P52588 (PDI_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

PDI

Organism

Zea mays (Maize)

Taxonomic identifier

4577 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	513 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 glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro protein folding Inferred from electronic annotation. Source: GOC
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 – 23	23	By similarity
	Chain	24 – 513	490	Protein disulfide-isomerase		PRO_0000034210
Regions
	Domain	24 – 145	122	Thioredoxin 1
	Domain	366 – 485	120	Thioredoxin 2
	Motif	510 – 513	4	Prevents secretion from ER Potential
Sites
	Active site	63	1	Nucleophile By similarity
	Active site	66	1	Nucleophile By similarity
	Active site	408	1	Nucleophile By similarity
	Active site	411	1	Nucleophile By similarity
	Site	64	1	Contributes to redox potential value By similarity
	Site	65	1	Contributes to redox potential value By similarity
	Site	131	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	409	1	Contributes to redox potential value By similarity
	Site	410	1	Contributes to redox potential value By similarity
	Site	471	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Glycosylation	279	1	N-linked (GlcNAc...) Potential
	Disulfide bond	63 ↔ 66		Redox-active By similarity
	Disulfide bond	408 ↔ 411		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P52588 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 29302DD01A3DEB80	FASTA	513	57,097
	10 20 30 40 50 60 MAIRSKAWIS LLLALAVALS ARAEEEPAAA AEGEAVLTLD VDSFDEAVAK HPFMVVEFYA 70 80 90 100 110 120 PWCGHCKKLA PEYENAAKAL SKHDPPIVLA KVDANEEKNR PLATKYEIQG FPTIKIFRDR 130 140 150 160 170 180 GKNIQEYKGP READGIVDYL KKQVGPASKE IKSPEDATAL IDDKKIYIVG IFAEFSGTEF 190 200 210 220 230 240 TNFMEVAEKL RSDYDFGHTL HANHLPRGDA AVERPLVRLL KPFDELVVDS KDFDVAALMK 250 260 270 280 290 300 FIDASTIPRV VTFDKNPDNH PYLMKFFQSS APKAMLFLNF STGPFDSFKS AYSAAAEEFK 310 320 330 340 350 360 DKEIKFLIGD IEASQGAFQY FGLKEDQTPL ILIQDGDSKK FLKVHVEADQ IVAWLKEYFD 370 380 390 400 410 420 GKLTPFRNSE PIPEVNNEPV KVVVADNVHD FVFKSGKNVL IEFYAPWCGH CKKLAPILDE 430 440 450 460 470 480 AATTLQSDEE VVIAKMDATA NDVPSEFDVQ GYPTLYFVTP SGKVTSYDSG RTADDIVDFI 490 500 510 KKSKETAAPH HHHHPGATGI REGSRAEPVK DEL

References

[1]	"Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant." Li C.P., Larkins B.A. Plant Mol. Biol. 30:873-882(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Wisconsin 64A. Tissue: Endosperm.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L39014 mRNA. Translation: AAB08519.1.
PIR	S69181.
3D structure databases
ProteinModelPortal	P52588.
ModBase	Search...
Proteomic databases
PRIDE	P52588.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Gramene	P52588.
MaizeGDB	86830.
Family and domain databases
Gene3D	3.40.30.10. 3 hits.
InterPro	IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 4 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

PDI_MAIZE

Accession

Primary (citable) accession number: P52588

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program