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Q9FF55 (PDI14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide isomerase-like 1-4

Short name=AtPDIL1-4
EC=5.3.4.1
Alternative name(s):
Protein disulfide isomerase 2
Short name=AtPDI2
Protein disulfide isomerase-like 2-2
Short name=AtPDIL2-2
Gene names
Name:PDIL1-4
Synonyms:PDI2, PDIL2-2
Ordered Locus Names:At5g60640
ORF Names:MUP24.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length597 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.8

Catalytic activity

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

Subunit structure

Interacts with MEE8 and MED37A. Ref.8

Subcellular location

Endoplasmic reticulum lumen. Golgi apparatus. Vacuole. Nucleus. Secretedcell wall Ref.8.

Tissue specificity

Expressed in germinating seedling, including the cotyledons and hypocotyl, in vascular tissues, in pollen grains, root tips, leaf trichomes, developing seeds and siliques. Ref.6 Ref.8

Disruption phenotype

No visible phenotype, probably due to functional redundancy. Ref.8

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Ontologies

Keywords
   Cellular componentCell wall
Endoplasmic reticulum
Golgi apparatus
Nucleus
Secreted
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.6. Source: GOC

response to oxidative stress

Inferred from direct assay PubMed 12492832. Source: TAIR

   Cellular_componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

chloroplast

Inferred from direct assay PubMed 15028209. Source: TAIR

endoplasmic reticulum

Inferred from direct assay PubMed 16618929Ref.8PubMed 22923678. Source: TAIR

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from direct assay PubMed 12492832PubMed 14671022. Source: TAIR

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

vacuolar membrane

Inferred from direct assay PubMed 17151019. Source: TAIR

   Molecular_functionprotein disulfide isomerase activity

Inferred from sequence or structural similarity Ref.6. Source: TAIR

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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: Q9FF55-1)

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 – 2525 Potential
Chain26 – 597572Protein disulfide isomerase-like 1-4
PRO_0000400019

Regions

Domain85 – 208124Thioredoxin 1
Domain429 – 550122Thioredoxin 2
Motif594 – 5974Prevents secretion from ER By similarity

Sites

Active site1321Nucleophile By similarity
Active site1351Nucleophile By similarity
Active site4711Nucleophile By similarity
Active site4741Nucleophile By similarity
Site1331Contributes to redox potential value By similarity
Site1341Contributes to redox potential value By similarity
Site1941Lowers pKa of C-terminal Cys of first active site By similarity
Site4721Contributes to redox potential value By similarity
Site4731Contributes to redox potential value By similarity
Site5361Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation5241N-linked (GlcNAc...) Potential
Disulfide bond132 ↔ 135Redox-active By similarity
Disulfide bond471 ↔ 474Redox-active By similarity

Experimental info

Sequence conflict4001P → H in AAM65262. Ref.4

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: 5A8FC7E72AA64B2B

FASTA59766,357
        10         20         30         40         50         60 
MAFRVLLLFS LTALLIFSAV SPSFAASSSD DVDDEDLSFL EDLKEDDVPG ADSLSSSTGF 

        70         80         90        100        110        120 
DEFEGGEEED PDMYNDDDDE EGDFSDLGNP DSDPLPTPEI DEKDVVVIKE RNFTDVIENN 

       130        140        150        160        170        180 
QYVLVEFYAP WCGHCQSLAP EYAAAATELK EDGVVLAKID ATEENELAQE YRVQGFPTLL 

       190        200        210        220        230        240 
FFVDGEHKPY TGGRTKETIV TWVKKKIGPG VYNLTTLDDA EKVLTSGNKV VLGYLNSLVG 

       250        260        270        280        290        300 
VEHDQLNAAS KAEDDVNFYQ TVNPDVAKMF HLDPESKRPA LVLVKKEEEK ISHFDGEFVK 

       310        320        330        340        350        360 
SALVSFVSAN KLALVSVFTR ETAPEIFESA IKKQLLLFVT KNESEKVLTE FQEAAKSFKG 

       370        380        390        400        410        420 
KLIFVSVDLD NEDYGKPVAE YFGVSGNGPK LIGYTGNEDP KKYFFDGEIQ SDKIKIFGED 

       430        440        450        460        470        480 
FLNDKLKPFY KSDPIPEKND EDVKIVVGDN FDEIVLDDSK DVLLEVYAPW CGHCQALEPM 

       490        500        510        520        530        540 
YNKLAKHLRS IDSLVITKMD GTTNEHPKAK AEGFPTILFF PAGNKTSEPI TVDTDRTVVA 

       550        560        570        580        590 
FYKFLRKHAT IPFKLEKPAS TESPKTAEST PKVETTETKE SPDSTTKSSQ SDSKDEL 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
DNA Res. 4:215-230(1997) [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]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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.
[6]"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.
[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.
[8]"Protein disulfide isomerase-2 of Arabidopsis mediates protein folding and localizes to both the secretory pathway and nucleus, where it interacts with maternal effect embryo arrest factor."
Cho E.J., Yuen C.Y., Kang B.H., Ondzighi C.A., Staehelin L.A., Christopher D.A.
Mol. Cells 32:459-475(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MEE8 AND MED37A/BIP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB005246 Genomic DNA. Translation: BAB09837.1.
CP002688 Genomic DNA. Translation: AED97360.1.
BT001994 mRNA. Translation: AAN72005.1.
BT008359 mRNA. Translation: AAP37718.1.
AY087725 mRNA. Translation: AAM65262.1.
RefSeqNP_851234.1. NM_180903.3.
UniGeneAt.22422.

3D structure databases

ProteinModelPortalQ9FF55.
SMRQ9FF55. Positions 5-550.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid21429. 10 interactions.
STRING3702.AT5G60640.1-P.

Proteomic databases

PaxDbQ9FF55.
PRIDEQ9FF55.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G60640.1; AT5G60640.1; AT5G60640. [Q9FF55-1]
GeneID836185.
KEGGath:AT5G60640.

Organism-specific databases

TAIRAT5G60640.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
InParanoidQ9FF55.
KOK09580.
OMAKHATIPF.
PhylomeDBQ9FF55.
ProtClustDBCLSN2680577.

Enzyme and pathway databases

BioCycARA:AT5G60640-MONOMER.
ARA:GQT-84-MONOMER.
ARA:GQT-85-MONOMER.

Gene expression databases

GenevestigatorQ9FF55.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. 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.
TIGR01126. pdi_dom. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDI14_ARATH
AccessionPrimary (citable) accession number: Q9FF55
Secondary accession number(s): Q8LAM5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 106 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