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P05307 (PDIA1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 124. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 – 2020 Ref.2 Ref.3
Chain21 – 510490Protein disulfide-isomerase
PRO_0000034193

Regions

Domain27 – 136110Thioredoxin 1
Domain351 – 477127Thioredoxin 2
Motif507 – 5104Prevents secretion from ER

Sites

Active site551Nucleophile By similarity
Active site581Nucleophile By similarity
Active site3991Nucleophile By similarity
Active site4021Nucleophile By similarity
Site561Contributes to redox potential value By similarity
Site571Contributes to redox potential value By similarity
Site1221Lowers pKa of C-terminal Cys of first active site By similarity
Site4001Contributes to redox potential value By similarity
Site4011Contributes to redox potential value By similarity
Site4631Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue2021N6-acetyllysine By similarity
Modified residue2241N6-succinyllysine By similarity
Modified residue2731N6-succinyllysine By similarity
Disulfide bond55 ↔ 58Redox-active By similarity
Disulfide bond399 ↔ 402Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P05307 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: F19BEC892E03C4CC

FASTA51057,266
        10         20         30         40         50         60 
MLRRALLCLA LTALFRAGAG APDEEDHVLV LHKGNFDEAL AAHKYLLVEF YAPWCGHCKA 

        70         80         90        100        110        120 
LAPEYAKAAG KLKAEGSEIR LAKVDATEES DLAQQYGVRG YPTIKFFKNG DTASPKEYTA 

       130        140        150        160        170        180 
GREADDIVNW LKKRTGPAAS TLSDGAAAEA LVESSEVAVI GFFKDMESDS AKQFFLAAEV 

       190        200        210        220        230        240 
IDDIPFGITS NSDVFSKYQL DKDGVVLFKK FDEGRNNFEG EVTKEKLLDF IKHNQLPLVI 

       250        260        270        280        290        300 
EFTEQTAPKI FGGEIKTHIL LFLPKSVSDY EGKLSNFKKA AESFKGKILF IFIDSDHTDN 

       310        320        330        340        350        360 
QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE GKIKPHLMSQ 

       370        380        390        400        410        420 
ELPDDWDKQP VKVLVGKNFE EVAFDEKKNV FVEFYAPWCG HCKQLAPIWD KLGETYKDHE 

       430        440        450        460        470        480 
NIVIAKMDST ANEVEAVKVH SFPTLKFFPA SADRTVIDYN GERTLDGFKK FLESGGQDGA 

       490        500        510 
GDDDDLEDLE EAEEPDLEED DDQKAVKDEL 

« Hide

References

[1]"Sequence of membrane-associated thyroid hormone binding protein from bovine liver: its identity with protein disulphide isomerase."
Yamauchi K., Yamamoto T., Hayashi H., Koya S., Takikawa H., Toyoshima K., Horiuchi R.
Biochem. Biophys. Res. Commun. 146:1485-1492(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex."
Wetterau J.R., Combs K.A., Spinner S.N., Joiner B.J.
J. Biol. Chem. 265:9800-9807(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-45, INTERACTION WITH MTTP.
[3]Parkinson D.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 21-32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17596 mRNA. Translation: AAA30690.1.
PIRISBOSS. A26829.
RefSeqNP_776560.1. NM_174135.3.
UniGeneBt.106831.

3D structure databases

ProteinModelPortalP05307.
SMRP05307. Positions 21-359, 370-473.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP05307.
PRIDEP05307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281373.
KEGGbta:281373.

Organism-specific databases

CTD5034.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
HOVERGENHBG005920.
InParanoidP05307.
KOK09580.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15199.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
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...

Other

NextBio20805377.

Entry information

Entry namePDIA1_BOVIN
AccessionPrimary (citable) accession number: P05307
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: June 11, 2014
This is version 124 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