Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P29828 (PDI_MEDSA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase

Short name=PDI
EC=5.3.4.1
Gene names
Name:PDI
OrganismMedicago sativa (Alfalfa)
Taxonomic identifier3879 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 Potential.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 512488Protein disulfide-isomerase
PRO_0000034209

Regions

Domain25 – 144120Thioredoxin 1
Domain357 – 485129Thioredoxin 2
Motif509 – 5124Prevents secretion from ER

Sites

Active site621Nucleophile By similarity
Active site651Nucleophile By similarity
Active site4071Nucleophile By similarity
Active site4101Nucleophile By similarity
Site631Contributes to redox potential value By similarity
Site641Contributes to redox potential value By similarity
Site1301Lowers pKa of C-terminal Cys of first active site By similarity
Site4081Contributes to redox potential value By similarity
Site4091Contributes to redox potential value By similarity
Site4711Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation2781N-linked (GlcNAc...) Potential
Disulfide bond62 ↔ 65Redox-active By similarity
Disulfide bond407 ↔ 410Redox-active By similarity

Experimental info

Sequence conflict161L → V in AAA32662. Ref.2
Sequence conflict3951G → A in AAA32662. Ref.2
Sequence conflict4911H → Q in AAA32662. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29828 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: E5EC7341A3FF7935

FASTA51257,087
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11499 mRNA. Translation: CAA77575.1.
M82973 mRNA. Translation: AAA32662.1.
PIRA41440.
ISAASS. S22479.

3D structure databases

ProteinModelPortalP29828.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

ProMEXP29828.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDI_MEDSA
AccessionPrimary (citable) accession number: P29828
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families