UniProt Accession

 PDIA1_RAT; P04785; P13700 

Genbank Protein ID

 M21018; BC061857; X02918; M21476 

Genbank Nucleotide ID

 AAA40620.1; AAH61857.1; CAA26675.1; AAA40619.1 

Protein Name

 Protein disulfide-isomerase 

Protein Synonyms/Alias

 PDI; Cellular thyroid hormone-binding protein; Prolyl 4-hydroxylase subunit beta 

Gene Name

 P4hb 

Gene Synonyms/Alias

 Pdia1 

Created Date

 July 27, 2013 

Organism

 Rattus norvegicus (Rat) 

NCBI Taxa ID

 10116 

Lysine Modification

Position	Peptide	Type	References
67	ALAPEYAKAAAKLKA	acetylation	[1]
73	AKAAAKLKAEGSEIR	acetylation	[1]
83	GSEIRLAKVDATEES	acetylation	[1]
105	VRGYPTIKFFKNGDT	acetylation	[1]
108	YPTIKFFKNGDTASP	acetylation	[1]
132	DDIVNWLKKRTGPAA	acetylation	[1]
202	FSKYQLDKDGVVLFK	acetylation	[1]
210	DGVVLFKKFDEGRNN	acetylation	[1]
224	NFEGEITKEKLLDFI	acetylation	[1]
226	EGEITKEKLLDFIKH	acetylation	[1]
273	SVSDYDGKLSNFKKA	acetylation	[1]
278	DGKLSNFKKAAEGFK	acetylation	[1]
310	ILEFFGLKKEECPAV	acetylation	[1]
328	TLEEEMTKYKPESDE	acetylation	[1]
330	EEEMTKYKPESDELT	acetylation	[1]
354	HFLEGKIKPHLMSQE	acetylation	[1]
368	ELPEDWDKQPVKVLV	acetylation	[1]
377	PVKVLVGKNFEEVAF	acetylation	[1]
387	EEVAFDEKKNVFVEF	acetylation	[1]
411	QLAPIWDKLGETYKD	acetylation	[1]
438	ANEVEAVKVHSFPTL	acetylation	[1]
469	ERTLDGFKKFLESGG	acetylation	[1]

Reference

 [1] 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 335 477 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; Direct protein sequencing; 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: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; IEA:Compara.
 GO:0003756; F:protein disulfide isomerase activity; IMP:RGD.
 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; IEA:Compara. 

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.