Q54EN4 (PDI2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase 2
Short name=PDI2
EC=5.3.4.1

Gene names

Name:	pdi2
ORF Names:	DDB_G0291434

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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
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 protein folding Inferred from sequence or structural similarity. Source: dictyBase response to bacterium Inferred from expression pattern. Source: dictyBase sexual reproduction Inferred from expression pattern. Source: dictyBase
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from direct assay. Source: dictyBase phagocytic vesicle Inferred from direct assay. Source: dictyBase
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from sequence or structural similarity. Source: dictyBase 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 – 20	20	Potential
	Chain	21 – 513	493	Protein disulfide-isomerase 2		PRO_0000327613
Regions
	Domain	21 – 147	127	Thioredoxin 1
	Domain	355 – 486	132	Thioredoxin 2
	Motif	510 – 513	4	Prevents secretion from ER Potential
Sites
	Active site	70	1	Nucleophile By similarity
	Active site	73	1	Nucleophile By similarity
	Active site	406	1	Nucleophile By similarity
	Active site	409	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	70 ↔ 73		Redox-active By similarity
	Disulfide bond	406 ↔ 409		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54EN4 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 8AAB6B6926069852	FASTA	513	57,753
	10 20 30 40 50 60 MNKFLALLFV LALFANIAFS CEGHPEHDHG DGDHEHDHDE SFVKILDSDN FHNSVSEHDV 70 80 90 100 110 120 TLVMFYAPWC GHCKTLKPLY EEAAKQLSAN KKIAIAKVDC TQHEQLCKQN KVQGYPTLVV 130 140 150 160 170 180 FKNGKAEPYE GDRTTKSIVQ TLEEELKPTI STLESNEDIE EFKKQHPISV VGFFDNDHDD 190 200 210 220 230 240 RFKLFSELAG NNKKSAKFAV VIDKDFSKEH VESTPNVVLF RSFDEPTVAH KGEFDSESLI 250 260 270 280 290 300 KFIKGNSVPL LGEINRNTYK KYESIAVPLA YLFIDSTQDN TQVLEDVKKI ATSQKGNAVF 310 320 330 340 350 360 CWVDMKKFPQ QATHMGLSGK VVPAISVDSV ANKARYNFDE KETFSFDTVS KWIQDVIGGK 370 380 390 400 410 420 VSPFVKSQPE PESNDAPVKV AVGTTFKKLV LDSPKDVLVE FYAPWCGHCK NLAPIYDKLG 430 440 450 460 470 480 EYLKDVESVS IVKIDADSND VPSDIEIRGY PTIMLFKADD KENPISYEGQ RNDHMNFVEF 490 500 510 IQDNAAIEFK LPSSQTDDNV ESKKDSSAKH DEL

References

[1]

"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.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000177 Genomic DNA. Translation: EAL61701.1.
RefSeq	XP_635206.1. XM_630114.1.
3D structure databases
HSSP	HSSP built from PDB template 2DJJ based on UniProtKB P55059.
ProteinModelPortal	Q54EN4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54EN4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0231409; DDB0231409; DDB_G0291434.
GeneID	8628151.
GenomeReviews	Gene locus pdi2 in contig CM000155_GR.
KEGG	ddi:DDB_G0291434.
Organism-specific databases
dictyBase	DDB_G0291434. pdi2.
Phylogenomic databases
eggNOG	KOG0190.
GeneTree	EPrGT00050000003699.
HOGENOM	HBG627841.
OMA	FANIAFS.
PhylomeDB	Q54EN4.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 3 hits.
KO	K09580.
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 3 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

PDI2_DICDI

Accession

Primary (citable) accession number: Q54EN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)