Reviewed, UniProtKB/Swiss-Prot Q00002 (PDI_ALTAL)

Names and origin

Protein names	Recommended name:     Protein disulfide-isomerase       Short name=PDI     EC=5.3.4.1 Alternative name(s):     Allergen=Alt a 4
Organism	Alternaria alternata (Alternaria rot fungus)
Taxonomic identifier	5599 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Pleosporomycetidae › Pleosporales › Pleosporaceae › mitosporic Pleosporaceae › Alternaria › Alternaria alternata group

Protein attributes

Sequence length	436 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
Allergenic properties	Causes an allergic reaction in human. Ref.1
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains at least 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Disease	Allergen
Domain	Redox-active center
Molecular function	Isomerase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein disulfide isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 436	›436	Protein disulfide-isomerase		PRO_0000120175
Regions
	Domain	216 – 365	150	Thioredoxin
	Motif	433 – 436	4	Prevents secretion from ER Potential
	Compositional bias	362 – 431	70	Ser-rich
Sites
	Active site	266	1	Nucleophile By similarity
	Active site	269	1	Nucleophile By similarity
	Site	267	1	Contributes to redox potential value By similarity
	Site	268	1	Contributes to redox potential value By similarity
Amino acid modifications
	Disulfide bond	266 ↔ 269		Redox-active By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q00002-1 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: ECBB7D93738BCEE3	FASTA	436	46,275
	10 20 30 40 50 60 ARDMTKQALP AVSEVTKDTL EEFKTADKVV LVAYFAADDK ASNETFTSVA NGLRDNFLFG 70 80 90 100 110 120 ATNDAALAKA EGVKQPGLVC TSPSTTARTS SPRPSMRTYP RLRKVASTPL IGEVGPETYA 130 140 150 160 170 180 GYMAAGIPLA YIFAETPEER EEFAKELKPL ALKHKGEINF ATIDAKSFGQ HAGNLNLKVG 190 200 210 220 230 240 TWPAFAIQRT EKNEKFPTNQ EAKITEKEIG KFVDDFLAGK IDPSIKSEPI PESNDGPVTV 250 260 270 280 290 300 VVAHNYKDVV IDNDKDVLVE FYAPWCGHCK ALAPKYEELG QLYASDELSK LVTIAKVDAT 310 320 330 340 350 360 LNDVPDEIQG FLPSSLFPLA RRMPQSTTLV PHCRGSRPVH RRERLTQASA SVGEAVEDAT 370 380 390 400 410 420 ESAKASASSA TDSAASAVSE GTETVKSGAS VASDSASSAA SEATKSVKSA ASEVTNSASS 430 AASEASASAS SVKDEL

References

[1]	"Molecular characterization of Alternaria alternata and Cladosporium herbarum allergens." Achatz G., Oberkofler H., Lechenauer E., Simon B., Unger A., Kandler D., Ebner C., Prillinger H., Kraft D., Breitenbach M. Adv. Exp. Med. Biol. 409:157-161(1996) [PubMed: 9095236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALLERGENICITY.
[2]	Unger A.M., Lechenauer E., Simon B., Oberkofler H., Probst G., Achatz G., Breitenbach M. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 08-0203-Berlin.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X84217 mRNA. Translation: CAA58999.1. U82634 mRNA. Translation: AAB40401.1.
3D structure databases
HSSP	HSSP built from PDB template 1EP7 based on UniProtKB P80028.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.3.4.1. 74336.
Family and domain databases
InterPro	IPR000886. ER_target_seq_motif. IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
Pfam	PF00085. Thioredoxin. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDI_ALTAL

Accession

Primary (citable) accession number: Q00002
Secondary accession number(s): P87325

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	January 24, 2006
Last modified:	September 22, 2009
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)