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Protein

Protein disulfide isomerase-like 1-3

Gene

PDIL1-3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei128 – 1281NucleophileBy similarity
Active sitei131 – 1311NucleophileBy similarity
Sitei190 – 1901Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei467 – 4671NucleophileBy similarity
Sitei468 – 4681Contributes to redox potential valueBy similarity
Sitei469 – 4691Contributes to redox potential valueBy similarity
Active sitei470 – 4701NucleophileBy similarity
Sitei532 – 5321Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • protein folding Source: GO_Central
  • response to endoplasmic reticulum stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide isomerase-like 1-3 (EC:5.3.4.1)
Short name:
AtPDIL1-3
Alternative name(s):
Protein disulfide isomerase 1
Short name:
AtPDI1
Protein disulfide isomerase-like 2-1
Short name:
AtPDIL2-1
Gene namesi
Name:PDIL1-3
Synonyms:PDI1, PDI72, PDIL2-1
Ordered Locus Names:At3g54960
ORF Names:F28P10.60, T15C9.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G54960.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • endoplasmic reticulum Source: TAIR
  • endoplasmic reticulum lumen Source: UniProtKB-SubCell
  • vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 579554Protein disulfide isomerase-like 1-3PRO_5000065917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi27 – 271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi128 ↔ 131Redox-activePROSITE-ProRule annotation
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi467 ↔ 470Redox-activePROSITE-ProRule annotation
Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8VX13.
PRIDEiQ8VX13.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

By chemically-induced ER stress response.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi9977. 1 interaction.
IntActiQ8VX13. 1 interaction.
STRINGi3702.AT3G54960.1.

Structurei

3D structure databases

ProteinModelPortaliQ8VX13.
SMRiQ8VX13. Positions 95-546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 204124Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini416 – 546131Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi576 – 5794Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000162459.
InParanoidiQ8VX13.
KOiK09580.
OMAiGGSYHEE.
PhylomeDBiQ8VX13.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VX13-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASSSTSISL LLFVSFILLL VNSRAENASS GSDLDEELAF LAAEESKEQS
60 70 80 90 100
HGGGSYHEEE HDHQHRDFEN YDDLEQGGGE FHHGDHGYEE EPLPPVDEKD
110 120 130 140 150
VAVLTKDNFT EFVGNNSFAM VEFYAPWCGA CQALTPEYAA AATELKGLAA
160 170 180 190 200
LAKIDATEEG DLAQKYEIQG FPTVFLFVDG EMRKTYEGER TKDGIVTWLK
210 220 230 240 250
KKASPSIHNI TTKEEAERVL SAEPKLVFGF LNSLVGSESE ELAAASRLED
260 270 280 290 300
DLSFYQTASP DIAKLFEIET QVKRPALVLL KKEEEKLARF DGNFTKTAIA
310 320 330 340 350
EFVSANKVPL VINFTREGAS LIFESSVKNQ LILFAKANES EKHLPTLREV
360 370 380 390 400
AKSFKGKFVF VYVQMDNEDY GEAVSGFFGV TGAAPKVLVY TGNEDMRKFI
410 420 430 440 450
LDGELTVNNI KTLAEDFLAD KLKPFYKSDP LPENNDGDVK VIVGNNFDEI
460 470 480 490 500
VLDESKDVLL EIYAPWCGHC QSFEPIYNKL GKYLKGIDSL VVAKMDGTSN
510 520 530 540 550
EHPRAKADGF PTILFFPGGN KSFDPIAVDV DRTVVELYKF LKKHASIPFK
560 570
LEKPATPEPV ISTMKSDEKI EGDSSKDEL
Length:579
Mass (Da):64,212
Last modified:March 1, 2002 - v1
Checksum:i0DF50E500B24B829
GO
Isoform 2 (identifier: Q8VX13-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     507-518: ADGFPTILFFPG → VIKKKELRKSFW
     519-579: Missing.

Note: No experimental confirmation available.
Show »
Length:518
Mass (Da):57,691
Checksum:iB3AA1BB3BAFE49FF
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei507 – 51812ADGFP…LFFPG → VIKKKELRKSFW in isoform 2. 1 PublicationVSP_039979Add
BLAST
Alternative sequencei519 – 57961Missing in isoform 2. 1 PublicationVSP_039980Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT06724.
RefSeqiNP_001118842.1. NM_001125370.1. [Q8VX13-2]
NP_191056.2. NM_115353.4. [Q8VX13-1]
UniGeneiAt.22358.

Genome annotation databases

EnsemblPlantsiAT3G54960.1; AT3G54960.1; AT3G54960. [Q8VX13-1]
GeneIDi824661.
KEGGiath:AT3G54960.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT06724.
RefSeqiNP_001118842.1. NM_001125370.1. [Q8VX13-2]
NP_191056.2. NM_115353.4. [Q8VX13-1]
UniGeneiAt.22358.

3D structure databases

ProteinModelPortaliQ8VX13.
SMRiQ8VX13. Positions 95-546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9977. 1 interaction.
IntActiQ8VX13. 1 interaction.
STRINGi3702.AT3G54960.1.

Proteomic databases

PaxDbiQ8VX13.
PRIDEiQ8VX13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G54960.1; AT3G54960.1; AT3G54960. [Q8VX13-1]
GeneIDi824661.
KEGGiath:AT3G54960.

Organism-specific databases

TAIRiAT3G54960.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000162459.
InParanoidiQ8VX13.
KOiK09580.
OMAiGGSYHEE.
PhylomeDBiQ8VX13.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ8VX13.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiPDI13_ARATH
AccessioniPrimary (citable) accession number: Q8VX13
Secondary accession number(s): B3H5N9, Q9SV44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: March 1, 2002
Last modified: July 22, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.