Q00216 (TIGA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase tigA
EC=5.3.4.1

Gene names

Name:

tigA

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	359 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)

Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subcellular location	Endoplasmic reticulum lumen Potential.
Induction	By stress, and tunicamycin. Ref.1
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Biological process	Stress response
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 glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from electronic annotation. Source: EC 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 – 19	19	Potential
	Chain	20 – 359	340	Protein disulfide-isomerase tigA		PRO_0000034245
Regions
	Domain	20 – 129	110	Thioredoxin 1
	Domain	131 – 250	120	Thioredoxin 2
	Motif	356 – 359	4	Prevents secretion from ER Potential
Sites
	Active site	49	1	Nucleophile By similarity
	Active site	52	1	Nucleophile By similarity
	Active site	169	1	Nucleophile By similarity
	Active site	172	1	Nucleophile By similarity
	Site	50	1	Contributes to redox potential value By similarity
	Site	51	1	Contributes to redox potential value By similarity
	Site	115	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	170	1	Contributes to redox potential value By similarity
	Site	171	1	Contributes to redox potential value By similarity
	Site	236	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Disulfide bond	49 ↔ 52		Redox-active By similarity
	Disulfide bond	169 ↔ 172		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q00216 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 346B64197BA37608	FASTA	359	38,592
	10 20 30 40 50 60 MVRLSNLVSC LGLASAVTAA VVDLVPKNFD DVVLKSGKPA LVEFFAPWCG HCKNLAPVYE 70 80 90 100 110 120 ELGQAFAHAS DKVTVGKVDA DEHRDLGRKF GVQGFPTLKW FDGKSDEPED YKGGRDLESL 130 140 150 160 170 180 SSFISEKTGV KPRGPKKEPS KVEMLNDATF KGAVGGDNDV LVAFTAPWCG HCKNLAPTWE 190 200 210 220 230 240 ALANDFVLEP NVVIAKVDAD AENGKATARE QGVSGYPTIK FFPKGSTESV PYEGARSEQA 250 260 270 280 290 300 FIDFLNEKTG THRTVGGGLD TKAGTIASLD ELIASTSAAD LAAAVKKAAT ELKDKYAQYY 310 320 330 340 350 VKVADKLSQN AEYAAKELAR LEKILAKGGS APEKVDDLIS RSNILRKFVG EEKEAKDEL

References

[1]	"Isolation and characterisation of a novel stress-inducible PDI-family gene from Aspergillus niger." Jeenes D.J., Pfaller R., Archer D.B. Gene 193:151-156(1997) [PubMed: 9256071] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X98748 Genomic DNA. Translation: CAA67299.1.
3D structure databases
ProteinModelPortal	Q00216.
ModBase	Search...
Protein-protein interaction databases
STRING	Q00216.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
PhylomeDB	Q00216.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR011679. ER_p29_C. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:1.20.1150.12. ERp29_C_type. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
Pfam	PF07749. ERp29. 1 hit. PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF47933. ERP29_C. 1 hit. SSF52833. Thiordxn-like_fd. 2 hits.
TIGRFAMs	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

TIGA_ASPNG

Accession

Primary (citable) accession number: Q00216

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	July 27, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program