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O48773 (PDI23_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 2-3
Short name=AtPDIL2-3
EC=5.3.4.1
Alternative name(s):
Protein disulfide-isomerase 5-2
Short name=AtPDIL5-2
Protein disulfide-isomerase 9
Short name=PDI9
Gene names
Name:PDIL2-3
Synonyms:PDI9, PDIL5-2
Ordered Locus Names:At2g32920
ORF Names:T21L14.14
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds By similarity.

Catalytic activity

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

Subcellular location

Endoplasmic reticulum lumen Probable.

Tissue specificity

Widely expressed. Ref.5

Induction

By chemically-induced ER stress response. Ref.5

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 – 2424 Potential
Chain25 – 440416Protein disulfide-isomerase 2-3
PRO_0000400023

Regions

Domain25 – 136112Thioredoxin 1
Domain154 – 269116Thioredoxin 2
Motif437 – 4404Prevents secretion from ER By similarity

Sites

Active site601Nucleophile By similarity
Active site631Nucleophile By similarity
Active site1921Nucleophile By similarity
Active site1951Nucleophile By similarity
Site611Contributes to redox potential value By similarity
Site621Contributes to redox potential value By similarity
Site1221Lowers pKa of C-terminal Cys of first active site By similarity
Site1931Contributes to redox potential value By similarity
Site1941Contributes to redox potential value By similarity
Site2551Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation1681N-linked (GlcNAc...) Potential
Disulfide bond60 ↔ 63Redox-active By similarity
Disulfide bond192 ↔ 195Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O48773 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 2CA62D29A9E9ED01

FASTA44047,755
        10         20         30         40         50         60 
MYKSPLTLLT LLTICFGFFD LSSALYGSSS PVVQLTASNF KSKVLNSNGV VLVEFFAPWC 

        70         80         90        100        110        120 
GHCKALTPTW EKVANILKGV ATVAAIDADA HQSAAQDYGI KGFPTIKVFV PGKAPIDYQG 

       130        140        150        160        170        180 
ARDAKSIANF AYKQIKGLLS DRLEGKSKPT GGGSKEKKSE PSASVELNAS NFDDLVIESN 

       190        200        210        220        230        240 
ELWIVEFFAP WCGHCKKLAP EWKRAAKNLQ GKVKLGHVNC DVEQSIMSRF KVQGFPTILV 

       250        260        270        280        290        300 
FGPDKSSPYP YEGARSASAI ESFASELVES SAGPVEVTEL TGPDVMEKKC GSAAICFISF 

       310        320        330        340        350        360 
LPDILDSKAE GRNKYLEMLL SVAEKFKKQP YSFMWVAAVT QMDLEKRVNV GGYGYPAMVA 

       370        380        390        400        410        420 
MNVKKGVYAP LKSAFELQHL LEFVKDAGTG GKGNVPMNGT PEIVKTKEWD GKDGELIEED 

       430        440 
EFSLDELMGG DDAVGSKDEL

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins."
Houston N.L., Fan C., Xiang J.Q., Schulze J.M., Jung R., Boston R.S.
Plant Physiol. 137:762-778(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[5]"Endoplasmic reticulum stress activates the expression of a sub-group of protein disulfide isomerase genes and AtbZIP60 modulates the response in Arabidopsis thaliana."
Lu D.-P., Christopher D.A.
Mol. Genet. Genomics 280:199-210(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[6]"The protein disulfide isomerase gene family in bread wheat (T. aestivum L.)."
d'Aloisio E., Paolacci A.R., Dhanapal A.P., Tanzarella O.A., Porceddu E., Ciaffi M.
BMC Plant Biol. 10:101-101(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC003033 Genomic DNA. Translation: AAB91984.1.
CP002685 Genomic DNA. Translation: AEC08762.1.
AY054270 mRNA. Translation: AAL06929.1.
AY072321 mRNA. Translation: AAL61928.1.
AY128728 mRNA. Translation: AAM91128.1.
IPIIPI00539108.
PIRT01115.
RefSeqNP_180851.1. NM_128852.4.
UniGeneAt.12475.

3D structure databases

ProteinModelPortalO48773.
SMRO48773. Positions 24-275.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT2G32920.1-P.

Proteomic databases

PaxDbO48773.
PRIDEO48773.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G32920.1; AT2G32920.1; AT2G32920.
GeneID817854.
KEGGath:AT2G32920.

Organism-specific databases

TAIRAt2g32920.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000012631.
InParanoidO48773.
KOK09584.
OMASNELWIV.
PhylomeDBO48773.
ProtClustDBCLSN2683410.

Gene expression databases

GenevestigatorO48773.

Family and domain databases

Gene3D3.40.30.10. 2 hits.
InterProIPR005788. 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. Thiordxn-like_fd. 3 hits.
TIGRFAMsTIGR01126. 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 namePDI23_ARATH
AccessionPrimary (citable) accession number: O48773
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: June 1, 1998
Last modified: May 29, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents