Q9XI01 (PDI11_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide isomerase-like 1-1
Short name=AtPDIL1-1
EC=5.3.4.1

Alternative name(s):
Protein disulfide-isomerase 1
Short name=PDI 1
Protein disulfide-isomerase 5
Short name=AtPDI5

Gene names

Name:	PDIL1-1
Synonyms:	PDI5
Ordered Locus Names:	At1g21750
ORF Names:	F8K7.19

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	501 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 associates with RD21A protease for trafficking from the ER through the Golgi to lytic and protein storage vacuoles of endothelial cells in developing seeds. Regulates the timing of programmed cell death (PCD) of the endothelial cells by chaperoning and inhibiting cysteine proteases during their trafficking to vacuoles. Ref.6
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Interacts with RD21A, At3g19390, At5g43060. Ref.6
Subcellular location	Endoplasmic reticulum lumen. Vacuole. Note: Found in protein storage vacuoles and lytic vacuoles in endothelial cells of developing seeds. Ref.6
Tissue specificity	Highly expressed in flowers, stems and immature seeds, and at lower levels in leaves and siliques (at protein level). Ref.5 Ref.6
Developmental stage	During embryo development, expressed exclusively in endothelial cells from the pre-embryo up to the heart stage. Expression disappears when the endothelial cells undergo PCD in the early-bent cotyledon stage (at protein level).
Induction	By chemically-induced ER stress response. Ref.5
Disruption phenotype	Reduced seed set. Ref.6
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Vacuole
Coding sequence diversity	Alternative splicing
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro embryo development Inferred from mutant phenotype Ref.6. Source: TAIR glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro regulation of programmed cell death Inferred from mutant phenotype Ref.6. Source: TAIR response to endoplasmic reticulum stress Inferred from expression pattern Ref.5. Source: TAIR response to salt stress Inferred from expression pattern PubMed 17916636. Source: TAIR response to zinc ion Inferred from expression pattern PubMed 19880396. Source: TAIR seed development Inferred from mutant phenotype Ref.6. Source: TAIR
Cellular_component	chloroplast Inferred from direct assay PubMed 15028209. Source: TAIR endoplasmic reticulum Inferred from direct assay PubMed 16618929PubMed 22923678. Source: TAIR endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell lytic vacuole within protein storage vacuole Inferred from direct assay Ref.6. Source: TAIR membrane Inferred from direct assay PubMed 17432890. Source: TAIR plant-type cell wall Inferred from direct assay PubMed 17526915. Source: TAIR thylakoid Inferred from direct assay PubMed 11826309. Source: TAIR
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from sequence or structural similarity Ref.5. Source: TAIR protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
At5g43060/MMG4.7	Q9FMH8	3	EBI-449394,EBI-1993115
RD21A	P43297	4	EBI-449394,EBI-1993101

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: Q9XI01-1)

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 – 23	23	Potential
	Chain	24 – 501	478	Protein disulfide isomerase-like 1-1		PRO_0000034205
Regions
	Domain	24 – 141	118	Thioredoxin 1
	Domain	354 – 482	129	Thioredoxin 2
	Motif	498 – 501	4	Prevents secretion from ER By similarity
Sites
	Active site	59	1	Nucleophile By similarity
	Active site	62	1	Nucleophile By similarity
	Active site	404	1	Nucleophile By similarity
	Active site	407	1	Nucleophile By similarity
	Site	60	1	Contributes to redox potential value By similarity
	Site	61	1	Contributes to redox potential value By similarity
	Site	127	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	405	1	Contributes to redox potential value By similarity
	Site	406	1	Contributes to redox potential value By similarity
	Site	468	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Glycosylation	39	1	N-linked (GlcNAc...) Potential
	Glycosylation	275	1	N-linked (GlcNAc...) Potential
	Disulfide bond	59 ↔ 62		Redox-active By similarity
	Disulfide bond	404 ↔ 407		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: C27C564D38ECA6E8	FASTA	501	55,602
	10 20 30 40 50 60 MAMRGFTLFS ILVLSLCASS IRSEETETKE FVLTLDHTNF TDTINKHDFI VVEFYAPWCG 70 80 90 100 110 120 HCKQLAPEYE KAASALSSNV PPVVLAKIDA SEETNREFAT QYEVQGFPTI KIFRNGGKAV 130 140 150 160 170 180 QEYNGPREAE GIVTYLKKQS GPASAEIKSA DDASEVVSDK KVVVVGIFPK LSGSEFDSFM 190 200 210 220 230 240 AIAEKLRSEL DFAHTSDAKL LPRGESSVTG PVVRLFKPFD EQFVDSKDFD GEALEKFVKE 250 260 270 280 290 300 SSIPLITVFD KDPNNHPYVI KFFESTNTKA MLFINFTGEG AESLKSKYRE VATSNKGQGL 310 320 330 340 350 360 SFLLGDAENS QGAFQYFGLE ESQVPLIIIQ TADDKKYLKT NVEVDQIESW VKDFKDGKIA 370 380 390 400 410 420 PHKKSQPIPA ENNEPVKVVV SDSLDDIVLN SGKNVLLEFY APWCGHCQKL APILDEVAVS 430 440 450 460 470 480 YQSDSSVVIA KLDATANDFP KDTFDVKGFP TIYFKSASGN VVVYEGDRTK EDFISFVDKN 490 500 KDTVGEPKKE EETTEEVKDE L

References

	« Hide 'large scale' referencesShow '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. , 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]	"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. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] 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]	"Arabidopsis protein disulfide isomerase-5 inhibits cysteine proteases during trafficking to vacuoles before programmed cell death of the endothelium in developing seeds." Andeme Ondzighi C., Christopher D.A., Cho E.J., Chang S.C., Staehelin L.A. Plant Cell 20:2205-2220(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RD21A; AT3G19390 AND AT5G43060, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[7]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC007727 Genomic DNA. Translation: AAD41430.1. CP002684 Genomic DNA. Translation: AEE30151.1. AY035096 mRNA. Translation: AAK59601.1. AY063059 mRNA. Translation: AAL34233.1.
IPI	IPI00522163.
PIR	B86351.
RefSeq	NP_173594.1. NM_102024.3.
UniGene	At.24814.
3D structure databases
ProteinModelPortal	Q9XI01.
SMR	Q9XI01. Positions 25-480.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9XI01. 5 interactions.
2D gel databases
SWISS-2DPAGE	Q9XI01.
Proteomic databases
PaxDb	Q9XI01.
PRIDE	Q9XI01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G21750.1; AT1G21750.1; AT1G21750.
GeneID	838779.
KEGG	ath:AT1G21750.
Organism-specific databases
TAIR	At1g21750.
Phylogenomic databases
eggNOG	COG0526.
HOGENOM	HOG000162459.
InParanoid	Q9XI01.
KO	K09580.
OMA	KFMAKHG.
PhylomeDB	Q9XI01.
ProtClustDB	CLSN2679750.
Gene expression databases
ArrayExpress	Q9XI01.
Genevestigator	Q9XI01.
Family and domain databases
Gene3D	3.40.30.10. 3 hits.
InterPro	IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 4 hits.
TIGRFAMs	TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. pdi_dom. 2 hits.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDI11_ARATH

Accession

Primary (citable) accession number: Q9XI01

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program