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

P21195 (PDIA1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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
Alternative name(s):
Cellular thyroid hormone-binding protein
Prolyl 4-hydroxylase subunit beta
p55
Gene names
Name:P4HB
Synonyms:PDIA1
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP By similarity.

Catalytic activity

Catalyzes the rearrangement of -S-S- bonds in proteins.

Subunit structure

Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1 By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity. Melanosome By similarity. Cell membrane; Peripheral membrane protein Potential. Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces By similarity.

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 – 1818 By similarity
Chain19 – 509491Protein disulfide-isomerase
PRO_0000034198

Regions

Domain19 – 135117Thioredoxin 1
Domain347 – 476130Thioredoxin 2
Motif506 – 5094Prevents secretion from ER

Sites

Active site541Nucleophile By similarity
Active site571Nucleophile By similarity
Active site3981Nucleophile By similarity
Active site4011Nucleophile By similarity
Site551Contributes to redox potential value By similarity
Site561Contributes to redox potential value By similarity
Site1211Lowers pKa of C-terminal Cys of first active site By similarity
Site3991Contributes to redox potential value By similarity
Site4001Contributes to redox potential value By similarity
Site4621Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue2231N6-succinyllysine By similarity
Modified residue2721N6-succinyllysine By similarity
Disulfide bond54 ↔ 57Redox-active By similarity
Disulfide bond398 ↔ 401Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P21195 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 093C8C18E209BAB5

FASTA50956,808
        10         20         30         40         50         60 
MLRRAVLCLA LAVTAGWAWA AEEEDNVLVL KSSNFAEELA AHKHLLVEFY APWCGHCKAL 

        70         80         90        100        110        120 
APEYAKAAGK LKAEGSDIRL AKVDATEESD LAQQYGVRGY PTIKFFKNGD TASPKEYTAG 

       130        140        150        160        170        180 
READDIVNWL KKRTGPAATT LADSAAAESL VESSEVAVIG FFKDVESDAA KQFLLAAEAT 

       190        200        210        220        230        240 
DDIPFGLTAS SDVFSRYQVH QDGVVLFKKF DEGRNNFEGE VTKEKLLDFI KHNQLPLVIE 

       250        260        270        280        290        300 
FTEQTAPKIF GGEIKTHILL FLPRSAADHD GKLSGFKQAA EGFKGKILFI FIDSDHADNQ 

       310        320        330        340        350        360 
RILEFFGLKK EECPAVRLIT LEEEMTKYKP ESDELTAEGI TEFCQRFLEG KIKPHLMSQE 

       370        380        390        400        410        420 
LPEDWDRQPV KVLVGKNFEE VAFDEKKNVF VEFYAPWCGH CKQLAPIWDK LGETYKEHQD 

       430        440        450        460        470        480 
IVIAKMDSTA NEVEAVKVHS FPTLKFFPAG PGRTVIDYNG ERTLDGFKKF LESGGQDGAG 

       490        500 
DEDGLEDLEE AEEPDLEEDD DQKAVRDEL 

« Hide

References

[1]"Molecular cloning of cDNA encoding a 55-kDa multifunctional thyroid hormone binding protein of skeletal muscle sarcoplasmic reticulum."
Fliegel L., Newton E., Burns K., Michalak M.
J. Biol. Chem. 265:15496-15502(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05602 mRNA. Translation: AAA31476.1.
PIRA38362.
RefSeqNP_001164518.1. NM_001171047.1.
UniGeneOcu.5912.

3D structure databases

ProteinModelPortalP21195.
SMRP21195. Positions 20-358, 369-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1173214. 2 interactions.

Proteomic databases

PRIDEP21195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100328595.

Organism-specific databases

CTD5034.

Phylogenomic databases

HOVERGENHBG005920.

Family and domain databases

Gene3D3.40.30.10. 4 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 namePDIA1_RABIT
AccessionPrimary (citable) accession number: P21195
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families