Reviewed, UniProtKB/Swiss-Prot Q12730 (PDI_ASPNG)

Names and origin

Protein names

Recommended name:
    Protein disulfide-isomerase
      Short name=PDI
    EC=5.3.4.1

Gene names

Name:	pdiA
Synonyms:	pdi1

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	515 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	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.
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
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	calcium ion binding Inferred from electronic annotation. Source: InterPro 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
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 515	495	Protein disulfide-isomerase		PRO_0000034213
Regions
	Domain	21 – 132	112	Thioredoxin 1
	Domain	339 – 470	132	Thioredoxin 2
	Motif	512 – 515	4	Prevents secretion from ER Potential
Sites
	Active site	54	1	Nucleophile By similarity
	Active site	57	1	Nucleophile By similarity
	Active site	389	1	Nucleophile By similarity
	Active site	392	1	Nucleophile By similarity
	Site	55	1	Contributes to redox potential value By similarity
	Site	56	1	Contributes to redox potential value By similarity
	Site	117	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	390	1	Contributes to redox potential value By similarity
	Site	391	1	Contributes to redox potential value By similarity
	Site	456	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Disulfide bond	54 ↔ 57		Redox-active By similarity
	Disulfide bond	389 ↔ 392		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q12730-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 2B0058B788400AD9	FASTA	515	56,292
	10 20 30 40 50 60 MRSFAPWLVS LLGASAVVAA ADTESDVISL DQDTFESFMN EHGLVLAEFF APWCGHCKAL 70 80 90 100 110 120 APKYEEAATE LKAKNIPLVK VDCTAEEDLC RSQGVEGYPT LKIFRGVDSS KPYQGARQTE 130 140 150 160 170 180 SIVSYMIKQS LPAVSSVNEE NLEEIKTMDK IVVIGYIPSD DQETYQAFEK YAESQRDNYL 190 200 210 220 230 240 FAATDDAAIA KSEGVEQPSI VLYKDFDEKK AVYDGEIEQE AIHSWVKSAS TPLVGEIGPE 250 260 270 280 290 300 TYSGYIGAGV PLAYIFAETK EEREKYTEDF KPIAQKHKGA INIATIDAKM FGAHAGNLNL 310 320 330 340 350 360 DSQKFPAFAI QDPAKNAKYP YDQAKELNAD EVEKFIQDVL DGKVEPSIKS EPVPESQEGP 370 380 390 400 410 420 VTVVVAHSYK DLVIDNDKDV LLEFYAPWCG HCKALAPKYD ELAALYADHP DLAAKVTIAK 430 440 450 460 470 480 IDATANDVPD PITGFPTLRL YPAGAKDSPI EYSGSRTVED LANFVKENGK HNVDALNVAS 490 500 510 EETQEGGDVT EAAPSATEAE TPAATDDEKA EHDEL

References

[1]	"Isolation and characterisation of a gene encoding protein disulphide isomerase, pdiA, from Aspergillus niger." Ngiam C., Jeenes D.J., Archer D.B. Curr. Genet. 31:133-138(1997) [PubMed: 9021130] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]	Malpricht S. Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X98797 Genomic DNA. Translation: CAA67332.1. X89449 mRNA. Translation: CAA61619.1.
PIR	S57942.
3D structure databases
HSSP	HSSP built from PDB template 1MEK based on UniProtKB P07237.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.3.4.1. 277.
Family and domain databases
InterPro	IPR001393. Calsequestrin. IPR005788. Disulphide_isomerase. IPR000886. ER_target_seq_motif. IPR005792. Prot_disulphide_isomerase. 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. 2 hits. [Graphical view]
PRINTS	PR00312. CALSEQUESTRN.
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

PDI_ASPNG

Accession

Primary (citable) accession number: Q12730

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	September 22, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)