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Protein

Protein disulfide-isomerase A5

Gene

PDIA5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

  • oxidoreductase activity Source: UniProtKB
  • protein disulfide isomerase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A5 (EC:5.3.4.1)
Alternative name(s):
Protein disulfide isomerase-related protein
Gene namesi
Name:PDIA5
Synonyms:PDIR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:24811. PDIA5.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671191.

Polymorphism and mutation databases

BioMutaiPDIA5.
DMDMi2501208.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 519498Protein disulfide-isomerase A5PRO_0000034233Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi182 ↔ 185Redox-activePROSITE-ProRule annotation
Disulfide bondi305 ↔ 308Redox-activePROSITE-ProRule annotation
Disulfide bondi426 ↔ 429Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ14554.
PaxDbiQ14554.
PRIDEiQ14554.

PTM databases

PhosphoSiteiQ14554.

Expressioni

Gene expression databases

BgeeiQ14554.
CleanExiHS_PDIA5.
ExpressionAtlasiQ14554. baseline and differential.
GenevisibleiQ14554. HS.

Organism-specific databases

HPAiHPA030353.
HPA030354.
HPA030355.
HPA030356.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KRTAP10-7P604093EBI-953879,EBI-10172290
MDFIQ997503EBI-953879,EBI-724076

Protein-protein interaction databases

BioGridi116154. 19 interactions.
IntActiQ14554. 14 interactions.
MINTiMINT-2868874.
STRINGi9606.ENSP00000323313.

Structurei

Secondary structure

1
519
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 4510Combined sources
Beta strandi47 – 5610Combined sources
Helixi57 – 7317Combined sources
Turni74 – 774Combined sources
Beta strandi79 – 846Combined sources
Helixi88 – 969Combined sources
Beta strandi108 – 1147Combined sources
Beta strandi117 – 1215Combined sources
Helixi128 – 1369Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I6XX-ray1.50A29-150[»]
ProteinModelPortaliQ14554.
SMRiQ14554. Positions 29-502.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 261128Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini270 – 384115Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST
Domaini378 – 506129Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi516 – 5194Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 3 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00730000110455.
HOGENOMiHOG000039967.
HOVERGENiHBG053547.
InParanoidiQ14554.
KOiK09583.
OMAiYYHYGKF.
OrthoDBiEOG74TWZ6.
PhylomeDBiQ14554.
TreeFamiTF106379.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14554-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARAGPAWLL LAIWVVLPSW LSSAKVSSLI ERISDPKDLK KLLRTRNNVL
60 70 80 90 100
VLYSKSEVAA ENHLRLLSTV AQAVKGQGTI CWVDCGDAES RKLCKKMKVD
110 120 130 140 150
LSPKDKKVEL FHYQDGAFHT EYNRAVTFKS IVAFLKDPKG PPLWEEDPGA
160 170 180 190 200
KDVVHLDSEK DFRRLLKKEE KPLLIMFYAP WCSMCKRMMP HFQKAATQLR
210 220 230 240 250
GHAVLAGMNV YSSEFENIKE EYSVRGFPTI CYFEKGRFLF QYDNYGSTAE
260 270 280 290 300
DIVEWLKNPQ PPQPQVPETP WADEGGSVYH LTDEDFDQFV KEHSSVLVMF
310 320 330 340 350
HAPWCGHCKK MKPEFEKAAE ALHGEADSSG VLAAVDATVN KALAERFHIS
360 370 380 390 400
EFPTLKYFKN GEKYAVPVLR TKKKFLEWMQ NPEAPPPPEP TWEEQQTSVL
410 420 430 440 450
HLVGDNFRET LKKKKHTLVM FYAPWCPHCK KVIPHFTATA DAFKDDRKIA
460 470 480 490 500
CAAVDCVKDK NQDLCQQEAV KGYPTFHYYH YGKFAEKYDS DRTELGFTNY
510
IRALREGDHE RLGKKKEEL
Length:519
Mass (Da):59,594
Last modified:November 1, 1997 - v1
Checksum:i6083FBEB8C019658
GO
Isoform 2 (identifier: Q14554-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     258-261: NPQP → KVWP
     262-518: Missing.

Note: No experimental confirmation available.
Show »
Length:262
Mass (Da):30,124
Checksum:i5F1F4564D9DB3955
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti391 – 3911T → M.
Corresponds to variant rs2292661 [ dbSNP | Ensembl ].
VAR_052581

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei258 – 2614NPQP → KVWP in isoform 2. 1 PublicationVSP_056536
Alternative sequencei262 – 518257Missing in isoform 2. 1 PublicationVSP_056537Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49490 mRNA. Translation: BAA08451.1.
AC063922 Genomic DNA. No translation available.
AC083797 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79452.1.
CH471052 Genomic DNA. Translation: EAW79453.1.
CH471052 Genomic DNA. Translation: EAW79454.1.
CH471052 Genomic DNA. Translation: EAW79456.1.
BC001625 mRNA. Translation: AAH01625.1.
CCDSiCCDS3020.1. [Q14554-1]
PIRiS66673.
RefSeqiNP_006801.1. NM_006810.3. [Q14554-1]
UniGeneiHs.477352.

Genome annotation databases

EnsembliENST00000316218; ENSP00000323313; ENSG00000065485.
ENST00000489923; ENSP00000417520; ENSG00000065485. [Q14554-2]
GeneIDi10954.
KEGGihsa:10954.
UCSCiuc003egc.2. human. [Q14554-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49490 mRNA. Translation: BAA08451.1.
AC063922 Genomic DNA. No translation available.
AC083797 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79452.1.
CH471052 Genomic DNA. Translation: EAW79453.1.
CH471052 Genomic DNA. Translation: EAW79454.1.
CH471052 Genomic DNA. Translation: EAW79456.1.
BC001625 mRNA. Translation: AAH01625.1.
CCDSiCCDS3020.1. [Q14554-1]
PIRiS66673.
RefSeqiNP_006801.1. NM_006810.3. [Q14554-1]
UniGeneiHs.477352.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I6XX-ray1.50A29-150[»]
ProteinModelPortaliQ14554.
SMRiQ14554. Positions 29-502.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116154. 19 interactions.
IntActiQ14554. 14 interactions.
MINTiMINT-2868874.
STRINGi9606.ENSP00000323313.

PTM databases

PhosphoSiteiQ14554.

Polymorphism and mutation databases

BioMutaiPDIA5.
DMDMi2501208.

Proteomic databases

MaxQBiQ14554.
PaxDbiQ14554.
PRIDEiQ14554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316218; ENSP00000323313; ENSG00000065485.
ENST00000489923; ENSP00000417520; ENSG00000065485. [Q14554-2]
GeneIDi10954.
KEGGihsa:10954.
UCSCiuc003egc.2. human. [Q14554-1]

Organism-specific databases

CTDi10954.
GeneCardsiGC03P122785.
HGNCiHGNC:24811. PDIA5.
HPAiHPA030353.
HPA030354.
HPA030355.
HPA030356.
neXtProtiNX_Q14554.
PharmGKBiPA142671191.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00730000110455.
HOGENOMiHOG000039967.
HOVERGENiHBG053547.
InParanoidiQ14554.
KOiK09583.
OMAiYYHYGKF.
OrthoDBiEOG74TWZ6.
PhylomeDBiQ14554.
TreeFamiTF106379.

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSiPDIA5. human.
GenomeRNAii10954.
NextBioi41621.
PROiQ14554.

Gene expression databases

BgeeiQ14554.
CleanExiHS_PDIA5.
ExpressionAtlasiQ14554. baseline and differential.
GenevisibleiQ14554. HS.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lung.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPDIA5_HUMAN
AccessioniPrimary (citable) accession number: Q14554
Secondary accession number(s): D3DN95, Q9BV43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 22, 2015
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.