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Q9XI01 (PDI11_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide isomerase-like 1-1

Short name=AtPDIL1-1
EC=5.3.4.1
Alternative name(s):
Protein disulfide-isomerase 1
Short name=PDI 1
Protein disulfide-isomerase 5
Short name=AtPDI5
Gene names
Name:PDIL1-1
Synonyms:PDI5
Ordered Locus Names:At1g21750
ORF Names:F8K7.19
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length501 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 that associates with RD21A protease for trafficking from the ER through the Golgi to lytic and protein storage vacuoles of endothelial cells in developing seeds. Regulates the timing of programmed cell death (PCD) of the endothelial cells by chaperoning and inhibiting cysteine proteases during their trafficking to vacuoles. Ref.6

Catalytic activity

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

Subunit structure

Interacts with RD21A, At3g19390, At5g43060. Ref.6

Subcellular location

Endoplasmic reticulum lumen. Vacuole. Note: Found in protein storage vacuoles and lytic vacuoles in endothelial cells of developing seeds. Ref.6

Tissue specificity

Highly expressed in flowers, stems and immature seeds, and at lower levels in leaves and siliques (at protein level). Ref.5 Ref.6

Developmental stage

During embryo development, expressed exclusively in endothelial cells from the pre-embryo up to the heart stage. Expression disappears when the endothelial cells undergo PCD in the early-bent cotyledon stage (at protein level).

Induction

By chemically-induced ER stress response. Ref.5

Disruption phenotype

Reduced seed set. Ref.6

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Vacuole
   Coding sequence diversityAlternative splicing
   DomainRedox-active center
Repeat
Signal
   Molecular functionIsomerase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

protein folding

Inferred from sequence or structural similarity Ref.5. Source: GOC

regulation of programmed cell death

Inferred from mutant phenotype Ref.6. Source: TAIR

response to endoplasmic reticulum stress

Inferred from expression pattern Ref.5. Source: TAIR

response to salt stress

Inferred from expression pattern PubMed 17916636. Source: TAIR

response to zinc ion

Inferred from expression pattern PubMed 19880396. Source: TAIR

seed development

Inferred from mutant phenotype Ref.6. Source: TAIR

   Cellular_componentchloroplast

Inferred from direct assay PubMed 15028209. Source: TAIR

endoplasmic reticulum

Inferred from direct assay PubMed 16618929PubMed 22923678. Source: TAIR

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

lytic vacuole within protein storage vacuole

Inferred from direct assay Ref.6. Source: TAIR

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

plant-type cell wall

Inferred from direct assay PubMed 17526915. Source: TAIR

protein storage vacuole

Inferred from direct assay Ref.6. Source: TAIR

thylakoid

Inferred from direct assay PubMed 11826309. Source: TAIR

vacuole

Inferred from direct assay PubMed 15539469. Source: TAIR

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6. Source: IntAct

protein disulfide isomerase activity

Inferred from sequence or structural similarity Ref.5. Source: TAIR

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

At5g43060/MMG4.7Q9FMH83EBI-449394,EBI-1993115
RD21AP432974EBI-449394,EBI-1993101

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9XI01-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 501478Protein disulfide isomerase-like 1-1
PRO_0000034205

Regions

Domain24 – 141118Thioredoxin 1
Domain354 – 482129Thioredoxin 2
Motif498 – 5014Prevents secretion from ER By similarity

Sites

Active site591Nucleophile By similarity
Active site621Nucleophile By similarity
Active site4041Nucleophile By similarity
Active site4071Nucleophile By similarity
Site601Contributes to redox potential value By similarity
Site611Contributes to redox potential value By similarity
Site1271Lowers pKa of C-terminal Cys of first active site By similarity
Site4051Contributes to redox potential value By similarity
Site4061Contributes to redox potential value By similarity
Site4681Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Disulfide bond59 ↔ 62Redox-active By similarity
Disulfide bond404 ↔ 407Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: C27C564D38ECA6E8

FASTA50155,602
        10         20         30         40         50         60 
MAMRGFTLFS ILVLSLCASS IRSEETETKE FVLTLDHTNF TDTINKHDFI VVEFYAPWCG 

        70         80         90        100        110        120 
HCKQLAPEYE KAASALSSNV PPVVLAKIDA SEETNREFAT QYEVQGFPTI KIFRNGGKAV 

       130        140        150        160        170        180 
QEYNGPREAE GIVTYLKKQS GPASAEIKSA DDASEVVSDK KVVVVGIFPK LSGSEFDSFM 

       190        200        210        220        230        240 
AIAEKLRSEL DFAHTSDAKL LPRGESSVTG PVVRLFKPFD EQFVDSKDFD GEALEKFVKE 

       250        260        270        280        290        300 
SSIPLITVFD KDPNNHPYVI KFFESTNTKA MLFINFTGEG AESLKSKYRE VATSNKGQGL 

       310        320        330        340        350        360 
SFLLGDAENS QGAFQYFGLE ESQVPLIIIQ TADDKKYLKT NVEVDQIESW VKDFKDGKIA 

       370        380        390        400        410        420 
PHKKSQPIPA ENNEPVKVVV SDSLDDIVLN SGKNVLLEFY APWCGHCQKL APILDEVAVS 

       430        440        450        460        470        480 
YQSDSSVVIA KLDATANDFP KDTFDVKGFP TIYFKSASGN VVVYEGDRTK EDFISFVDKN 

       490        500 
KDTVGEPKKE EETTEEVKDE L 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [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]"Arabidopsis protein disulfide isomerase-5 inhibits cysteine proteases during trafficking to vacuoles before programmed cell death of the endothelium in developing seeds."
Andeme Ondzighi C., Christopher D.A., Cho E.J., Chang S.C., Staehelin L.A.
Plant Cell 20:2205-2220(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RD21A; AT3G19390 AND AT5G43060, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[7]"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
AC007727 Genomic DNA. Translation: AAD41430.1.
CP002684 Genomic DNA. Translation: AEE30151.1.
AY035096 mRNA. Translation: AAK59601.1.
AY063059 mRNA. Translation: AAL34233.1.
PIRB86351.
RefSeqNP_173594.1. NM_102024.3. [Q9XI01-1]
UniGeneAt.24814.

3D structure databases

ProteinModelPortalQ9XI01.
SMRQ9XI01. Positions 25-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid24018. 4 interactions.
IntActQ9XI01. 5 interactions.

2D gel databases

SWISS-2DPAGEQ9XI01.

Proteomic databases

PaxDbQ9XI01.
PRIDEQ9XI01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G21750.1; AT1G21750.1; AT1G21750. [Q9XI01-1]
GeneID838779.
KEGGath:AT1G21750.

Organism-specific databases

TAIRAT1G21750.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
InParanoidQ9XI01.
KOK09580.
OMAIYFAPRD.
PhylomeDBQ9XI01.

Enzyme and pathway databases

BioCycARA:AT1G21750-MONOMER.
ARA:GQT-2441-MONOMER.

Gene expression databases

ArrayExpressQ9XI01.
GenevestigatorQ9XI01.

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 namePDI11_ARATH
AccessionPrimary (citable) accession number: Q9XI01
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 118 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names