Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9XI01

- PDI11_ARATH

UniProt

Q9XI01 - PDI11_ARATH

Protein

Protein disulfide isomerase-like 1-1

Gene

PDIL1-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 binding Source: IntAct
    2. protein disulfide isomerase activity Source: TAIR

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. protein folding Source: GOC
    3. regulation of programmed cell death Source: TAIR
    4. response to endoplasmic reticulum stress Source: TAIR
    5. response to salt stress Source: TAIR
    6. response to zinc ion Source: TAIR
    7. seed development Source: TAIR

    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

    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

    ArrayExpressiQ9XI01.
    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.
    OMAiIYFAPRD.
    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

    MAMRGFTLFS ILVLSLCASS IRSEETETKE FVLTLDHTNF TDTINKHDFI    50
    VVEFYAPWCG HCKQLAPEYE KAASALSSNV PPVVLAKIDA SEETNREFAT 100
    QYEVQGFPTI KIFRNGGKAV QEYNGPREAE GIVTYLKKQS GPASAEIKSA 150
    DDASEVVSDK KVVVVGIFPK LSGSEFDSFM AIAEKLRSEL DFAHTSDAKL 200
    LPRGESSVTG PVVRLFKPFD EQFVDSKDFD GEALEKFVKE SSIPLITVFD 250
    KDPNNHPYVI KFFESTNTKA MLFINFTGEG AESLKSKYRE VATSNKGQGL 300
    SFLLGDAENS QGAFQYFGLE ESQVPLIIIQ TADDKKYLKT NVEVDQIESW 350
    VKDFKDGKIA PHKKSQPIPA ENNEPVKVVV SDSLDDIVLN SGKNVLLEFY 400
    APWCGHCQKL APILDEVAVS YQSDSSVVIA KLDATANDFP KDTFDVKGFP 450
    TIYFKSASGN VVVYEGDRTK EDFISFVDKN KDTVGEPKKE EETTEEVKDE 500
    L 501
    Length:501
    Mass (Da):55,602
    Last modified:November 1, 1999 - v1
    Checksum:iC27C564D38ECA6E8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC007727 Genomic DNA. Translation: AAD41430.1 .
    CP002684 Genomic DNA. Translation: AEE30151.1 .
    AY035096 mRNA. Translation: AAK59601.1 .
    AY063059 mRNA. Translation: AAL34233.1 .
    PIRi B86351.
    RefSeqi NP_173594.1. NM_102024.3. [Q9XI01-1 ]
    UniGenei At.24814.

    3D structure databases

    ProteinModelPortali Q9XI01.
    SMRi Q9XI01. Positions 25-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 24018. 4 interactions.
    IntActi Q9XI01. 5 interactions.

    2D gel databases

    SWISS-2DPAGE Q9XI01.

    Proteomic databases

    PaxDbi Q9XI01.
    PRIDEi Q9XI01.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G21750.1 ; AT1G21750.1 ; AT1G21750 . [Q9XI01-1 ]
    GeneIDi 838779.
    KEGGi ath:AT1G21750.

    Organism-specific databases

    TAIRi AT1G21750.

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000162459.
    InParanoidi Q9XI01.
    KOi K09580.
    OMAi IYFAPRD.
    PhylomeDBi Q9XI01.

    Enzyme and pathway databases

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

    Gene expression databases

    ArrayExpressi Q9XI01.
    Genevestigatori Q9XI01.

    Family and domain databases

    Gene3Di 3.40.30.10. 3 hits.
    InterProi IPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 4 hits.
    TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 2 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 120 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