Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7XRB5 (PDI12_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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 1-2

Short name=OsPDIL1-2
EC=5.3.4.1
Gene names
Name:PDIL1-2
Ordered Locus Names:Os04g0436300, LOC_Os04g35600
ORF Names:OSJNBa0006B20.4
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds. May play a role in storage protein biogenesis By similarity.

Catalytic activity

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

Subcellular location

Endoplasmic reticulum lumen Probable.

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 – 2323 Potential
Chain24 – 517494Protein disulfide isomerase-like 1-2
PRO_0000400029

Regions

Domain24 – 143120Thioredoxin 1
Domain357 – 484128Thioredoxin 2
Motif514 – 5174Prevents secretion from ER By similarity

Sites

Active site611Nucleophile By similarity
Active site641Nucleophile By similarity
Active site4071Nucleophile By similarity
Active site4101Nucleophile By similarity
Site621Contributes to redox potential value By similarity
Site631Contributes to redox potential value By similarity
Site1291Lowers pKa of C-terminal Cys of first active site By similarity
Site4081Contributes to redox potential value By similarity
Site4091Contributes to redox potential value By similarity
Site4701Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Disulfide bond61 ↔ 64Redox-active By similarity
Disulfide bond407 ↔ 410Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7XRB5 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: B7DB4CEEEE6AAD65

FASTA51757,335
        10         20         30         40         50         60 
MAVNLVLSFA LAILISSSPT AVGVDATEEL KEAVLTLDAG NFSEVVAKHP FIVVKFYAPW 

        70         80         90        100        110        120 
CGHCKQLAPE YEKAASILRK NELPVVLAKV DAYNERNKEL KDKYGVYSYP TIKIMKNGGS 

       130        140        150        160        170        180 
DVRGYGGPRE ADGIVEYLKR QVGPASLKLE SAEEAAHSVV DKGVILVGVF PEFAGMEYEN 

       190        200        210        220        230        240 
FMVVAEKMRA DYDFFHTSDA SILPRGDQSV KGPIVRLFKP FDELFVDSED FGKDALEKFI 

       250        260        270        280        290        300 
EVSGFPMVVT YDADPTNHKF LERYYSTPSS KAMLFVSFGD DRIESFKSQI HEAARKFSGN 

       310        320        330        340        350        360 
NISFLIGDVA DADRVFQYFG LRESDVPLLF VIASTGKYLN PTMDPDQIIP WLKQYIVEYG 

       370        380        390        400        410        420 
NLTPYVKSEP IPKVNDQPVK VVVADNIDDI VFNSGKNVLL EFYAPWCGHC RKFALILEEI 

       430        440        450        460        470        480 
AVSLQDDQDI VIAKMDGTVN DIPTDFTVEG YPTIYFYSSS GNLLSYDGAR TAEEIISFIN 

       490        500        510 
ENRGPKAGAA AAVDEKTQID AVEEEVTSSS EPVKDEL 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
Strain: cv. Nipponbare.
[2]"Sequence and analysis of rice chromosome 4."
Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., Zhang L. expand/collapse author list , Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y., Han B.
Nature 420:316-320(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"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.
[4]"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.
[5]"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
AY739308 mRNA. Translation: AAX14679.1.
AL606592 Genomic DNA. Translation: CAE02742.2.
AP008210 Genomic DNA. Translation: BAF14766.2.
RefSeqNP_001052852.2. NM_001059387.2.
UniGeneOs.53966.

3D structure databases

ProteinModelPortalQ7XRB5.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ7XRB5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4335906.
KEGGosa:4335906.

Organism-specific databases

GrameneQ7XRB5.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
KOK09580.
OMADYDFFHT.

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDI12_ORYSJ
AccessionPrimary (citable) accession number: Q7XRB5
Secondary accession number(s): Q0JD21
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: March 1, 2004
Last modified: June 11, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations