Reviewed, UniProtKB/Swiss-Prot Q43116 (PDI_RICCO)

Names and origin

Protein names	Recommended name:     Protein disulfide-isomerase       Short name=PDI     EC=5.3.4.1
Organism	Ricinus communis (Castor bean)
Taxonomic identifier	3988 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus

Protein attributes

Sequence length	498 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 Potential.
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 Glycoprotein
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW 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 – 23	23	Potential
	Chain	24 – 498	475	Protein disulfide-isomerase		PRO_0000034211
Regions
	Domain	24 – 143	120	Thioredoxin 1
	Domain	339 – 484	146	Thioredoxin 2
	Motif	495 – 498	4	Prevents secretion from ER By similarity
Sites
	Active site	61	1	Nucleophile By similarity
	Active site	64	1	Nucleophile By similarity
	Active site	406	1	Nucleophile By similarity
	Active site	409	1	Nucleophile By similarity
	Site	62	1	Contributes to redox potential value By similarity
	Site	63	1	Contributes to redox potential value By similarity
	Site	129	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	407	1	Contributes to redox potential value By similarity
	Site	408	1	Contributes to redox potential value By similarity
	Site	470	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Glycosylation	41	1	N-linked (GlcNAc...) Potential
	Disulfide bond	61 ↔ 64		Redox-active By similarity
	Disulfide bond	406 ↔ 409		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q43116-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D556492D78F955D5	FASTA	498	55,561
	10 20 30 40 50 60 MASFRGSIWY CIFVLSLIAV AISAAESEEE QSSVLTLDST NFTDTISKHD FIVVEFYAPW 70 80 90 100 110 120 CGHCKKLRPE YEKAASILKS HDIPVVLAKV DANEEANKEL ATQYDIKGFP TLKILRNGGK 130 140 150 160 170 180 SIQEYKGPRE ADGIAEYLKK QSGPASVEIK STEAANTFIG DKKIFIVGVF PKFSGEEYEN 190 200 210 220 230 240 YMSVADKLRS DYEFGHTLDA KHLPQGESSV TGPVVRLFKP FDELFVDFKD FNVDALEKFV 250 260 270 280 290 300 EESSMPVVTV FNSDPSNHPF VIKFFNSPDA KAMLFMNFNG EAADSIKSKY QEVAHQFKGE 310 320 330 340 350 360 GIILLLGDVE ASQGAFQYFG LKEDQVPLII IQTNDGQKYL KANLEPDHIA PWVKAYKEGK 370 380 390 400 410 420 VQAYRKSEPI PEVNNEPVKV VVADTLQDIV FNSGKNVLLE FYAPWCGHCK QLAPILDEVA 430 440 450 460 470 480 VSYKSDADIV IAKLDATAND IPSDTFDVRG YPTVYFRSAS GKVEQYDGDR TKDDIISFIE 490 KNRDKAAQQE SANGKDEL

References

[1]	"Molecular characterisation of plant endoplasmic reticulum. Identification of protein disulfide-isomerase as the major reticuloplasmin." Coughlan S.J., Hastings C., Winfrey R.J. Eur. J. Biochem. 235:215-224(1996) [PubMed: 8631332] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Hale.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U41385 mRNA. Translation: AAB05641.1.
PIR	S62626.
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. 816.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR000886. ER_targeting_sequence. IPR005792. Prot_disulphide_isomerase. IPR017936. Thioredoxin-like. IPR006662. Thioredoxin-like_subdom. 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	PR00421. THIOREDOXIN.
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_RICCO

Accession

Primary (citable) accession number: Q43116

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)