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Q9SRG3 (PDI12_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. 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=AtPDIL1-2
EC=5.3.4.1
Alternative name(s):
Protein disulfide-isomerase 2
Short name=PDI 2
Protein disulfide-isomerase 6
Short name=AtPDI6
Gene names
Name:PDIL1-2
Synonyms:PDI6
Ordered Locus Names:At1g77510
ORF Names:T5M16.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length508 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 By similarity.

Catalytic activity

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

Subcellular location

Endoplasmic reticulum lumen Probable.

Tissue specificity

Widely expressed. Ref.5

Induction

By chemically-induced ER stress response. Ref.5

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 – 2424 Potential
Chain25 – 508484Protein disulfide isomerase-like 1-2
PRO_0000034206

Regions

Domain25 – 140116Thioredoxin 1
Domain336 – 480145Thioredoxin 2
Motif505 – 5084Prevents secretion from ER By similarity

Sites

Active site581Nucleophile By similarity
Active site611Nucleophile By similarity
Active site4021Nucleophile By similarity
Active site4051Nucleophile By similarity
Site591Contributes to redox potential value By similarity
Site601Contributes to redox potential value By similarity
Site1261Lowers pKa of C-terminal Cys of first active site By similarity
Site4031Contributes to redox potential value By similarity
Site4041Contributes to redox potential value By similarity
Site4661Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 61Redox-active By similarity
Disulfide bond402 ↔ 405Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SRG3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B6300A31DFD2AB62

FASTA50856,365
        10         20         30         40         50         60 
MAFKGFACFS ILLLLSLFVS SIRSEETKEF VLTLDHSNFT ETISKHDFIV VEFYAPWCGH 

        70         80         90        100        110        120 
CQKLAPEYEK AASELSSHNP PLALAKIDAS EEANKEFANE YKIQGFPTLK ILRNGGKSVQ 

       130        140        150        160        170        180 
DYNGPREAEG IVTYLKKQSG PASVEIKSAD SATEVVGEKN VVAVGVFPKL SGDEFDSFMA 

       190        200        210        220        230        240 
LAEKLRADYD FAHTLDAKFL PRGESVEGPA VRLFKPFDEL FVDSKDFNGE ALEKFVKESS 

       250        260        270        280        290        300 
IPLVTVFDSD PNNHPYVAKF FESPATKAMM FVNFTGATAE ALKSKYREVA TSNKDQSLAF 

       310        320        330        340        350        360 
LVGDAESSQG AFQYFGLEES QVPLIIIQTP DNKKYLKVNV EVDQIESWFK DFQDGKVAVH 

       370        380        390        400        410        420 
KKSQPIPAEN NEPVKVVVAE SLDDIVFKSG KNVLIEFYAP WCGHCQKLAP ILDEVALSFQ 

       430        440        450        460        470        480 
NDPSVIIAKL DATANDIPSD TFDVKGFPTI YFRSASGNVV VYEGDRTKED FINFVEKNSE 

       490        500 
KKPTSHGEES TKSEEPKKTE ETAAKDEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
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]"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
AC010704 Genomic DNA. Translation: AAG51673.1.
CP002684 Genomic DNA. Translation: AEE35987.1.
AK226862 mRNA. Translation: BAE98951.1.
PIRE96804.
RefSeqNP_177875.1. NM_106400.2.
UniGeneAt.17801.

3D structure databases

ProteinModelPortalQ9SRG3.
SMRQ9SRG3. Positions 25-508.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9SRG3.
PRIDEQ9SRG3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G77510.1; AT1G77510.1; AT1G77510.
GeneID844087.
KEGGath:AT1G77510.

Organism-specific databases

TAIRAT1G77510.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
InParanoidQ9SRG3.
KOK09580.
OMASHGEEST.
PhylomeDBQ9SRG3.
ProtClustDBCLSN2679750.

Enzyme and pathway databases

BioCycARA:AT1G77510-MONOMER.

Gene expression databases

ArrayExpressQ9SRG3.
GenevestigatorQ9SRG3.

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. SSF52833. 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...

Other

PROQ9SRG3.

Entry information

Entry namePDI12_ARATH
AccessionPrimary (citable) accession number: Q9SRG3
Secondary accession number(s): Q0WV97
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 113 of the entry and version 1 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names