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Q14554 (PDIA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 A5

EC=5.3.4.1
Alternative name(s):
Protein disulfide isomerase-related protein
Gene names
Name:PDIA5
Synonyms:PDIR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Endoplasmic reticulum lumen By similarity.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 3 thioredoxin domains.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityPolymorphism
   DomainRedox-active center
Repeat
Signal
   Molecular functionIsomerase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation-reduction process

Traceable author statement Ref.1. Source: UniProtKB

protein folding

Traceable author statement Ref.1. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentendoplasmic reticulum

Inferred from Biological aspect of Ancestor. Source: RefGenome

endoplasmic reticulum lumen

Traceable author statement Ref.1. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

   Molecular_functionoxidoreductase activity

Traceable author statement Ref.1. Source: UniProtKB

protein disulfide isomerase activity

Traceable author statement Ref.1. Source: UniProtKB

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 519498Protein disulfide-isomerase A5
PRO_0000034233

Regions

Domain134 – 261128Thioredoxin 1
Domain270 – 384115Thioredoxin 2
Domain378 – 506129Thioredoxin 3
Motif516 – 5194Prevents secretion from ER Potential

Amino acid modifications

Disulfide bond182 ↔ 185Redox-active By similarity
Disulfide bond305 ↔ 308Redox-active By similarity
Disulfide bond426 ↔ 429Redox-active By similarity

Natural variations

Natural variant3911T → M.
Corresponds to variant rs2292661 [ dbSNP | Ensembl ].
VAR_052581

Secondary structure

................. 519
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14554 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 6083FBEB8C019658

FASTA51959,594
        10         20         30         40         50         60 
MARAGPAWLL LAIWVVLPSW LSSAKVSSLI ERISDPKDLK KLLRTRNNVL VLYSKSEVAA 

        70         80         90        100        110        120 
ENHLRLLSTV AQAVKGQGTI CWVDCGDAES RKLCKKMKVD LSPKDKKVEL FHYQDGAFHT 

       130        140        150        160        170        180 
EYNRAVTFKS IVAFLKDPKG PPLWEEDPGA KDVVHLDSEK DFRRLLKKEE KPLLIMFYAP 

       190        200        210        220        230        240 
WCSMCKRMMP HFQKAATQLR GHAVLAGMNV YSSEFENIKE EYSVRGFPTI CYFEKGRFLF 

       250        260        270        280        290        300 
QYDNYGSTAE DIVEWLKNPQ PPQPQVPETP WADEGGSVYH LTDEDFDQFV KEHSSVLVMF 

       310        320        330        340        350        360 
HAPWCGHCKK MKPEFEKAAE ALHGEADSSG VLAAVDATVN KALAERFHIS EFPTLKYFKN 

       370        380        390        400        410        420 
GEKYAVPVLR TKKKFLEWMQ NPEAPPPPEP TWEEQQTSVL HLVGDNFRET LKKKKHTLVM 

       430        440        450        460        470        480 
FYAPWCPHCK KVIPHFTATA DAFKDDRKIA CAAVDCVKDK NQDLCQQEAV KGYPTFHYYH 

       490        500        510 
YGKFAEKYDS DRTELGFTNY IRALREGDHE RLGKKKEEL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR)."
Hayano T., Kikuchi M.
FEBS Lett. 372:210-214(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D49490 mRNA. Translation: BAA08451.1.
CH471052 Genomic DNA. Translation: EAW79452.1.
CH471052 Genomic DNA. Translation: EAW79454.1.
CCDSCCDS3020.1.
PIRS66673.
RefSeqNP_006801.1. NM_006810.3.
UniGeneHs.477352.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4I6XX-ray1.50A29-150[»]
ProteinModelPortalQ14554.
SMRQ14554. Positions 29-502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116154. 4 interactions.
IntActQ14554. 12 interactions.
MINTMINT-2868874.
STRING9606.ENSP00000323313.

PTM databases

PhosphoSiteQ14554.

Polymorphism databases

DMDM2501208.

Proteomic databases

MaxQBQ14554.
PaxDbQ14554.
PRIDEQ14554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316218; ENSP00000323313; ENSG00000065485.
GeneID10954.
KEGGhsa:10954.
UCSCuc003egc.2. human.

Organism-specific databases

CTD10954.
GeneCardsGC03P122785.
HGNCHGNC:24811. PDIA5.
HPAHPA030353.
HPA030354.
HPA030355.
HPA030356.
neXtProtNX_Q14554.
PharmGKBPA142671191.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000039967.
HOVERGENHBG053547.
InParanoidQ14554.
KOK09583.
OMAYYHYGKF.
PhylomeDBQ14554.
TreeFamTF106379.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ14554.
BgeeQ14554.
CleanExHS_PDIA5.
GenevestigatorQ14554.

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 3 hits.
[Graphical view]
SUPFAMSSF52833. SSF52833. 4 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDIA5. human.
GenomeRNAi10954.
NextBio41621.
PROQ14554.

Entry information

Entry namePDIA5_HUMAN
AccessionPrimary (citable) accession number: Q14554
Secondary accession number(s): D3DN95
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM