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Protein

Protein disulfide isomerase-like 1-2

Gene

PDIL1-2

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score: Annotation score: 3 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. May play a role in storage protein biogenesis (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei61NucleophileBy similarity1
Sitei62Contributes to redox potential valueBy similarity1
Sitei63Contributes to redox potential valueBy similarity1
Active sitei64NucleophileBy similarity1
Sitei129Lowers pKa of C-terminal Cys of first active siteBy similarity1
Active sitei407NucleophileBy similarity1
Sitei408Contributes to redox potential valueBy similarity1
Sitei409Contributes to redox potential valueBy similarity1
Active sitei410NucleophileBy similarity1
Sitei470Lowers pKa of C-terminal Cys of second active siteBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide isomerase-like 1-2 (EC:5.3.4.1)
Short name:
OsPDIL1-2
Gene namesi
Name:PDIL1-2
Ordered Locus Names:Os04g0436300, LOC_Os04g35600
ORF Names:OSJNBa0006B20.4
OrganismiOryza sativa subsp. japonica (Rice)
Taxonomic identifieri39947 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
Proteomesi
  • UP000059680 Componenti: Chromosome 4

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000040002924 – 517Protein disulfide isomerase-like 1-2Add BLAST494

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi41N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi61 ↔ 64Redox-activePROSITE-ProRule annotation
Glycosylationi301N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi407 ↔ 410Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ7XRB5.
PRIDEiQ7XRB5.

Expressioni

Gene expression databases

GenevisibleiQ7XRB5. OS.

Interactioni

Protein-protein interaction databases

STRINGi39947.LOC_Os04g35600.1.

Structurei

3D structure databases

ProteinModelPortaliQ7XRB5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 143Thioredoxin 1PROSITE-ProRule annotationAdd BLAST120
Domaini357 – 484Thioredoxin 2PROSITE-ProRule annotationAdd BLAST128

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi514 – 517Prevents secretion from ERPROSITE-ProRule annotation4

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

eggNOGiKOG0190. Eukaryota.
COG0526. LUCA.
HOGENOMiHOG000162459.
InParanoidiQ7XRB5.

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. 1 hit.
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.

Q7XRB5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVNLVLSFA LAILISSSPT AVGVDATEEL KEAVLTLDAG NFSEVVAKHP
60 70 80 90 100
FIVVKFYAPW CGHCKQLAPE YEKAASILRK NELPVVLAKV DAYNERNKEL
110 120 130 140 150
KDKYGVYSYP TIKIMKNGGS DVRGYGGPRE ADGIVEYLKR QVGPASLKLE
160 170 180 190 200
SAEEAAHSVV DKGVILVGVF PEFAGMEYEN FMVVAEKMRA DYDFFHTSDA
210 220 230 240 250
SILPRGDQSV KGPIVRLFKP FDELFVDSED FGKDALEKFI EVSGFPMVVT
260 270 280 290 300
YDADPTNHKF LERYYSTPSS KAMLFVSFGD DRIESFKSQI HEAARKFSGN
310 320 330 340 350
NISFLIGDVA DADRVFQYFG LRESDVPLLF VIASTGKYLN PTMDPDQIIP
360 370 380 390 400
WLKQYIVEYG NLTPYVKSEP IPKVNDQPVK VVVADNIDDI VFNSGKNVLL
410 420 430 440 450
EFYAPWCGHC RKFALILEEI AVSLQDDQDI VIAKMDGTVN DIPTDFTVEG
460 470 480 490 500
YPTIYFYSSS GNLLSYDGAR TAEEIISFIN ENRGPKAGAA AAVDEKTQID
510
AVEEEVTSSS EPVKDEL
Length:517
Mass (Da):57,335
Last modified:March 1, 2004 - v2
Checksum:iB7DB4CEEEE6AAD65
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY739308 mRNA. Translation: AAX14679.1.
AL606592 Genomic DNA. Translation: CAE02742.2.
AP008210 Genomic DNA. Translation: BAF14766.2.
AP014960 Genomic DNA. No translation available.
UniGeneiOs.53966.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY739308 mRNA. Translation: AAX14679.1.
AL606592 Genomic DNA. Translation: CAE02742.2.
AP008210 Genomic DNA. Translation: BAF14766.2.
AP014960 Genomic DNA. No translation available.
UniGeneiOs.53966.

3D structure databases

ProteinModelPortaliQ7XRB5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os04g35600.1.

Proteomic databases

PaxDbiQ7XRB5.
PRIDEiQ7XRB5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0190. Eukaryota.
COG0526. LUCA.
HOGENOMiHOG000162459.
InParanoidiQ7XRB5.

Gene expression databases

GenevisibleiQ7XRB5. OS.

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. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDI12_ORYSJ
AccessioniPrimary (citable) accession number: Q7XRB5
Secondary accession number(s): Q0JD21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: March 1, 2004
Last modified: September 7, 2016
This is version 105 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.