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P52588 (PDI_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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
Gene names
Name:PDI
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer By similarity.

Catalytic activity

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

Subcellular location

Endoplasmic reticulum lumen Potential.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 By similarity
Chain24 – 513490Protein disulfide-isomerase
PRO_0000034210

Regions

Domain24 – 145122Thioredoxin 1
Domain366 – 485120Thioredoxin 2
Motif510 – 5134Prevents secretion from ER Potential

Sites

Active site631Nucleophile By similarity
Active site661Nucleophile By similarity
Active site4081Nucleophile By similarity
Active site4111Nucleophile By similarity
Site641Contributes to redox potential value By similarity
Site651Contributes to redox potential value By similarity
Site1311Lowers pKa of C-terminal Cys of first active site By similarity
Site4091Contributes to redox potential value By similarity
Site4101Contributes to redox potential value By similarity
Site4711Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation2791N-linked (GlcNAc...) Potential
Disulfide bond63 ↔ 66Redox-active By similarity
Disulfide bond408 ↔ 411Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P52588 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 29302DD01A3DEB80

FASTA51357,097
        10         20         30         40         50         60 
MAIRSKAWIS LLLALAVALS ARAEEEPAAA AEGEAVLTLD VDSFDEAVAK HPFMVVEFYA 

        70         80         90        100        110        120 
PWCGHCKKLA PEYENAAKAL SKHDPPIVLA KVDANEEKNR PLATKYEIQG FPTIKIFRDR 

       130        140        150        160        170        180 
GKNIQEYKGP READGIVDYL KKQVGPASKE IKSPEDATAL IDDKKIYIVG IFAEFSGTEF 

       190        200        210        220        230        240 
TNFMEVAEKL RSDYDFGHTL HANHLPRGDA AVERPLVRLL KPFDELVVDS KDFDVAALMK 

       250        260        270        280        290        300 
FIDASTIPRV VTFDKNPDNH PYLMKFFQSS APKAMLFLNF STGPFDSFKS AYSAAAEEFK 

       310        320        330        340        350        360 
DKEIKFLIGD IEASQGAFQY FGLKEDQTPL ILIQDGDSKK FLKVHVEADQ IVAWLKEYFD 

       370        380        390        400        410        420 
GKLTPFRNSE PIPEVNNEPV KVVVADNVHD FVFKSGKNVL IEFYAPWCGH CKKLAPILDE 

       430        440        450        460        470        480 
AATTLQSDEE VVIAKMDATA NDVPSEFDVQ GYPTLYFVTP SGKVTSYDSG RTADDIVDFI 

       490        500        510 
KKSKETAAPH HHHHPGATGI REGSRAEPVK DEL 

« Hide

References

[1]"Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant."
Li C.P., Larkins B.A.
Plant Mol. Biol. 30:873-882(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Wisconsin 64A.
Tissue: Endosperm.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L39014 mRNA. Translation: AAB08519.1.
PIRS69181.

3D structure databases

ProteinModelPortalP52588.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP52588.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP52588.
MaizeGDB86830.

Family and domain databases

Gene3D3.40.30.10. 3 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...

Entry information

Entry namePDI_MAIZE
AccessionPrimary (citable) accession number: P52588
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families