Reviewed, UniProtKB/Swiss-Prot Q86IA3 (PDI1_DICDI)

Names and origin

Protein names

Recommended name:
    Protein disulfide-isomerase 1
      Short name=PDI1
    EC=5.3.4.1

Gene names

Name:	pdi1
ORF Names:	DDB_G0276141

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	363 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	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. Ref.1
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
Technical term	Complete proteome
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
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 363	343	Protein disulfide-isomerase 1		PRO_0000327718
Regions
	Domain	21 – 132	112	Thioredoxin 1
	Domain	133 – 285	153	Thioredoxin 2
Sites
	Active site	51	1	Nucleophile By similarity
	Active site	54	1	Nucleophile By similarity
	Active site	172	1	Nucleophile By similarity
	Active site	175	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	51 ↔ 54		Redox-active By similarity
	Disulfide bond	172 ↔ 175		Redox-active By similarity
Experimental info
	Sequence conflict	307	1	T → I in AAB86685. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q86IA3-1 [UniParc]. Last modified July 5, 2004. Version 2. Checksum: 774E3D9AC0434A91	FASTA	363	39,905
	10 20 30 40 50 60 MKILLFVTLI ALAFVALCSA EGNVVVLSPD NFDTVVDGSK TVFVKFYAPW CGHCKKLAPD 70 80 90 100 110 120 FEILADTFAP VSNKVVIAKV DCDQADNKAL CSKYDVSGYP TLKIFDKSTT AKDYNGARSV 130 140 150 160 170 180 DELLTYINNH AKTNVKVKKA PSNVVDLSPS NFDSVVLDKS KNVLVEFYAP WCGHCKKLMP 190 200 210 220 230 240 DYEILGNTYA NEKDVVIAKI DCDAADNKAI CSKYGVTGFP TLKWFGKQSK DGEKYEQGRD 250 260 270 280 290 300 LDTFINYINK QAGVNRVKGG KLAVGAGRVE QLDTIATEFI AAAAEVRKEL VKKAQTVVDS 310 320 330 340 350 360 LPEELRTEGS YYVKVMKTIA EKSIDFVTTE IARITKLVSG SMSGKKADEF AKKLNILESF KSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Dictyostelium discoideum protein disulfide isomerase, an endoplasmic reticulum resident enzyme lacking a KDEL-type retrieval signal." Monnat J., Hacker U., Geissler H., Rauchenberger R., Neuhaus E.M., Maniak M., Soldati T. FEBS Lett. 418:357-362(1997) [PubMed: 9428745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Strain: AX2.
[2]	"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed: 12097910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[4]	"Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake." Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M., Soldati T. Mol. Cell. Proteomics 5:2228-2243(2006) [PubMed: 16926386] [Abstract] Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF019112 mRNA. Translation: AAB86685.1. AC116979 Genomic DNA. Translation: AAO52220.2. AAFI02000014 Genomic DNA. Translation: EAL69370.1.
RefSeq	XP_643357.1.
3D structure databases
HSSP	HSSP built from PDB template 1AUC based on UniProtKB P10599.
ModBase	Search...
Genome annotation databases
GeneID	3394471.
GenomeReviews	Gene locus pdi1 in contig CM000151_GR.
KEGG	ddi:DDB_0185040.
Organism-specific databases
dictyBase	DDB_G0276141. pdi1.
Phylogenomic databases
OMA	GFPTLKW.
Enzyme and pathway databases
BRENDA	5.3.4.1. 424.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR011679. ER_p29_C. IPR017936. Thioredoxin-like. IPR006662. Thioredoxin-like_subdom. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [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.
TIGRFAMs	TIGR01126. pdi_dom. 2 hits.
PROSITE	PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDI1_DICDI

Accession

Primary (citable) accession number: Q86IA3
Secondary accession number(s): O15735, Q552H4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)