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Q9SRG3

- PDI12_ARATH

UniProt

Q9SRG3 - PDI12_ARATH

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Protein

Protein disulfide isomerase-like 1-2

Gene

PDIL1-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581NucleophileBy similarity
Sitei59 – 591Contributes to redox potential valueBy similarity
Sitei60 – 601Contributes to redox potential valueBy similarity
Active sitei61 – 611NucleophileBy similarity
Sitei126 – 1261Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei402 – 4021NucleophileBy similarity
Sitei403 – 4031Contributes to redox potential valueBy similarity
Sitei404 – 4041Contributes to redox potential valueBy similarity
Active sitei405 – 4051NucleophileBy similarity
Sitei466 – 4661Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: TAIR

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. photoinhibition Source: TAIR
  3. response to cadmium ion Source: TAIR
  4. response to endoplasmic reticulum stress Source: TAIR
  5. response to high light intensity Source: TAIR
  6. response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciARA:AT1G77510-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide isomerase-like 1-2 (EC:5.3.4.1)
Short name:
AtPDIL1-2
Alternative name(s):
Protein disulfide-isomerase 2
Short name:
PDI 2
Protein disulfide-isomerase 6
Short name:
AtPDI6
Gene namesi
Name:PDIL1-2
Synonyms:PDI6
Ordered Locus Names:At1g77510
ORF Names:T5M16.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G77510.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: TAIR
  3. endoplasmic reticulum Source: TAIR
  4. Golgi apparatus Source: TAIR
  5. plasma membrane Source: TAIR
  6. vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 508484Protein disulfide isomerase-like 1-2PRO_0000034206Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi58 ↔ 61Redox-activePROSITE-ProRule annotation
Glycosylationi273 – 2731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi402 ↔ 405Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9SRG3.
PRIDEiQ9SRG3.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

By chemically-induced ER stress response.1 Publication

Gene expression databases

ExpressionAtlasiQ9SRG3. baseline and differential.
GenevestigatoriQ9SRG3.

Structurei

3D structure databases

ProteinModelPortaliQ9SRG3.
SMRiQ9SRG3. Positions 29-483.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 140116Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini336 – 480145Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi505 – 5084Prevents 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.
InParanoidiQ9SRG3.
KOiK09580.
OMAiSHGEEST.
PhylomeDBiQ9SRG3.

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.

Q9SRG3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFKGFACFS ILLLLSLFVS SIRSEETKEF VLTLDHSNFT ETISKHDFIV
60 70 80 90 100
VEFYAPWCGH CQKLAPEYEK AASELSSHNP PLALAKIDAS EEANKEFANE
110 120 130 140 150
YKIQGFPTLK ILRNGGKSVQ DYNGPREAEG IVTYLKKQSG PASVEIKSAD
160 170 180 190 200
SATEVVGEKN VVAVGVFPKL SGDEFDSFMA LAEKLRADYD FAHTLDAKFL
210 220 230 240 250
PRGESVEGPA VRLFKPFDEL FVDSKDFNGE ALEKFVKESS IPLVTVFDSD
260 270 280 290 300
PNNHPYVAKF FESPATKAMM FVNFTGATAE ALKSKYREVA TSNKDQSLAF
310 320 330 340 350
LVGDAESSQG AFQYFGLEES QVPLIIIQTP DNKKYLKVNV EVDQIESWFK
360 370 380 390 400
DFQDGKVAVH KKSQPIPAEN NEPVKVVVAE SLDDIVFKSG KNVLIEFYAP
410 420 430 440 450
WCGHCQKLAP ILDEVALSFQ NDPSVIIAKL DATANDIPSD TFDVKGFPTI
460 470 480 490 500
YFRSASGNVV VYEGDRTKED FINFVEKNSE KKPTSHGEES TKSEEPKKTE

ETAAKDEL
Length:508
Mass (Da):56,365
Last modified:May 1, 2000 - v1
Checksum:iB6300A31DFD2AB62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010704 Genomic DNA. Translation: AAG51673.1.
CP002684 Genomic DNA. Translation: AEE35987.1.
AK226862 mRNA. Translation: BAE98951.1.
PIRiE96804.
RefSeqiNP_177875.1. NM_106400.2.
UniGeneiAt.17801.

Genome annotation databases

EnsemblPlantsiAT1G77510.1; AT1G77510.1; AT1G77510.
GeneIDi844087.
KEGGiath:AT1G77510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010704 Genomic DNA. Translation: AAG51673.1 .
CP002684 Genomic DNA. Translation: AEE35987.1 .
AK226862 mRNA. Translation: BAE98951.1 .
PIRi E96804.
RefSeqi NP_177875.1. NM_106400.2.
UniGenei At.17801.

3D structure databases

ProteinModelPortali Q9SRG3.
SMRi Q9SRG3. Positions 29-483.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q9SRG3.
PRIDEi Q9SRG3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G77510.1 ; AT1G77510.1 ; AT1G77510 .
GeneIDi 844087.
KEGGi ath:AT1G77510.

Organism-specific databases

TAIRi AT1G77510.

Phylogenomic databases

eggNOGi COG0526.
HOGENOMi HOG000162459.
InParanoidi Q9SRG3.
KOi K09580.
OMAi SHGEEST.
PhylomeDBi Q9SRG3.

Enzyme and pathway databases

BioCyci ARA:AT1G77510-MONOMER.

Miscellaneous databases

PROi Q9SRG3.

Gene expression databases

ExpressionAtlasi Q9SRG3. baseline and differential.
Genevestigatori Q9SRG3.

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

« Hide 'large scale' publications
  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. "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.
    , 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.

Entry informationi

Entry nameiPDI12_ARATH
AccessioniPrimary (citable) accession number: Q9SRG3
Secondary accession number(s): Q0WV97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 118 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