Reviewed, UniProtKB/Swiss-Prot Q9XI01 (PDI1_ARATH)

Names and origin

Protein names

Recommended name:
    Probable protein disulfide-isomerase 1
      Short name=PDI 1
    EC=5.3.4.1

Gene names

Ordered Locus Names:	At1g21750
ORF Names:	F8K7.19

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › 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	Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer By similarity.
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subcellular location	Endoplasmic reticulum lumen Potential.
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 Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro embryonic development Inferred from mutant phenotype. Source: TAIR regulation of programmed cell death Inferred from mutant phenotype. Source: TAIR response to endoplasmic reticulum stress Inferred from expression pattern. Source: TAIR response to salt stress Inferred from expression pattern. Source: TAIR seed development Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast Inferred from direct assay. Source: TAIR endoplasmic reticulum Inferred from direct assay. Source: TAIR endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell lytic vacuole within protein storage vacuole Inferred from direct assay. Source: TAIR membrane Inferred from direct assay. Source: TAIR plant-type cell wall Inferred from direct assay. Source: TAIR thylakoid Inferred from direct assay. Source: TAIR
Molecular function	protein binding Inferred from physical interaction. Source: IntAct protein disulfide isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
At3g19400	Q9LT78	2	EBI-449394,EBI-1993134
At5g43060/MMG4.7	Q9FMH8	3	EBI-449394,EBI-1993115
RD21A	P43297	4	EBI-449394,EBI-1993101
TRX3	Q42403	1	EBI-449394,EBI-449157

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	By similarity
	Chain	24 – 501	478	Probable protein disulfide-isomerase 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

[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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.

[2]

"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC007727 Genomic DNA. Translation: AAD41430.1. AY035096 mRNA. Translation: AAK59601.1. AY063059 mRNA. Translation: AAL34233.1.
IPI	IPI00522163.
PIR	B86351.
RefSeq	NP_173594.1.
UniGene	At.24814
3D structure databases
HSSP	HSSP built from PDB template 1MEK based on UniProtKB P07237.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9XI01. 4 interactions.
2-D gel databases
SWISS-2DPAGE	Q9XI01.
Proteomic databases
PRIDE	Q9XI01.
ProMEX	Q9XI01.
Genome annotation databases
GeneID	838779.
GenomeReviews	Gene locus AT1G21750 in contig CT485782_GR.
KEGG	ath:AT1G21750.
NMPDR	fig|3702.1.peg.2535.
Organism-specific databases
TAIR	At1g21750.
Phylogenomic databases
OMA	Q9XI01. DHTANDV.
Enzyme and pathway databases
BRENDA	5.3.4.1. 302.
Gene expression databases
ArrayExpress	Q9XI01.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR000886. ER_targeting_sequence. IPR005792. Prot_disulphide_isomerase. IPR017936. Thioredoxin-like. IPR006662. Thioredoxin-like_subdom. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
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

PDI1_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:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)