Reviewed, UniProtKB/Swiss-Prot P29828 (PDI_MEDSA)

Names and origin

Protein names

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

Gene names

Name:

PDI

Organism

Medicago sativa (Alfalfa)

Taxonomic identifier

3879 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago

Protein attributes

Sequence length	512 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 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 – 24	24	By similarity
	Chain	25 – 512	488	Protein disulfide-isomerase		PRO_0000034209
Regions
	Domain	25 – 144	120	Thioredoxin 1
	Domain	357 – 485	129	Thioredoxin 2
	Motif	509 – 512	4	Prevents secretion from ER
Sites
	Active site	62	1	Nucleophile By similarity
	Active site	65	1	Nucleophile By similarity
	Active site	407	1	Nucleophile By similarity
	Active site	410	1	Nucleophile By similarity
	Site	63	1	Contributes to redox potential value By similarity
	Site	64	1	Contributes to redox potential value By similarity
	Site	130	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	408	1	Contributes to redox potential value By similarity
	Site	409	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	278	1	N-linked (GlcNAc...) Potential
	Disulfide bond	62 ↔ 65		Redox-active By similarity
	Disulfide bond	407 ↔ 410		Redox-active By similarity
Experimental info
	Sequence conflict	16	1	L → V in AAA32662. Ref.2
	Sequence conflict	395	1	G → A in AAA32662. Ref.2
	Sequence conflict	491	1	H → Q in AAA32662. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P29828-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: E5EC7341A3FF7935	FASTA	512	57,087
	10 20 30 40 50 60 MAKNVAIFGL LFSLLLLVPS QIFAEESSTD AKEFVLTLDN TNFHDTVKKH DFIVVEFYAP 70 80 90 100 110 120 WCGHCKKLAP EYEKAASILS THEPPVVLAK VDANEEHNKD LASENDVKGF PTIKIFRNGG 130 140 150 160 170 180 KNIQEYKGPR EAEGIVEYLK KQSGPASTEI KSADDATAFV GDNKVVIVGV FPKFSGEEYD 190 200 210 220 230 240 NFIALAEKLR SDYDFAHTLN AKHLPKGDSS VSGPVVRLFK PFDELFVDSK DFNVEALEKF 250 260 270 280 290 300 IEESSTPIVT VFNNEPSNHP FVVKFFNSPN AKAMLFINFT TEGAESFKTK YHEVAEQYKQ 310 320 330 340 350 360 QGVSFLVGDV ESSQGAFQYF GLKEEQVPLI IIQHNDGKKF FKPNLELDQL PTWLKAYKDG 370 380 390 400 410 420 KVEPFVKSEP IPETNNEPVK VVVGQTLEDV VFKSGKNVLI EFYAPWCGHC KQLAPILDEV 430 440 450 460 470 480 AVSFQSDADV VIAKLDATAN DIPTDTFDVQ GYPTLYFRSA SGKLSQYDGG RTKEDIIEFI 490 500 510 EKNKDKTGAA HQEVEQPKAA AQPEAEQPKD EL

References

[1]	"Sequence analysis and developmental expression of an alfalfa protein disulfide isomerase." Shorrosh B.S., Dixon R.A. Plant Mol. Biol. 19:319-321(1992) [PubMed: 1623182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Apollo.
[2]	"Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C." Shorrosh B.S., Dixon R.A. Proc. Natl. Acad. Sci. U.S.A. 88:10941-10945(1991) [PubMed: 1720555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z11499 mRNA. Translation: CAA77575.1. M82973 mRNA. Translation: AAA32662.1.
PIR	A41440. ISAASS. S22479.
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. 815.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR000886. ER_target_seq_motif. 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_MEDSA

Accession

Primary (citable) accession number: P29828

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	September 22, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)