Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein disulfide isomerase-like 1-1

Gene

PDIL1-1

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

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei59 – 591NucleophileBy similarity
Sitei60 – 601Contributes to redox potential valueBy similarity
Sitei61 – 611Contributes to redox potential valueBy similarity
Active sitei62 – 621NucleophileBy similarity
Sitei127 – 1271Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei404 – 4041NucleophileBy similarity
Sitei405 – 4051Contributes to redox potential valueBy similarity
Sitei406 – 4061Contributes to redox potential valueBy similarity
Active sitei407 – 4071NucleophileBy similarity
Sitei468 – 4681Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: GO_Central

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. embryo development ending in seed dormancy Source: TAIR
  3. protein folding Source: GO_Central
  4. regulation of programmed cell death Source: TAIR
  5. response to cytokinin Source: TAIR
  6. response to endoplasmic reticulum stress Source: TAIR
  7. response to salt stress Source: TAIR
  8. response to zinc ion Source: TAIR
  9. seed development Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide isomerase-like 1-1 (EC:5.3.4.1)
Short name:
AtPDIL1-1
Alternative name(s):
Protein disulfide-isomerase 1
Short name:
PDI 1
Protein disulfide-isomerase 5
Short name:
AtPDI5
Gene namesi
Name:PDIL1-1
Synonyms:PDI5
Ordered Locus Names:At1g21750
ORF Names:F8K7.19
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G21750.

Subcellular locationi

Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation. Vacuole 1 Publication
Note: Found in protein storage vacuoles and lytic vacuoles in endothelial cells of developing seeds.

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. endoplasmic reticulum Source: TAIR
  3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  4. lytic vacuole within protein storage vacuole Source: TAIR
  5. membrane Source: TAIR
  6. plant-type cell wall Source: TAIR
  7. protein storage vacuole Source: TAIR
  8. thylakoid Source: TAIR
  9. vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Vacuole

Pathology & Biotechi

Disruption phenotypei

Reduced seed set.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 501478Protein disulfide isomerase-like 1-1PRO_0000034205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi59 ↔ 62Redox-activePROSITE-ProRule annotation
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi404 ↔ 407Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9XI01.
PRIDEiQ9XI01.

2D gel databases

SWISS-2DPAGEQ9XI01.

Expressioni

Tissue specificityi

Highly expressed in flowers, stems and immature seeds, and at lower levels in leaves and siliques (at protein level).2 Publications

Developmental stagei

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).

Inductioni

By chemically-induced ER stress response.1 Publication

Gene expression databases

ExpressionAtlasiQ9XI01. baseline and differential.
GenevestigatoriQ9XI01.

Interactioni

Subunit structurei

Interacts with RD21A, At3g19390, At5g43060.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
At5g43060/MMG4.7Q9FMH83EBI-449394,EBI-1993115
RD21AP432974EBI-449394,EBI-1993101

Protein-protein interaction databases

BioGridi24018. 4 interactions.
IntActiQ9XI01. 5 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9XI01.
SMRiQ9XI01. Positions 25-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 141118Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini354 – 482129Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi498 – 5014Prevents 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.
InParanoidiQ9XI01.
KOiK09580.
OMAiGTKAMLF.
PhylomeDBiQ9XI01.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. 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.
TIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9XI01-1) [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
MAMRGFTLFS ILVLSLCASS IRSEETETKE FVLTLDHTNF TDTINKHDFI
60 70 80 90 100
VVEFYAPWCG HCKQLAPEYE KAASALSSNV PPVVLAKIDA SEETNREFAT
110 120 130 140 150
QYEVQGFPTI KIFRNGGKAV QEYNGPREAE GIVTYLKKQS GPASAEIKSA
160 170 180 190 200
DDASEVVSDK KVVVVGIFPK LSGSEFDSFM AIAEKLRSEL DFAHTSDAKL
210 220 230 240 250
LPRGESSVTG PVVRLFKPFD EQFVDSKDFD GEALEKFVKE SSIPLITVFD
260 270 280 290 300
KDPNNHPYVI KFFESTNTKA MLFINFTGEG AESLKSKYRE VATSNKGQGL
310 320 330 340 350
SFLLGDAENS QGAFQYFGLE ESQVPLIIIQ TADDKKYLKT NVEVDQIESW
360 370 380 390 400
VKDFKDGKIA PHKKSQPIPA ENNEPVKVVV SDSLDDIVLN SGKNVLLEFY
410 420 430 440 450
APWCGHCQKL APILDEVAVS YQSDSSVVIA KLDATANDFP KDTFDVKGFP
460 470 480 490 500
TIYFKSASGN VVVYEGDRTK EDFISFVDKN KDTVGEPKKE EETTEEVKDE

L
Length:501
Mass (Da):55,602
Last modified:November 1, 1999 - v1
Checksum:iC27C564D38ECA6E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007727 Genomic DNA. Translation: AAD41430.1.
CP002684 Genomic DNA. Translation: AEE30151.1.
AY035096 mRNA. Translation: AAK59601.1.
AY063059 mRNA. Translation: AAL34233.1.
PIRiB86351.
RefSeqiNP_173594.1. NM_102024.3. [Q9XI01-1]
UniGeneiAt.24814.

Genome annotation databases

EnsemblPlantsiAT1G21750.1; AT1G21750.1; AT1G21750. [Q9XI01-1]
GeneIDi838779.
KEGGiath:AT1G21750.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007727 Genomic DNA. Translation: AAD41430.1.
CP002684 Genomic DNA. Translation: AEE30151.1.
AY035096 mRNA. Translation: AAK59601.1.
AY063059 mRNA. Translation: AAL34233.1.
PIRiB86351.
RefSeqiNP_173594.1. NM_102024.3. [Q9XI01-1]
UniGeneiAt.24814.

3D structure databases

ProteinModelPortaliQ9XI01.
SMRiQ9XI01. Positions 25-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi24018. 4 interactions.
IntActiQ9XI01. 5 interactions.

2D gel databases

SWISS-2DPAGEQ9XI01.

Proteomic databases

PaxDbiQ9XI01.
PRIDEiQ9XI01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G21750.1; AT1G21750.1; AT1G21750. [Q9XI01-1]
GeneIDi838779.
KEGGiath:AT1G21750.

Organism-specific databases

TAIRiAT1G21750.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000162459.
InParanoidiQ9XI01.
KOiK09580.
OMAiGTKAMLF.
PhylomeDBiQ9XI01.

Enzyme and pathway databases

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

Gene expression databases

ExpressionAtlasiQ9XI01. baseline and differential.
GenevestigatoriQ9XI01.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. 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.
TIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiPDI11_ARATH
AccessioniPrimary (citable) accession number: Q9XI01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: February 4, 2015
This is version 123 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.