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P09102 (PDIA1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. 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
Retina cognin
Short name=R-cognin
Gene names
Name:P4HB
Synonyms:PDI, PDIA1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length515 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). Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase 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. Stabilizes this enzyme and retains it in the ER without contributing to the catalytic activity. Binds UBQLN1 By similarity.

Subcellular location

Endoplasmic reticulum lumen 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 caution

The sequence AAA49054.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.4
Chain23 – 515493Protein disulfide-isomerase Ref.4
PRO_0000034200

Regions

Domain23 – 139117Thioredoxin 1
Domain351 – 480130Thioredoxin 2
Motif512 – 5154Prevents secretion from ER

Sites

Active site581Nucleophile By similarity
Active site611Nucleophile By similarity
Active site4021Nucleophile By similarity
Active site4051Nucleophile By similarity
Site591Contributes to redox potential value By similarity
Site601Contributes to redox potential value By similarity
Site1251Lowers pKa of C-terminal Cys of first active site By similarity
Site4031Contributes to redox potential value By similarity
Site4041Contributes to redox potential value By similarity
Site4661Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond58 ↔ 61Redox-active By similarity
Disulfide bond402 ↔ 405Redox-active By similarity

Experimental info

Sequence conflict231E → Q Ref.1
Sequence conflict231E → Q Ref.3
Sequence conflict94 – 952EL → DV Ref.3
Sequence conflict3591H → Q Ref.3
Sequence conflict4471T → M in CAB57801. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P09102 [UniParc].

Last modified May 16, 2003. Version 3.
Checksum: E7CC978A5109C2CE

FASTA51557,410
        10         20         30         40         50         60 
MAVVRVRAIV ALLCLVAALG LAEPLEEEDG VLVLRAANFE QALAAHRHLL VEFYAPWCGH 

        70         80         90        100        110        120 
CKALAPEYAK AAAQLKAEGS EIRLAKVDAT EEAELAQQFG VRGYPTIKFF RNGDKAAPRE 

       130        140        150        160        170        180 
YTAGREADDI VSWLKKRTGP AATTLTDAAA AETLVDSSEV VVIGFFKDVT SDAAKEFLLA 

       190        200        210        220        230        240 
AESVDDIPFG ISSSADVFSK YQLSQDGVVL FKKFDEGRNN FEGDLTKDNL LNFIKSNQLP 

       250        260        270        280        290        300 
LVIEFTEQTA PKIFGGEIKT HILLFLPKSV SDYEGKLDNF KTAAGNFKGK ILFIFIDSDH 

       310        320        330        340        350        360 
SDNQRILEFF GLKKEECPAV RLITLEEEMT KYKPESDDLT ADKIKEFCNK FLEGKIKPHL 

       370        380        390        400        410        420 
MSQDLPEDWD KQPVKVLVGK NFEEVAFDEN KNVFVEFYAP WCGHCKQLAP IWDKLGETYR 

       430        440        450        460        470        480 
DHENIVIAKM DSTANEVEAV KIHSFPTLKF FPAGSGRNVI DYNGERTLEG FKKFLESGGQ 

       490        500        510 
DGAAADDDLE DLETDEETDL EEGDDDEQKI QKDEL 

« Hide

References

[1]Hausman R.E.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO 315; 356; 488; 491-493 AND 497.
[2]"cDNA for R-cognin: homology with a multifunctional protein."
Krishna Rao A.S., Hausman R.E.
Proc. Natl. Acad. Sci. U.S.A. 90:2950-2954(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 139-515.
Tissue: Retina.
[3]"Structure of the gene encoding the beta-subunit of chicken prolyl 4-hydroxylase."
Nakazawa M., Aida T., Everson W.V., Gonda M.A., Hughes S.H., Kao W.W.
Gene 71:451-460(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-129; 163-172; 209-218; 244-253; 286-295; 353-463 AND 483-515.
[4]"Molecular cloning of a multifunctional chicken protein acting as the prolyl 4-hydroxylase beta-subunit, protein disulphide-isomerase and a cellular thyroid-hormone-binding protein. Comparison of cDNA-deduced amino acid sequences with those in other species."
Parkkonen T., Kivirikko K.Z., Pihlajaniemi T.
Biochem. J. 256:1005-1011(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-515, PROTEIN SEQUENCE OF 23-31 AND 95-109.
[5]Bassuk J.A.
Submitted (FEB-1988) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-459.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11147 mRNA. Translation: AAA49054.2. Different initiation.
X13110 mRNA. Translation: CAA31502.1.
X06768 Genomic DNA. Translation: CAB57801.1.
PIRISCHSS. S02084.
RefSeqNP_001185639.1. NM_001198710.1.
UniGeneGga.4976.

3D structure databases

ProteinModelPortalP09102.
SMRP09102. Positions 26-362, 373-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000011689.

Proteomic databases

PaxDbP09102.
PRIDEP09102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID374091.
KEGGgga:374091.

Organism-specific databases

CTD5034.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
HOVERGENHBG005920.
InParanoidP09102.
KOK09580.
PhylomeDBP09102.

Enzyme and pathway databases

SABIO-RKP09102.

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...

Other

NextBio20813610.
PROP09102.

Entry information

Entry namePDIA1_CHICK
AccessionPrimary (citable) accession number: P09102
Secondary accession number(s): Q90969
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 16, 2003
Last modified: April 16, 2014
This is version 126 of the entry and version 3 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