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Protein

Protein disulfide isomerase-like 1-6

Gene

PDIL1-6

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei104 – 1041NucleophileBy similarity
Active sitei446 – 4461NucleophileBy similarity
Active sitei449 – 4491NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciARA:AT3G16110-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide isomerase-like 1-6 (EC:5.3.4.1)
Short name:
AtPDIL1-6
Alternative name(s):
Protein disulfide isomerase 4
Short name:
AtPDI4
Protein disulfide isomerase-like 3-2
Short name:
AtPDIL3-2
Gene namesi
Name:PDIL1-6
Synonyms:PDI4, PDIL3-2
Ordered Locus Names:At3g16110
ORF Names:MSL1.15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G16110.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 534504Protein disulfide isomerase-like 1-6PRO_0000400021Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi446 ↔ 449Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ66GQ3.
PRIDEiQ66GQ3.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

GenevestigatoriQ66GQ3.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G16110.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ66GQ3.
SMRiQ66GQ3. Positions 77-530.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 182127Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini407 – 524118Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi531 – 5344Prevents 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.
HOGENOMiHOG000241706.
InParanoidiQ66GQ3.
KOiK09580.
OMAiPWCINCE.
PhylomeDBiQ66GQ3.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q66GQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTKPKPNSK FSILFTFLLL LSFLIFVARS SDVAVEAGSE EELDDLEQLL
60 70 80 90 100
AVDEQLQEER PEQQSEAETV SKAQRIVVEL NGDNTKRLID GNEYVMVLGY
110 120 130 140 150
APWCARSAEL MPRFAEAATD LKEIGSSVLM AKIDGERYSK VASQLEIKGF
160 170 180 190 200
PTLLLFVNGT SQSYTGGFSS EEIVIWVQKK TGASTIKLDT VDEASGFLKK
210 220 230 240 250
HHTFILGLFE KSEDSSGHDE FVKAASLDNE IQFVETSSID VAKLLFPNLK
260 270 280 290 300
TNNVFVGLVK TEAEKYTSYD GPCQAEKIVE FLNSNKFPLV TKLTESNTVR
310 320 330 340 350
VYSSPVKLQV MVFSKTDDFE SLAQPLEDIA RKFKSKLMLI YIDISNENLA
360 370 380 390 400
MPFLTLFGIE DAKKTVVAAF DNNLNSKYLL ESDPSPSNIE EFCFGLAHGT
410 420 430 440 450
VSAYYKSQPI PDNQNASVVA VVGRTFDEVV LRSSENVLLE VHTPWCINCE
460 470 480 490 500
ALSKQVEKLS QHFKGFENLV FARIDASANE HPKLTVDDYP TILLYKTGEK
510 520 530
ENPLKLSTKS SAKDMAVLIN KELKWKDQSG KDEL
Length:534
Mass (Da):59,571
Last modified:October 11, 2004 - v1
Checksum:i66FA90F57CF5FF85
GO

Sequence cautioni

The sequence BAB02677.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti326 – 3261L → P in BAD94313 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012247 Genomic DNA. Translation: BAB02677.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE75772.1.
BT015349 mRNA. Translation: AAU05472.1.
BT015798 mRNA. Translation: AAU93570.1.
AK221388 mRNA. Translation: BAD94313.1.
RefSeqiNP_188232.2. NM_112481.3.
UniGeneiAt.50187.

Genome annotation databases

EnsemblPlantsiAT3G16110.1; AT3G16110.1; AT3G16110.
GeneIDi820856.
KEGGiath:AT3G16110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012247 Genomic DNA. Translation: BAB02677.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE75772.1.
BT015349 mRNA. Translation: AAU05472.1.
BT015798 mRNA. Translation: AAU93570.1.
AK221388 mRNA. Translation: BAD94313.1.
RefSeqiNP_188232.2. NM_112481.3.
UniGeneiAt.50187.

3D structure databases

ProteinModelPortaliQ66GQ3.
SMRiQ66GQ3. Positions 77-530.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G16110.1-P.

Proteomic databases

PaxDbiQ66GQ3.
PRIDEiQ66GQ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G16110.1; AT3G16110.1; AT3G16110.
GeneIDi820856.
KEGGiath:AT3G16110.

Organism-specific databases

TAIRiAT3G16110.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000241706.
InParanoidiQ66GQ3.
KOiK09580.
OMAiPWCINCE.
PhylomeDBiQ66GQ3.

Enzyme and pathway databases

BioCyciARA:AT3G16110-MONOMER.

Miscellaneous databases

PROiQ66GQ3.

Gene expression databases

GenevestigatoriQ66GQ3.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(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. "Arabidopsis ORF clones."
    Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    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.

Entry informationi

Entry nameiPDI16_ARATH
AccessioniPrimary (citable) accession number: Q66GQ3
Secondary accession number(s): Q56YD5, Q9LW75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: October 11, 2004
Last modified: April 29, 2015
This is version 88 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.