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Q8VX13 (PDI13_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. 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 1-3

Short name=AtPDIL1-3
EC=5.3.4.1
Alternative name(s):
Protein disulfide isomerase 1
Short name=AtPDI1
Protein disulfide isomerase-like 2-1
Short name=AtPDIL2-1
Gene names
Name:PDIL1-3
Synonyms:PDI1, PDI72, PDIL2-1
Ordered Locus Names:At3g54960
ORF Names:F28P10.60, T15C9.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length579 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.7

Induction

By chemically-induced ER stress response. Ref.7

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence caution

The sequence CAB41088.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VX13-1)

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.
Isoform 2 (identifier: Q8VX13-2)

The sequence of this isoform differs from the canonical sequence as follows:
     507-518: ADGFPTILFFPG → VIKKKELRKSFW
     519-579: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 579554Protein disulfide isomerase-like 1-3
PRO_5000065917

Regions

Domain81 – 204124Thioredoxin 1
Domain416 – 546131Thioredoxin 2
Motif576 – 5794Prevents secretion from ER By similarity

Sites

Active site1281Nucleophile By similarity
Active site1311Nucleophile By similarity
Active site4671Nucleophile By similarity
Active site4701Nucleophile By similarity
Site1901Lowers pKa of C-terminal Cys of first active site By similarity
Site4681Contributes to redox potential value By similarity
Site4691Contributes to redox potential value By similarity
Site5321Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation271N-linked (GlcNAc...) Potential
Glycosylation1081N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Potential
Glycosylation3381N-linked (GlcNAc...) Potential
Glycosylation5201N-linked (GlcNAc...) Potential
Disulfide bond128 ↔ 131Redox-active By similarity
Disulfide bond467 ↔ 470Redox-active By similarity

Natural variations

Alternative sequence507 – 51812ADGFP…LFFPG → VIKKKELRKSFW in isoform 2.
VSP_039979
Alternative sequence519 – 57961Missing in isoform 2.
VSP_039980

Sequences

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

Last modified March 1, 2002. Version 1.
Checksum: 0DF50E500B24B829

FASTA57964,212
        10         20         30         40         50         60 
MASSSTSISL LLFVSFILLL VNSRAENASS GSDLDEELAF LAAEESKEQS HGGGSYHEEE 

        70         80         90        100        110        120 
HDHQHRDFEN YDDLEQGGGE FHHGDHGYEE EPLPPVDEKD VAVLTKDNFT EFVGNNSFAM 

       130        140        150        160        170        180 
VEFYAPWCGA CQALTPEYAA AATELKGLAA LAKIDATEEG DLAQKYEIQG FPTVFLFVDG 

       190        200        210        220        230        240 
EMRKTYEGER TKDGIVTWLK KKASPSIHNI TTKEEAERVL SAEPKLVFGF LNSLVGSESE 

       250        260        270        280        290        300 
ELAAASRLED DLSFYQTASP DIAKLFEIET QVKRPALVLL KKEEEKLARF DGNFTKTAIA 

       310        320        330        340        350        360 
EFVSANKVPL VINFTREGAS LIFESSVKNQ LILFAKANES EKHLPTLREV AKSFKGKFVF 

       370        380        390        400        410        420 
VYVQMDNEDY GEAVSGFFGV TGAAPKVLVY TGNEDMRKFI LDGELTVNNI KTLAEDFLAD 

       430        440        450        460        470        480 
KLKPFYKSDP LPENNDGDVK VIVGNNFDEI VLDESKDVLL EIYAPWCGHC QSFEPIYNKL 

       490        500        510        520        530        540 
GKYLKGIDSL VVAKMDGTSN EHPRAKADGF PTILFFPGGN KSFDPIAVDV DRTVVELYKF 

       550        560        570 
LKKHASIPFK LEKPATPEPV ISTMKSDEKI EGDSSKDEL 

« Hide

Isoform 2 [UniParc].

Checksum: B3AA1BB3BAFE49FF
Show »

FASTA51857,691

References

« Hide 'large scale' references
[1]"Arabidopsis thaliana mRNA for ERp72."
Mahon P.
Thesis (2000), Cambridge University, United Kingdom
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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] (ISOFORM 1).
Strain: cv. Columbia.
[5]"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[6]"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.
[7]"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.
[8]"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
AK318844 mRNA. Translation: BAH56959.1.
AJ271376 mRNA. Translation: CAC81067.1.
AL049655 Genomic DNA. Translation: CAB41088.1. Sequence problems.
AL132970 Genomic DNA. No translation available.
CP002686 Genomic DNA. Translation: AEE79318.1.
CP002686 Genomic DNA. Translation: AEE79319.1.
AY093115 mRNA. Translation: AAM13114.1.
BT000172 mRNA. Translation: AAN15491.1.
PIRT06724.
RefSeqNP_001118842.1. NM_001125370.1. [Q8VX13-2]
NP_191056.2. NM_115353.4. [Q8VX13-1]
UniGeneAt.22358.

3D structure databases

ProteinModelPortalQ8VX13.
SMRQ8VX13. Positions 95-546.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid9977. 1 interaction.
IntActQ8VX13. 1 interaction.
STRING3702.AT3G54960.1-P.

Proteomic databases

PaxDbQ8VX13.
PRIDEQ8VX13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G54960.1; AT3G54960.1; AT3G54960. [Q8VX13-1]
GeneID824661.
KEGGath:AT3G54960.

Organism-specific databases

TAIRAT3G54960.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
InParanoidQ8VX13.
KOK09580.
OMAANESEKH.
PhylomeDBQ8VX13.

Enzyme and pathway databases

BioCycARA:AT3G54960-MONOMER.
ARA:GQT-1367-MONOMER.

Gene expression databases

GenevestigatorQ8VX13.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005792. 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.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDI13_ARATH
AccessionPrimary (citable) accession number: Q8VX13
Secondary accession number(s): B3H5N9, Q9SV44
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 104 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