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Protein

Protein disulfide isomerase-like 1-5

Gene

PDIL1-5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei106 – 1061NucleophileBy similarity
Active sitei447 – 4471NucleophileBy similarity
Active sitei450 – 4501NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciARA:AT1G52260-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide isomerase-like 1-5 (EC:5.3.4.1)
Short name:
AtPDIL1-5
Alternative name(s):
Protein disulfide isomerase 3
Short name:
AtPDI3
Protein disulfide isomerase-like 3-1
Short name:
AtPDIL3-1
Gene namesi
Name:PDIL1-5
Synonyms:PDI3, PDIL3-1
Ordered Locus Names:At1g52260
ORF Names:F19K6.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G52260.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: TAIR
  • endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 537508Protein disulfide isomerase-like 1-5PRO_0000400020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi447 ↔ 450Redox-activePROSITE-ProRule annotation
Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiA3KPF5.
PRIDEiA3KPF5.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

GenevestigatoriA3KPF5.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G52260.1-P.

Structurei

3D structure databases

ProteinModelPortaliA3KPF5.
SMRiA3KPF5. Positions 61-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 184127Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini380 – 526147Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi534 – 5374Prevents 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.
HOGENOMiHOG000241706.
InParanoidiA3KPF5.
KOiK09580.
OMAiSANEHTK.
PhylomeDBiA3KPF5.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A3KPF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLIPKPISK VSTFTFILLI LLSFTIIIAY SSPDSNVESN EPGFDSDLDQ
60 70 80 90 100
LLAVDEQLQE DRPEQQSEAE TVSKAQRIVL ELNGDYTKRV IDGNEFVMVL
110 120 130 140 150
GYAPWCARSA ELMPRFAEAA TALKEIGSSV LMAKIDGDRY SKIASELEIK
160 170 180 190 200
GFPTLLLFVN GTSLTYNGGS SAEDIVIWVQ KKTGAPIITL NTVDEAPRFL
210 220 230 240 250
DKYHTFVLGL FEKFEGSEHN EFVKAAKSDD EIQFIETRDS DVAKLLFPDL
260 270 280 290 300
KSNNVFIGLV KPEAERYTVY DGSYKMEKIL EFLGSNKFPL FTKLTETNTV
310 320 330 340 350
WVYSSPVKLQ VMLFSKADDF QKLAQPLEDI ARKFKSKLMF IYVDITNENL
360 370 380 390 400
AMPFLILFGI EAGNKTVVAA FDNNLNSKYL LESDPSPNSI EEFCSGLAHG
410 420 430 440 450
TVSRYYRSEP VPDNENASIV TVVGKTFDGL VLNSRENVLL EVHTPWCVNC
460 470 480 490 500
EALSKQIEKL AKHFKGFENL VFARIDASAN EHTKLQVDDK YPIILLYKSG
510 520 530
EKEKPLKLST KLSAKDIAVF INEELLKPKN GSAKDEL
Length:537
Mass (Da):60,158
Last modified:April 3, 2007 - v1
Checksum:i6380842BE6CFB1C4
GO

Sequence cautioni

The sequence AAG51554.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC037424 Genomic DNA. Translation: AAG51554.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32775.1.
BT030322 mRNA. Translation: ABO09885.1.
PIRiF96562.
RefSeqiNP_175636.2. NM_104105.2.
UniGeneiAt.49972.

Genome annotation databases

EnsemblPlantsiAT1G52260.1; AT1G52260.1; AT1G52260.
GeneIDi841656.
KEGGiath:AT1G52260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC037424 Genomic DNA. Translation: AAG51554.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32775.1.
BT030322 mRNA. Translation: ABO09885.1.
PIRiF96562.
RefSeqiNP_175636.2. NM_104105.2.
UniGeneiAt.49972.

3D structure databases

ProteinModelPortaliA3KPF5.
SMRiA3KPF5. Positions 61-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G52260.1-P.

Proteomic databases

PaxDbiA3KPF5.
PRIDEiA3KPF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G52260.1; AT1G52260.1; AT1G52260.
GeneIDi841656.
KEGGiath:AT1G52260.

Organism-specific databases

TAIRiAT1G52260.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000241706.
InParanoidiA3KPF5.
KOiK09580.
OMAiSANEHTK.
PhylomeDBiA3KPF5.

Enzyme and pathway databases

BioCyciARA:AT1G52260-MONOMER.

Miscellaneous databases

PROiA3KPF5.

Gene expression databases

GenevestigatoriA3KPF5.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

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. "Arabidopsis ORF clones."
    Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.
    Submitted (FEB-2007) 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.
  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 nameiPDI15_ARATH
AccessioniPrimary (citable) accession number: A3KPF5
Secondary accession number(s): Q9C818
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: April 3, 2007
Last modified: April 29, 2015
This is version 61 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

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 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.