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Q53LQ0

- PDI11_ORYSJ

UniProt

Q53LQ0 - PDI11_ORYSJ

Protein

Protein disulfide isomerase-like 1-1

Gene

PDIL1-1

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    Probable protein disulfide isomerase that plays an essential role in the segregation of proglutelin and prolamin polypeptides within the ER lumen of endosperm. Required to retain proglutelin in the cisternal ER lumen until ER export and, thereby, indirectly prevents heterotypic interactions with prolamin polypeptides.2 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei69 – 691NucleophileBy similarity
    Sitei70 – 701Contributes to redox potential valueBy similarity
    Sitei71 – 711Contributes to redox potential valueBy similarity
    Active sitei72 – 721NucleophileBy similarity
    Sitei137 – 1371Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei414 – 4141NucleophileBy similarity
    Sitei415 – 4151Contributes to redox potential valueBy similarity
    Sitei416 – 4161Contributes to redox potential valueBy similarity
    Active sitei417 – 4171NucleophileBy similarity
    Sitei477 – 4771Lowers pKa of C-terminal Cys of second active siteBy similarity

    GO - Molecular functioni

    1. protein disulfide isomerase activity Source: RefGenome

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. embryo development Source: EnsemblPlants/Gramene
    3. protein folding in endoplasmic reticulum Source: UniProtKB
    4. regulation of programmed cell death Source: EnsemblPlants/Gramene
    5. response to cadmium ion Source: EnsemblPlants/Gramene
    6. response to endoplasmic reticulum stress Source: RefGenome
    7. response to salt stress Source: EnsemblPlants/Gramene
    8. response to zinc ion Source: EnsemblPlants/Gramene
    9. seed development Source: EnsemblPlants/Gramene

    Keywords - Molecular functioni

    Isomerase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide isomerase-like 1-1 (EC:5.3.4.1)
    Short name:
    OsPDIL1-1
    Alternative name(s):
    Endosperm storage protein 2
    Short name:
    Protein ESP2
    Gene namesi
    Name:PDIL1-1
    Ordered Locus Names:Os11g0199200, LOC_Os11g09280
    ORF Names:OsJ_33281
    OrganismiOryza sativa subsp. japonica (Rice)
    Taxonomic identifieri39947 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza
    ProteomesiUP000000763: Chromosome 11

    Organism-specific databases

    GrameneiQ53LQ0.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. chloroplast Source: EnsemblPlants/Gramene
    2. endoplasmic reticulum lumen Source: UniProtKB
    3. Golgi apparatus Source: EnsemblPlants/Gramene
    4. lytic vacuole within protein storage vacuole Source: EnsemblPlants/Gramene
    5. plant-type cell wall Source: EnsemblPlants/Gramene
    6. plasma membrane Source: EnsemblPlants/Gramene
    7. thylakoid Source: EnsemblPlants/Gramene
    8. vacuolar membrane Source: EnsemblPlants/Gramene

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Disruption phenotypei

    Accumulation of large quantities of glutelin precursor (proglutelin) in the endosperm.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 512487Protein disulfide isomerase-like 1-1PRO_0000400028Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi69 ↔ 72Redox-activePROSITE-ProRule annotation
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi414 ↔ 417Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ53LQ0.
    PRIDEiQ53LQ0.

    Expressioni

    Developmental stagei

    Expressed in developing seeds from 3 to 9 days after anthesis.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ53LQ0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 151120Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini372 – 491120Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi509 – 5124Prevents 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.
    KOiK09580.
    OMAiPEANEEP.

    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.

    Q53LQ0-1 [UniParc]FASTAAdd to Basket

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    MAISKAWISL LLALAVVLSA PAARAEEAAA AEEGGDAAAE AVLTLDADGF    50
    DEAVAKHPFM VVEFYAPWCG HCKKLAPEYE KAAQELSKHD PPIVLAKVDA 100
    NDEKNKPLAT KYEIQGFPTL KIFRNQGKNI QEYKGPREAE GIVEYLKKQV 150
    GPASKEIKSP EDATNLIDDK KIYIVGIFSE LSGTEYTNFI EVAEKLRSDY 200
    DFGHTLHANH LPRGDAAVER PLVRLFKPFD ELVVDSKDFD VTALEKFIDA 250
    SSTPKVVTFD KNPDNHPYLL KFFQSSAAKA MLFLNFSTGP FESFKSVYYG 300
    AAEEFKDKEI KFLIGDIEAS QGAFQYFGLR EDQVPLIIIQ DGESKKFLKA 350
    HVEPDQIVSW LKEYFDGKLS PFRKSEPIPE VNDEPVKVVV ADNVHDFVFK 400
    SGKNVLVEFY APWCGHCKKL APILDEAATT LKSDKDVVIA KMDATANDVP 450
    SEFDVQGYPT LYFVTPSGKM VPYESGRTAD EIVDFIKKNK ETAGQAKEKA 500
    ESAPAEPLKD EL 512
    Length:512
    Mass (Da):56,855
    Last modified:May 24, 2005 - v1
    Checksum:i60CA68E115728496
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti435 – 4351K → E in AAX85991. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB373950 mRNA. Translation: BAG50157.1.
    AY987391 mRNA. Translation: AAX85991.1.
    AC139170 Genomic DNA. Translation: AAX96742.1.
    DP000010 Genomic DNA. Translation: ABA91939.1.
    AP008217 Genomic DNA. Translation: BAF27799.1.
    CM000148 Genomic DNA. Translation: EAZ17736.1.
    AK068268 mRNA. Translation: BAG90833.1.
    RefSeqiNP_001067436.1. NM_001073968.1.
    UniGeneiOs.10985.

    Genome annotation databases

    EnsemblPlantsiOS11T0199200-01; OS11T0199200-01; OS11G0199200.
    GeneIDi4350002.
    KEGGiosa:4350002.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB373950 mRNA. Translation: BAG50157.1 .
    AY987391 mRNA. Translation: AAX85991.1 .
    AC139170 Genomic DNA. Translation: AAX96742.1 .
    DP000010 Genomic DNA. Translation: ABA91939.1 .
    AP008217 Genomic DNA. Translation: BAF27799.1 .
    CM000148 Genomic DNA. Translation: EAZ17736.1 .
    AK068268 mRNA. Translation: BAG90833.1 .
    RefSeqi NP_001067436.1. NM_001073968.1.
    UniGenei Os.10985.

    3D structure databases

    ProteinModelPortali Q53LQ0.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q53LQ0.
    PRIDEi Q53LQ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi OS11T0199200-01 ; OS11T0199200-01 ; OS11G0199200 .
    GeneIDi 4350002.
    KEGGi osa:4350002.

    Organism-specific databases

    Gramenei Q53LQ0.

    Phylogenomic databases

    eggNOGi COG0526.
    KOi K09580.
    OMAi PEANEEP.

    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. "Protein disulfide isomerase like 1-1 participates in the maturation of proglutelin within the endoplasmic reticulum in rice endosperm."
      Satoh-Cruz M., Crofts A.J., Takemoto-Kuno Y., Sugino A., Washida H., Crofts N., Okita T.W., Ogawa M., Satoh H., Kumamaru T.
      Plant Cell Physiol. 51:1581-1593(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    2. "Cloning and characterization of the protein disulfide isomerase in rice."
      Wan J.M., Niu H.B., Zhai H.Q., Zhang X., Jiang L., Qin H.D.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications."
      The rice chromosomes 11 and 12 sequencing consortia
      BMC Biol. 3:20-20(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    5. "The rice annotation project database (RAP-DB): 2008 update."
      The rice annotation project (RAP)
      Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: cv. Nipponbare.
    6. "The genomes of Oryza sativa: a history of duplications."
      Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
      , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
      PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    7. "Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
      The rice full-length cDNA consortium
      Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Nipponbare.
    8. "The rice mutant esp2 greatly accumulates the glutelin precursor and deletes the protein disulfide isomerase."
      Takemoto Y., Coughlan S.J., Okita T.W., Satoh H., Ogawa M., Kumamaru T.
      Plant Physiol. 128:1212-1222(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    9. "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.
    10. "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_ORYSJ
    AccessioniPrimary (citable) accession number: Q53LQ0
    Secondary accession number(s): Q52PJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2010
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 91 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. Oryza sativa (rice)
      Index of Oryza sativa entries and their corresponding gene designations
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3