P4hb, Pdia1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei55 – 551Nucleophile By similarity
Sitei56 – 561Contributes to redox potential value By similarity
Sitei57 – 571Contributes to redox potential value By similarity
Active sitei58 – 581Nucleophile By similarity
Sitei122 – 1221Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei399 – 3991Nucleophile By similarity
Sitei400 – 4001Contributes to redox potential value By similarity
Sitei401 – 4011Contributes to redox potential value By similarity
Active sitei402 – 4021Nucleophile By similarity
Sitei463 – 4631Lowers pKa of C-terminal Cys of second active site By similarity

GO - Molecular functioni

  1. enzyme binding Source: RGD
  2. procollagen-proline 4-dioxygenase activity Source: Ensembl
  3. protein disulfide isomerase activity Source: RGD
  4. protein heterodimerization activity Source: RGD
Complete GO annotation...

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to hypoxia Source: Ensembl
  3. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: Ensembl
  4. protein folding Source: GOC
  5. regulation of intrinsic apoptotic signaling pathway in response to oxidative stress Source: RefGenome
  6. response to endoplasmic reticulum stress Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Enzyme and pathway databases

ReactomeiREACT_198584. Collagen biosynthesis and modifying enzymes.
REACT_213899. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase (EC:5.3.4.1)
Short name:
PDI
Alternative name(s):
Cellular thyroid hormone-binding protein
Prolyl 4-hydroxylase subunit beta
Gene namesi
Name:P4hb
Synonyms:Pdia1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi3244. P4hb.

Subcellular locationi

Endoplasmic reticulum lumen By similarity. Melanosome By similarity. Cell membrane; Peripheral membrane protein Reviewed prediction
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.

GO - Cellular componenti

  1. endoplasmic reticulum Source: RefGenome
  2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  3. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  4. melanosome Source: UniProtKB-SubCell
  5. plasma membrane Source: UniProtKB-SubCell
  6. procollagen-proline 4-dioxygenase complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 Publication
Add
BLAST
Chaini20 – 509490Protein disulfide-isomerase
PRO_0000034199Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 58Redox-active By similarity
Modified residuei202 – 2021N6-acetyllysine By similarity
Modified residuei224 – 2241N6-succinyllysine By similarity
Modified residuei273 – 2731N6-succinyllysine By similarity
Disulfide bondi399 ↔ 402Redox-active By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP04785.
PRIDEiP04785.

PTM databases

PhosphoSiteiP04785.

Expressioni

Gene expression databases

GenevestigatoriP04785.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi247538. 1 interaction.
IntActiP04785. 1 interaction.
MINTiMINT-4996344.
STRINGi10116.ENSRNOP00000051841.

Structurei

3D structure databases

ProteinModelPortaliP04785.
SMRiP04785. Positions 20-359, 370-473.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 136117Thioredoxin 1
Add
BLAST
Domaini335 – 477143Thioredoxin 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi506 – 5094Prevents secretion from ER

Sequence similaritiesi

Contains 2 thioredoxin domains.

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00740000115202.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP04785.
KOiK09580.
OMAiCHHFLEG.
OrthoDBiEOG7VHSX1.
PhylomeDBiP04785.
TreeFamiTF106381.

Family and domain databases

Gene3Di3.40.30.10. 4 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.

P04785-1 [UniParc]FASTAAdd to Basket

« Hide

MLSRALLCLA LAWAARVGAD ALEEEDNVLV LKKSNFAEAL AAHNYLLVEF    50
YAPWCGHCKA LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG 100
YPTIKFFKNG DTASPKEYTA GREADDIVNW LKKRTGPAAT TLSDTAAAES 150
LVDSSEVTVI GFFKDAGSDS AKQFLLAAEA VDDIPFGITS NSDVFSKYQL 200
DKDGVVLFKK FDEGRNNFEG EITKEKLLDF IKHNQLPLVI EFTEQTAPKI 250
FGGEIKTHIL LFLPKSVSDY DGKLSNFKKA AEGFKGKILF IFIDSDHTDN 300
QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITQFCHHFLE 350
GKIKPHLMSQ ELPEDWDKQP VKVLVGKNFE EVAFDEKKNV FVEFYAPWCG 400
HCKQLAPIWD KLGETYKDHE NIVIAKMDST ANEVEAVKVH SFPTLKFFPA 450
SADRTVIDYN GERTLDGFKK FLESGGQDGA GDNDDLDLEE ALEPDMEEDD 500
DQKAVKDEL 509
Length:509
Mass (Da):56,951
Last modified:October 1, 1989 - v2
Checksum:i3056107F5E8B1B54
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 402AL → P in CAA26675. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21018 mRNA. Translation: AAA40620.1.
BC061857 mRNA. Translation: AAH61857.1.
X02918 mRNA. Translation: CAA26675.1.
M21476 mRNA. Translation: AAA40619.1.
PIRiA24595. ISRTSS.
S68028.
RefSeqiNP_037130.1. NM_012998.1.
UniGeneiRn.4234.

Genome annotation databases

EnsembliENSRNOT00000054958; ENSRNOP00000051841; ENSRNOG00000036689.
GeneIDi25506.
KEGGirno:25506.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21018 mRNA. Translation: AAA40620.1 .
BC061857 mRNA. Translation: AAH61857.1 .
X02918 mRNA. Translation: CAA26675.1 .
M21476 mRNA. Translation: AAA40619.1 .
PIRi A24595. ISRTSS.
S68028.
RefSeqi NP_037130.1. NM_012998.1.
UniGenei Rn.4234.

3D structure databases

ProteinModelPortali P04785.
SMRi P04785. Positions 20-359, 370-473.
ModBasei Search...

Protein-protein interaction databases

BioGridi 247538. 1 interaction.
IntActi P04785. 1 interaction.
MINTi MINT-4996344.
STRINGi 10116.ENSRNOP00000051841.

PTM databases

PhosphoSitei P04785.

Proteomic databases

PaxDbi P04785.
PRIDEi P04785.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000054958 ; ENSRNOP00000051841 ; ENSRNOG00000036689 .
GeneIDi 25506.
KEGGi rno:25506.

Organism-specific databases

CTDi 5034.
RGDi 3244. P4hb.

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00740000115202.
HOGENOMi HOG000162459.
HOVERGENi HBG005920.
InParanoidi P04785.
KOi K09580.
OMAi CHHFLEG.
OrthoDBi EOG7VHSX1.
PhylomeDBi P04785.
TreeFami TF106381.

Enzyme and pathway databases

Reactomei REACT_198584. Collagen biosynthesis and modifying enzymes.
REACT_213899. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi 606925.
PROi P04785.

Gene expression databases

Genevestigatori P04785.

Family and domain databases

Gene3Di 3.40.30.10. 4 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

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPDIA1_RAT
AccessioniPrimary (citable) accession number: P04785
Secondary accession number(s): P13700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 1, 1989
Last modified: September 3, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally (1 Publication and 1 Publication) thought to be identical to thyroxine deiodinase but this was later shown (1 Publication) to be incorrect.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi