Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P17967 (PDI_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
Thioredoxin-related glycoprotein 1
Gene names
Name:PDI1
Synonyms:MFP1, TRG1
Ordered Locus Names:YCL043C
ORF Names:YCL313, YCL43C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bonds. Forms a complex with MNL1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response. Ref.9 Ref.10 Ref.11

Catalytic activity

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

Subunit structure

Interacts with EPS1, KAR2 and MNL1. Ref.9 Ref.10 Ref.11

Subcellular location

Endoplasmic reticulum lumen Potential.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RNASE1P618232EBI-13012,EBI-908364From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828Or 22 Potential
Chain29 – 522494Protein disulfide-isomerase
PRO_0000034218

Regions

Domain29 – 141113Thioredoxin 1
Domain356 – 485130Thioredoxin 2
Motif519 – 5224Prevents secretion from ER

Sites

Active site611Nucleophile By similarity
Active site641Nucleophile By similarity
Active site4061Nucleophile By similarity
Active site4091Nucleophile By similarity
Site621Contributes to redox potential value By similarity
Site631Contributes to redox potential value By similarity
Site1261Lowers pKa of C-terminal Cys of first active site By similarity
Site4071Contributes to redox potential value By similarity
Site4081Contributes to redox potential value By similarity
Site4711Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation4251N-linked (GlcNAc...) Potential
Disulfide bond61 ↔ 64Redox-active Ref.12
Disulfide bond406 ↔ 409Redox-active Ref.12

Experimental info

Sequence conflict33 – 5220AVVKL…SHDLV → LSLSWPPTLSMNTFSRTTWW in AAA34848. Ref.3
Sequence conflict831I → V in CAA36550. Ref.4
Sequence conflict831I → V in AAA35169. Ref.4
Sequence conflict1141S → R in CAA38402. Ref.5
Sequence conflict1431V → S Ref.4
Sequence conflict1461Missing Ref.4
Sequence conflict1681K → E in CAA36550. Ref.4
Sequence conflict1681K → E in AAA35169. Ref.4
Sequence conflict1971D → E in AAA34848. Ref.3
Sequence conflict2151V → R AA sequence Ref.1
Sequence conflict2261A → V in CAA36550. Ref.4
Sequence conflict2261A → V in AAA35169. Ref.4
Sequence conflict3331E → S AA sequence Ref.1
Sequence conflict3511S → P in AAA34848. Ref.3
Sequence conflict4551L → F in AAA34848. Ref.3
Sequence conflict4581G → S in CAA36550. Ref.4
Sequence conflict4581G → S in AAA35169. Ref.4
Sequence conflict5051A → AEADAEAEA Ref.4
Sequence conflict5051A → AEADAEAEA Ref.5

Secondary structure

............................................................................ 522
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17967 [UniParc].

Last modified March 1, 1992. Version 2.
Checksum: 69CF3E05D7F74C94

FASTA52258,227
        10         20         30         40         50         60 
MKFSAGAVLS WSSLLLASSV FAQQEAVAPE DSAVVKLATD SFNEYIQSHD LVLAEFFAPW 

        70         80         90        100        110        120 
CGHCKNMAPE YVKAAETLVE KNITLAQIDC TENQDLCMEH NIPGFPSLKI FKNSDVNNSI 

       130        140        150        160        170        180 
DYEGPRTAEA IVQFMIKQSQ PAVAVVADLP AYLANETFVT PVIVQSGKID ADFNATFYSM 

       190        200        210        220        230        240 
ANKHFNDYDF VSAENADDDF KLSIYLPSAM DEPVVYNGKK ADIADADVFE KWLQVEALPY 

       250        260        270        280        290        300 
FGEIDGSVFA QYVESGLPLG YLFYNDEEEL EEYKPLFTEL AKKNRGLMNF VSIDARKFGR 

       310        320        330        340        350        360 
HAGNLNMKEQ FPLFAIHDMT EDLKYGLPQL SEEAFDELSD KIVLESKAIE SLVKDFLKGD 

       370        380        390        400        410        420 
ASPIVKSQEI FENQDSSVFQ LVGKNHDEIV NDPKKDVLVL YYAPWCGHCK RLAPTYQELA 

       430        440        450        460        470        480 
DTYANATSDV LIAKLDHTEN DVRGVVIEGY PTIVLYPGGK KSESVVYQGS RSLDSLFDFI 

       490        500        510        520 
KENGHFDVDG KALYEEAQEK AAEEADADAE LADEEDAIHD EL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular structure of a yeast gene, PDI1, encoding protein disulfide isomerase that is essential for cell growth."
Tachikawa H., Miura T., Katakura Y., Mizunaga T.
J. Biochem. 110:306-313(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 26786 / X2180-1A and TM5.
[2]"Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms."
Scherens B., Dubois E., Messenguy F.
Yeast 7:185-193(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast."
Lamantia M., Miura T., Tachikawa H., Kaplan H.A., Lennarz W.J., Mizunaga T.
Proc. Natl. Acad. Sci. U.S.A. 88:4453-4457(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes a lumenal endoplasmic reticulum glycoprotein involved in the maturation of vacuolar carboxypeptidase."
Guenther R., Braeuer C., Janetzky B., Foerster H.H., Ehbrecht I.M., Lehle L., Kuentzel H.
J. Biol. Chem. 266:24557-24563(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae."
Farquhar R., Honey N., Murant S.J., Bossier P., Schultz L., Montogomery D., Ellis R.W., Freedman R.B., Tuite M.F.
Gene 108:81-89(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The complete sequence of a 9,543 bp segment on the left arm of chromosome III reveals five open reading frames including glucokinase and the protein disulfide isomerase."
Scherens B., Messenguy F., Gigot D., Dubois E.
Yeast 8:577-586(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[8]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[9]"Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities."
Kimura T., Hosoda Y., Sato Y., Kitamura Y., Ikeda T., Horibe T., Kikuchi M.
J. Biol. Chem. 280:31438-31441(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EPS1 AND KAR2.
[10]"Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum."
Clerc S., Hirsch C., Oggier D.M., Deprez P., Jakob C., Sommer T., Aebi M.
J. Cell Biol. 184:159-172(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MNL1.
[11]"A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum."
Gauss R., Kanehara K., Carvalho P., Ng D.T., Aebi M.
Mol. Cell 42:782-793(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MNL1.
[12]"The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites."
Tian G., Xiang S., Noiva R., Lennarz W.J., Schindelin H.
Cell 124:61-73(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-522, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00842 Genomic DNA. Translation: BAA00723.1.
X57712 Genomic DNA. Translation: CAA40883.1.
M62815 Genomic DNA. Translation: AAA34848.1.
X52313 Genomic DNA. Translation: CAA36550.1.
M76982 Genomic DNA. Translation: AAA35169.1.
X54535 Genomic DNA. Translation: CAA38402.1.
X59720 Genomic DNA. Translation: CAA42373.1.
BK006937 Genomic DNA. Translation: DAA07442.1.
PIRISBYSS. JX0182.
RefSeqNP_009887.1. NM_001178688.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B5EX-ray2.40A23-522[»]
3BOAX-ray3.70A23-522[»]
ProteinModelPortalP17967.
SMRP17967. Positions 23-494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30941. 162 interactions.
DIPDIP-4978N.
IntActP17967. 10 interactions.
MINTMINT-497035.
STRING4932.YCL043C.

Proteomic databases

PaxDbP17967.
PeptideAtlasP17967.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL043C; YCL043C; YCL043C.
GeneID850314.
KEGGsce:YCL043C.

Organism-specific databases

CYGDYCL043c.
SGDS000000548. PDI1.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00740000115037.
HOGENOMHOG000162459.
KOK09580.
OMAMDSSVNE.
OrthoDBEOG71CFZN.

Enzyme and pathway databases

BioCycYEAST:YCL043C-MONOMER.

Gene expression databases

GenevestigatorP17967.

Family and domain databases

Gene3D3.40.30.10. 2 hits.
InterProIPR005792. Prot_disulphide_isomerase.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17967.
NextBio965715.
PROP17967.

Entry information

Entry namePDI_YEAST
AccessionPrimary (citable) accession number: P17967
Secondary accession number(s): D6VQX3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: March 1, 1992
Last modified: February 19, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references