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Q53LQ0 (PDI11_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide isomerase-like 1-1
Short name=OsPDIL1-1
EC=5.3.4.1
Alternative name(s):
Endosperm storage protein 2
Short name=Protein ESP2
Gene names
Name:PDIL1-1
Ordered Locus Names:Os11g0199200, LOC_Os11g09280
ORF Names:OsJ_33281
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza ›

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.1 Ref.8

Catalytic activity

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

Subcellular location

Endoplasmic reticulum lumen Ref.1.

Developmental stage

Expressed in developing seeds from 3 to 9 days after anthesis. Ref.8

Disruption phenotype

Accumulation of large quantities of glutelin precursor (proglutelin) in the endosperm. Ref.1 Ref.8

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 512487Protein disulfide isomerase-like 1-1
PRO_0000400028

Regions

Domain32 – 151120Thioredoxin 1
Domain372 – 491120Thioredoxin 2
Motif509 – 5124Prevents secretion from ER By similarity

Sites

Active site691Nucleophile By similarity
Active site721Nucleophile By similarity
Active site4141Nucleophile By similarity
Active site4171Nucleophile By similarity
Site701Contributes to redox potential value By similarity
Site711Contributes to redox potential value By similarity
Site1371Lowers pKa of C-terminal Cys of first active site By similarity
Site4151Contributes to redox potential value By similarity
Site4161Contributes to redox potential value By similarity
Site4771Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation2851N-linked (GlcNAc...) Potential
Disulfide bond69 ↔ 72Redox-active By similarity
Disulfide bond414 ↔ 417Redox-active By similarity

Experimental info

Sequence conflict4351K → E in AAX85991. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q53LQ0 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: 60CA68E115728496

FASTA51256,855
        10         20         30         40         50         60 
MAISKAWISL LLALAVVLSA PAARAEEAAA AEEGGDAAAE AVLTLDADGF DEAVAKHPFM 

        70         80         90        100        110        120 
VVEFYAPWCG HCKKLAPEYE KAAQELSKHD PPIVLAKVDA NDEKNKPLAT KYEIQGFPTL 

       130        140        150        160        170        180 
KIFRNQGKNI QEYKGPREAE GIVEYLKKQV GPASKEIKSP EDATNLIDDK KIYIVGIFSE 

       190        200        210        220        230        240 
LSGTEYTNFI EVAEKLRSDY DFGHTLHANH LPRGDAAVER PLVRLFKPFD ELVVDSKDFD 

       250        260        270        280        290        300 
VTALEKFIDA SSTPKVVTFD KNPDNHPYLL KFFQSSAAKA MLFLNFSTGP FESFKSVYYG 

       310        320        330        340        350        360 
AAEEFKDKEI KFLIGDIEAS QGAFQYFGLR EDQVPLIIIQ DGESKKFLKA HVEPDQIVSW 

       370        380        390        400        410        420 
LKEYFDGKLS PFRKSEPIPE VNDEPVKVVV ADNVHDFVFK SGKNVLVEFY APWCGHCKKL 

       430        440        450        460        470        480 
APILDEAATT LKSDKDVVIA KMDATANDVP SEFDVQGYPT LYFVTPSGKM VPYESGRTAD 

       490        500        510 
EIVDFIKKNK ETAGQAKEKA ESAPAEPLKD EL

« Hide

References

« Hide 'large scale' references
[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]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
RefSeqNP_001067436.1. NM_001073968.1.
UniGeneOs.10985.

3D structure databases

ProteinModelPortalQ53LQ0.
ModBaseSearch...

Proteomic databases

PaxDbQ53LQ0.
PRIDEQ53LQ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsLOC_Os11g09280.1; LOC_Os11g09280.1; LOC_Os11g09280.
LOC_Os11g09280.2; LOC_Os11g09280.2; LOC_Os11g09280.
GeneID4350002.
KEGGdosa:Os11t0199200-01.
osa:4350002.

Organism-specific databases

GrameneQ53LQ0.

Phylogenomic databases

eggNOGCOG0526.
KOK09580.
OMAPEVNDEP.
ProtClustDBCLSN2679750.

Gene expression databases

ArrayExpressQ53LQ0.

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. Thiordxn-like_fd. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDI11_ORYSJ
AccessionPrimary (citable) accession number: Q53LQ0
Secondary accession number(s): Q52PJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: May 24, 2005
Last modified: April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents