CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008862
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein disulfide-isomerase 
Protein Synonyms/Alias
 PDI; dPDI 
Gene Name
 Pdi 
Gene Synonyms/Alias
 CG6988 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
68ALAPEYAKAAQQLAEacetylation[1]
76AAQQLAEKESPIKLAacetylation[1]
106VRGYPTLKFFRSGSPacetylation[1]
170DLESEEAKTFTKVANacetylation[1]
270REGGHIEKYVDPLKEacetylation[1]
444ISSFPTIKYFRKEDNacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702] 
Functional Description
 Participates in the folding of proteins containing disulfide bonds (By similarity). 
Sequence Annotation
 DOMAIN 19 134 Thioredoxin 1.
 DOMAIN 349 474 Thioredoxin 2.
 MOTIF 493 496 Prevents secretion from ER.
 ACT_SITE 56 56 Nucleophile (By similarity).
 ACT_SITE 59 59 Nucleophile (By similarity).
 ACT_SITE 397 397 Nucleophile (By similarity).
 ACT_SITE 400 400 Nucleophile (By similarity).
 DISULFID 56 59 Redox-active (By similarity).
 DISULFID 397 400 Redox-active (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center; Reference proteome; Repeat; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 496 AA 
Protein Sequence
MKFLICALFL AASYVAASAE AEVKVEEGVL VATVDNFKQL IADNEFVLVE FYAPWCGHCK 60
ALAPEYAKAA QQLAEKESPI KLAKVDATVE GELAEQYAVR GYPTLKFFRS GSPVEYSGGR 120
QAADIIAWVT KKTGPPAKDL TSVADAEQFL KDNEIAIIGF FKDLESEEAK TFTKVANALD 180
SFVFGVSSNA DVIAKYEAKD NGVVLFKPFD DKKSVFEGEL NEENLKKFAQ VQSLPLIVDF 240
NHESASKIFG GSIKSHLLFF VSREGGHIEK YVDPLKEIAK KYRDDILFVT ISSDEEDHTR 300
IFEFFGMNKE EVPTIRLIKL EEDMAKYKPE SDDLSAETIE AFLKKFLDGK LKQHLLSQEL 360
PEDWDKNPVK VLVSSNFESV ALDKSKSVLV EFYAPWCGHC KQLAPIYDQL AEKYKDNEDI 420
VIAKMDSTAN ELESIKISSF PTIKYFRKED NKVIDFNLDR TLDDFVKFLD ANGEVADSEP 480
VEETEEEEEA PKKDEL 496 
Gene Ontology
 GO:0060187; C:cell pole; IDA:FlyBase.
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0005615; C:extracellular space; IDA:FlyBase.
 GO:0045169; C:fusome; IDA:FlyBase.
 GO:0005811; C:lipid particle; IDA:FlyBase.
 GO:0043025; C:neuronal cell body; IDA:FlyBase.
 GO:0005635; C:nuclear envelope; IDA:FlyBase.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
 GO:0005791; C:rough endoplasmic reticulum; IDA:FlyBase.
 GO:0070732; C:spindle envelope; IDA:FlyBase.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 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: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.