Q9SRG3 (PDI12_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide isomerase-like 1-2
Short name=AtPDIL1-2
EC=5.3.4.1

Alternative name(s):
Protein disulfide-isomerase 2
Short name=PDI 2
Protein disulfide-isomerase 6
Short name=AtPDI6

Gene names

Name:	PDIL1-2
Synonyms:	PDI6
Ordered Locus Names:	At1g77510
ORF Names:	T5M16.10

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	508 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subcellular location	Endoplasmic reticulum lumen Probable.
Tissue specificity	Widely expressed. Ref.5
Induction	By chemically-induced ER stress response. Ref.5
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
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 cadmium ion Inferred from expression pattern PubMed 16502469. 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
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 22430844. Source: TAIR chloroplast Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR endoplasmic reticulum Inferred from direct assay PubMed 16618929PubMed 22923678. Source: TAIR endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 17644812. Source: TAIR 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.5. Source: TAIR protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 508	484	Protein disulfide isomerase-like 1-2		PRO_0000034206
Regions
	Domain	25 – 140	116	Thioredoxin 1
	Domain	336 – 480	145	Thioredoxin 2
	Motif	505 – 508	4	Prevents secretion from ER By similarity
Sites
	Active site	58	1	Nucleophile By similarity
	Active site	61	1	Nucleophile By similarity
	Active site	402	1	Nucleophile By similarity
	Active site	405	1	Nucleophile By similarity
	Site	59	1	Contributes to redox potential value By similarity
	Site	60	1	Contributes to redox potential value By similarity
	Site	126	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	403	1	Contributes to redox potential value By similarity
	Site	404	1	Contributes to redox potential value By similarity
	Site	466	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Glycosylation	38	1	N-linked (GlcNAc...) Potential
	Glycosylation	273	1	N-linked (GlcNAc...) Potential
	Disulfide bond	58 ↔ 61		Redox-active By similarity
	Disulfide bond	402 ↔ 405		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9SRG3 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: B6300A31DFD2AB62	FASTA	508	56,365
	10 20 30 40 50 60 MAFKGFACFS ILLLLSLFVS SIRSEETKEF VLTLDHSNFT ETISKHDFIV VEFYAPWCGH 70 80 90 100 110 120 CQKLAPEYEK AASELSSHNP PLALAKIDAS EEANKEFANE YKIQGFPTLK ILRNGGKSVQ 130 140 150 160 170 180 DYNGPREAEG IVTYLKKQSG PASVEIKSAD SATEVVGEKN VVAVGVFPKL SGDEFDSFMA 190 200 210 220 230 240 LAEKLRADYD FAHTLDAKFL PRGESVEGPA VRLFKPFDEL FVDSKDFNGE ALEKFVKESS 250 260 270 280 290 300 IPLVTVFDSD PNNHPYVAKF FESPATKAMM FVNFTGATAE ALKSKYREVA TSNKDQSLAF 310 320 330 340 350 360 LVGDAESSQG AFQYFGLEES QVPLIIIQTP DNKKYLKVNV EVDQIESWFK DFQDGKVAVH 370 380 390 400 410 420 KKSQPIPAEN NEPVKVVVAE SLDDIVFKSG KNVLIEFYAP WCGHCQKLAP ILDEVALSFQ 430 440 450 460 470 480 NDPSVIIAKL DATANDIPSD TFDVKGFPTI YFRSASGNVV VYEGDRTKED FINFVEKNSE 490 500 KKPTSHGEES TKSEEPKKTE ETAAKDEL

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]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) 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, INDUCTION.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC010704 Genomic DNA. Translation: AAG51673.1. CP002684 Genomic DNA. Translation: AEE35987.1. AK226862 mRNA. Translation: BAE98951.1.
IPI	IPI00538827.
PIR	E96804.
RefSeq	NP_177875.1. NM_106400.2.
UniGene	At.17801.
3D structure databases
ProteinModelPortal	Q9SRG3.
SMR	Q9SRG3. Positions 29-483.
ModBase	Search...
Proteomic databases
PaxDb	Q9SRG3.
PRIDE	Q9SRG3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G77510.1; AT1G77510.1; AT1G77510.
GeneID	844087.
KEGG	ath:AT1G77510.
Organism-specific databases
TAIR	At1g77510.
Phylogenomic databases
eggNOG	COG0526.
HOGENOM	HOG000162459.
InParanoid	Q9SRG3.
KO	K09580.
OMA	PEVNDEP.
PhylomeDB	Q9SRG3.
ProtClustDB	CLSN2679750.
Gene expression databases
ArrayExpress	Q9SRG3.
Genevestigator	Q9SRG3.
GermOnline	AT1G77510. Arabidopsis thaliana.
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

PDI12_ARATH

Accession

Primary (citable) accession number: Q9SRG3
Secondary accession number(s): Q0WV97

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program