Protein disulfide-isomerase like 2-1 precursor - Arabidopsis thaliana (Mouse-ear cress)

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O22263 (PDI21_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase like 2-1
Short name=AtPDIL2-1
EC=5.3.4.1

Alternative name(s):
P5
Protein MATERNAL EFFECT EMBRYO ARREST 30
Protein UNFERTILIZED EMBRYO SAC 5
Protein disulfide isomerase 11
Short name=AtPDI11
Protein disulfide-isomerase A6
Protein disulfide-isomerase like 4-1
Short name=AtPDIL4-1

Gene names

Name:	PDIL2-1
Synonyms:	MEE30, PDI11, PDIL4-1, UNE5
Ordered Locus Names:	At2g47470
ORF Names:	T30B22.23

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein disulfide isomerase that may be required for proper pollen development, ovule fertilization and embryo development. Ref.8
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subcellular location	Endoplasmic reticulum Ref.8.
Tissue specificity	Widely expressed. Ref.7 Ref.8
Developmental stage	During flower development, expressed at early stage in inner and outer integuments, and nucellar cells. Later, expressed in the integument cells but not in the embryo sac. In the mature ovule, highly expressed in the micropylar region. After fertilization, expressed in the seed integuments but not in the embryo. Ref.8
Induction	By chemically-induced ER stress response. Ref.7
Disruption phenotype	Smaller siliques and reduced seed set. Disrupted pollen tube guidance. Ref.8
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro double fertilization forming a zygote and endosperm Inferred from mutant phenotype. Source: TAIR embryo development ending in seed dormancy Inferred from mutant phenotype. Source: TAIR embryo sac development Inferred from mutant phenotype Ref.8. Source: TAIR glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro pollen tube development Inferred from mutant phenotype. Source: TAIR response to cadmium ion Inferred from expression pattern. Source: TAIR response to endoplasmic reticulum stress Inferred from expression pattern Ref.7. Source: TAIR
Cellular component	endoplasmic reticulum Inferred from direct assay Ref.8. Source: TAIR plant-type cell wall Inferred from direct assay. Source: TAIR vacuolar membrane Inferred from direct assay. Source: TAIR
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from electronic annotation. Source: EC protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select] Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O22263-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Potential

Chain

23 – 361

339

Protein disulfide-isomerase like 2-1

PRO_0000034242

Regions

Domain

23 – 131

109

Thioredoxin 1

Domain

132 – 250

119

Thioredoxin 2

Sites

Active site

Nucleophile By similarity

Active site

Nucleophile By similarity

Active site

171

Nucleophile By similarity

Active site

174

Nucleophile By similarity

Site

Contributes to redox potential value By similarity

Site

Contributes to redox potential value By similarity

Site

117

Lowers pKa of C-terminal Cys of first active site By similarity

Site

172

Contributes to redox potential value By similarity

Site

173

Contributes to redox potential value By similarity

Site

236

Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond

52 ↔ 55

Redox-active By similarity

Disulfide bond

171 ↔ 174

Redox-active By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9F4C7A07B0209DB5
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FASTA

361

39,497

        10         20         30         40         50         60 
MAKSQIWFGF ALLALLLVSA VADDVVVLTD DSFEKEVGKD KGALVEFYAP WCGHCKKLAP 

        70         80         90        100        110        120 
EYEKLGASFK KAKSVLIAKV DCDEQKSVCT KYGVSGYPTI QWFPKGSLEP QKYEGPRNAE 

       130        140        150        160        170        180 
ALAEYVNKEG GTNVKLAAVP QNVVVLTPDN FDEIVLDQNK DVLVEFYAPW CGHCKSLAPT 

       190        200        210        220        230        240 
YEKVATVFKQ EEGVVIANLD ADAHKALGEK YGVSGFPTLK FFPKDNKAGH DYDGGRDLDD 

       250        260        270        280        290        300 
FVSFINEKSG TSRDSKGQLT SKAGIVESLD ALVKELVAAS EDEKKAVLSR IEEEASTLKG 

       310        320        330        340        350        360 
STTRYGKLYL KLAKSYIEKG SDYASKETER LGRVLGKSIS PVKADELTLK RNILTTFVAS 


S

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells." Stracke R., Palme K. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Arabidopsis thaliana mRNA for ERp72." Mahon P. Thesis (2000), Cambridge University, United Kingdom Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"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: 15684019] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[7]	"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: 18574595] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[8]	"Truncation of a protein disulfide isomerase, PDIL2-1, delays embryo sac maturation and disrupts pollen tube guidance in Arabidopsis thaliana." Wang H., Boavida L.C., Ron M., McCormick S. Plant Cell 20:3300-3311(2008) [PubMed: 19050167] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[9]	"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: 20525253] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF083688 mRNA. Translation: AAN60247.1. AJ271470 mRNA. Translation: CAC81060.1. AC002535 Genomic DNA. Translation: AAC62863.1. CP002685 Genomic DNA. Translation: AEC10845.1. AY074348 mRNA. Translation: AAL67044.1. AY091388 mRNA. Translation: AAM14327.1.
IPI	IPI00539517.
PIR	T00437.
RefSeq	NP_182269.1. NM_130315.4.
UniGene	At.24396. At.66351.
3D structure databases
ProteinModelPortal	O22263.
SMR	O22263. Positions 19-360.
ModBase	Search...
Protein-protein interaction databases
STRING	O22263.
2D gel databases
SWISS-2DPAGE	O22263.
Proteomic databases
PRIDE	O22263.
ProMEX	O22263.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G47470.1; AT2G47470.1; AT2G47470.
GeneID	819360.
GenomeReviews	Gene locus AT2G47470 in contig CT485783_GR.
KEGG	ath:AT2G47470.
Organism-specific databases
TAIR	At2g47470.
Phylogenomic databases
HOGENOM	HBG523089.
InParanoid	O22263.
OMA	FFPKGST.
PhylomeDB	O22263.
ProtClustDB	CLSN2683612.
Gene expression databases
ArrayExpress	O22263.
Genevestigator	O22263.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR011679. ER_p29_C. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:1.20.1150.12. ERp29_C_type. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
KO	K09584.
Pfam	PF07749. ERp29. 1 hit. PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF47933. ERP29_C. 1 hit. SSF52833. Thiordxn-like_fd. 2 hits.
TIGRFAMs	TIGR01126. Pdi_dom. 2 hits.
PROSITE	PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDI21_ARATH

Accession

Primary (citable) accession number: O22263
Secondary accession number(s): Q546R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 1, 1998
Last modified:	November 16, 2011
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents