Q9FF55 (PDI14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide isomerase-like 1-4
Short name=AtPDIL1-4
EC=5.3.4.1

Alternative name(s):
Protein disulfide isomerase 2
Short name=AtPDI2
Protein disulfide isomerase-like 2-2
Short name=AtPDIL2-2

Gene names

Name:	PDIL1-4
Synonyms:	PDI2, PDIL2-2
Ordered Locus Names:	At5g60640
ORF Names:	MUP24.6

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	597 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	Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds. Ref.8
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Interacts with MEE8 and MED37A. Ref.8
Subcellular location	Endoplasmic reticulum lumen. Golgi apparatus. Vacuole. Nucleus. Secreted › cell wall Ref.8.
Tissue specificity	Expressed in germinating seedling, including the cotyledons and hypocotyl, in vascular tissues, in pollen grains, root tips, leaf trichomes, developing seeds and siliques. Ref.6 Ref.8
Disruption phenotype	No visible phenotype, probably due to functional redundancy. Ref.8
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Cell wall Endoplasmic reticulum Golgi apparatus Nucleus Secreted 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 glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro response to oxidative stress Inferred from direct assay PubMed 12492832. Source: TAIR
Cellular_component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell 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 extracellular region Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from direct assay PubMed 12492832PubMed 14671022. Source: TAIR nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell vacuolar membrane Inferred from direct assay PubMed 17151019. Source: TAIR
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from sequence or structural similarity Ref.6. Source: TAIR 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: Q9FF55-1)

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 – 25	25	Potential
	Chain	26 – 597	572	Protein disulfide isomerase-like 1-4		PRO_0000400019
Regions
	Domain	85 – 208	124	Thioredoxin 1
	Domain	429 – 550	122	Thioredoxin 2
	Motif	594 – 597	4	Prevents secretion from ER By similarity
Sites
	Active site	132	1	Nucleophile By similarity
	Active site	135	1	Nucleophile By similarity
	Active site	471	1	Nucleophile By similarity
	Active site	474	1	Nucleophile By similarity
	Site	133	1	Contributes to redox potential value By similarity
	Site	134	1	Contributes to redox potential value By similarity
	Site	194	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	472	1	Contributes to redox potential value By similarity
	Site	473	1	Contributes to redox potential value By similarity
	Site	536	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Glycosylation	112	1	N-linked (GlcNAc...) Potential
	Glycosylation	213	1	N-linked (GlcNAc...) Potential
	Glycosylation	342	1	N-linked (GlcNAc...) Potential
	Glycosylation	524	1	N-linked (GlcNAc...) Potential
	Disulfide bond	132 ↔ 135		Redox-active By similarity
	Disulfide bond	471 ↔ 474		Redox-active By similarity
Experimental info
	Sequence conflict	400	1	P → H in AAM65262. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 5A8FC7E72AA64B2B	FASTA	597	66,357
	10 20 30 40 50 60 MAFRVLLLFS LTALLIFSAV SPSFAASSSD DVDDEDLSFL EDLKEDDVPG ADSLSSSTGF 70 80 90 100 110 120 DEFEGGEEED PDMYNDDDDE EGDFSDLGNP DSDPLPTPEI DEKDVVVIKE RNFTDVIENN 130 140 150 160 170 180 QYVLVEFYAP WCGHCQSLAP EYAAAATELK EDGVVLAKID ATEENELAQE YRVQGFPTLL 190 200 210 220 230 240 FFVDGEHKPY TGGRTKETIV TWVKKKIGPG VYNLTTLDDA EKVLTSGNKV VLGYLNSLVG 250 260 270 280 290 300 VEHDQLNAAS KAEDDVNFYQ TVNPDVAKMF HLDPESKRPA LVLVKKEEEK ISHFDGEFVK 310 320 330 340 350 360 SALVSFVSAN KLALVSVFTR ETAPEIFESA IKKQLLLFVT KNESEKVLTE FQEAAKSFKG 370 380 390 400 410 420 KLIFVSVDLD NEDYGKPVAE YFGVSGNGPK LIGYTGNEDP KKYFFDGEIQ SDKIKIFGED 430 440 450 460 470 480 FLNDKLKPFY KSDPIPEKND EDVKIVVGDN FDEIVLDDSK DVLLEVYAPW CGHCQALEPM 490 500 510 520 530 540 YNKLAKHLRS IDSLVITKMD GTTNEHPKAK AEGFPTILFF PAGNKTSEPI TVDTDRTVVA 550 560 570 580 590 FYKFLRKHAT IPFKLEKPAS TESPKTAEST PKVETTETKE SPDSTTKSSQ SDSKDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones." Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S. DNA Res. 4:215-230(1997) [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]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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.
[6]	"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.
[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.
[8]	"Protein disulfide isomerase-2 of Arabidopsis mediates protein folding and localizes to both the secretory pathway and nucleus, where it interacts with maternal effect embryo arrest factor." Cho E.J., Yuen C.Y., Kang B.H., Ondzighi C.A., Staehelin L.A., Christopher D.A. Mol. Cells 32:459-475(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MEE8 AND MED37A/BIP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB005246 Genomic DNA. Translation: BAB09837.1. CP002688 Genomic DNA. Translation: AED97360.1. BT001994 mRNA. Translation: AAN72005.1. BT008359 mRNA. Translation: AAP37718.1. AY087725 mRNA. Translation: AAM65262.1.
IPI	IPI00523230.
RefSeq	NP_851234.1. NM_180903.3.
UniGene	At.22422.
3D structure databases
HSSP	HSSP built from PDB template 1MEK based on UniProtKB P07237.
ProteinModelPortal	Q9FF55.
SMR	Q9FF55. Positions 41-552.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G60640.1-P.
Proteomic databases
PaxDb	Q9FF55.
PRIDE	Q9FF55.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G60640.1; AT5G60640.1; AT5G60640.
GeneID	836185.
KEGG	ath:AT5G60640.
Organism-specific databases
TAIR	At5g60640.
Phylogenomic databases
eggNOG	COG0526.
HOGENOM	HOG000162459.
InParanoid	Q9FF55.
KO	K09580.
OMA	YKPESND.
PhylomeDB	Q9FF55.
ProtClustDB	CLSN2680577.
Gene expression databases
ArrayExpress	Q9FF55.
Genevestigator	Q9FF55.
Family and domain databases
Gene3D	3.40.30.10. 4 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. 3 hits.
TIGRFAMs	TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. pdi_dom. 1 hit.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDI14_ARATH

Accession

Primary (citable) accession number: Q9FF55
Secondary accession number(s): Q8LAM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2010
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program