UniProt Accession

 PDIA1_MOUSE; P09103; Q922C8 

Genbank Protein ID

 X06453; J05185; AK150002; AK150422; AK150805; AK152141; AK152217; AK159606; AK159965; AK168330; AK168893; AK170603; AL663030; BC008549; BC093512 

Genbank Nucleotide ID

 CAA29759.1; AAA39906.1; BAE29230.1; BAE29545.1; BAE29868.1; BAE30979.1; BAE31045.1; BAE35225.1; BAE35520.1; BAE40268.1; BAE40710.1; BAE41907.1; CAM27084.1; AAH08549.1; AAH93512.1 

Protein Name

 Protein disulfide-isomerase 

Protein Synonyms/Alias

 PDI; Cellular thyroid hormone-binding protein; Endoplasmic reticulum resident protein 59; ER protein 59; ERp59; Prolyl 4-hydroxylase subunit beta; p55 

Gene Name

 P4hb 

Gene Synonyms/Alias

 Pdia1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
33	DNVLVLKKSNFEEAL	ubiquitination	[1]
67	ALAPEYAKAAAKLKA	acetylation	[2, 3, 4]
67	ALAPEYAKAAAKLKA	succinylation	[3]
67	ALAPEYAKAAAKLKA	ubiquitination	[1]
83	GSEIRLAKVDATEES	acetylation	[4]
83	GSEIRLAKVDATEES	ubiquitination	[1]
105	VRGYPTIKFFKNGDT	acetylation	[2]
108	YPTIKFFKNGDTASP	acetylation	[2]
108	YPTIKFFKNGDTASP	ubiquitination	[1]
132	DDIVNWLKKRTGPAA	acetylation	[2, 3]
132	DDIVNWLKKRTGPAA	succinylation	[3]
132	DDIVNWLKKRTGPAA	ubiquitination	[1]
202	FSKYQLDKDGVVLFK	acetylation	[2, 3, 5]
202	FSKYQLDKDGVVLFK	succinylation	[3]
202	FSKYQLDKDGVVLFK	ubiquitination	[1]
209	KDGVVLFKKFDEGRN	acetylation	[2, 4]
224	NFEGEITKEKLLDFI	acetylation	[2, 3, 4, 5, 6]
224	NFEGEITKEKLLDFI	succinylation	[3]
226	EGEITKEKLLDFIKH	ubiquitination	[1]
232	EKLLDFIKHNQLPLV	acetylation	[2]
265	HILLFLPKSVSDYDG	acetylation	[4]
273	SVSDYDGKLSSFKRA	acetylation	[2, 3, 4, 5, 7]
273	SVSDYDGKLSSFKRA	succinylation	[3]
273	SVSDYDGKLSSFKRA	ubiquitination	[1]
278	DGKLSSFKRAAEGFK	acetylation	[2, 8]
310	ILEFFGLKKEECPAV	ubiquitination	[1]
311	LEFFGLKKEECPAVR	acetylation	[2]
328	TLEEEMTKYKPESDE	acetylation	[2, 4]
330	EEEMTKYKPESDELT	acetylation	[2, 4, 5]
340	SDELTAEKITEFCHR	acetylation	[2, 4]
354	RFLEGKIKPHLMSQE	acetylation	[2, 5]
368	EVPEDWDKQPVKVLV	acetylation	[2, 3]
387	EEVAFDEKKNVFVEF	acetylation	[2, 3]
387	EEVAFDEKKNVFVEF	ubiquitination	[1]
411	QLAPIWDKLGETYKD	acetylation	[5]
417	DKLGETYKDHENIII	acetylation	[5]
446	VHSFPTLKFFPASAD	acetylation	[5]
446	VHSFPTLKFFPASAD	ubiquitination	[1]
469	ERTLDGFKKFLESGG	acetylation	[5]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [8] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 

Functional Description

 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). 

Sequence Annotation

 DOMAIN 20 136 Thioredoxin 1.
 DOMAIN 348 477 Thioredoxin 2.
 MOTIF 506 509 Prevents secretion from ER.
 ACT_SITE 55 55 Nucleophile (By similarity).
 ACT_SITE 58 58 Nucleophile (By similarity).
 ACT_SITE 399 399 Nucleophile (By similarity).
 ACT_SITE 402 402 Nucleophile (By similarity).
 DISULFID 55 58 Redox-active (By similarity).
 DISULFID 399 402 Redox-active (By similarity).  

Keyword

 Cell membrane; Chaperone; Complete proteome; Disulfide bond; Endoplasmic reticulum; Isomerase; Membrane; Redox-active center; Reference proteome; Repeat; Signal. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 509 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; IEA:Compara.
 GO:0005783; C:endoplasmic reticulum; IDA:MGI.
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0004656; F:procollagen-proline 4-dioxygenase activity; ISO:MGI.
 GO:0003756; F:protein disulfide isomerase activity; IEA:EC.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
 GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; ISO:MGI.
 GO:0006457; P:protein folding; IEA:GOC. 

Interpro

 IPR005788; Disulphide_isomerase.
 IPR005792; Prot_disulphide_isomerase.
 IPR005746; Thioredoxin.
 IPR012336; Thioredoxin-like_fold.
 IPR017937; Thioredoxin_CS.
 IPR013766; Thioredoxin_domain. 

Pfam

 PF00085; Thioredoxin 

SMART

  

PROSITE

 PS00014; ER_TARGET
 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 

PRINTS

 PR00421; THIOREDOXIN.