CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018663
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein disulfide-isomerase A5 
Protein Synonyms/Alias
 Protein disulfide isomerase-related protein 
Gene Name
 Pdia5 
Gene Synonyms/Alias
 Pdir 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
96RKLCKKMKVDLSPKDacetylation[1]
134KSIVAFLKDPKGPPLacetylation[1]
137VAFLKDPKGPPLWEEacetylation[2]
192RIMPHFQKAATQVRGacetylation[1]
233PTICYFEKGRFLFPYacetylation[1]
446DAFKEDRKIACAAVDacetylation[1]
458AVDCVKDKNQDLCQQacetylation[3]
485HYGKLVEKYESDRTEacetylation[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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
Functional Description
  
Sequence Annotation
 DOMAIN 132 259 Thioredoxin 1.
 DOMAIN 268 382 Thioredoxin 2.
 DOMAIN 376 504 Thioredoxin 3.
 MOTIF 514 517 Prevents secretion from ER (Potential).
 DISULFID 180 183 Redox-active (By similarity).
 DISULFID 303 306 Redox-active (By similarity).
 DISULFID 424 427 Redox-active (By similarity).  
Keyword
 Complete proteome; Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center; Reference proteome; Repeat; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 517 AA 
Protein Sequence
MARAWGLLLA IGVVLPTWLS STKVSSLIER ISDPKDLKKL LRTRNNVLVL YSESEVAAES 60
HLKLLSTVAQ AVKGQGTVCW VDCGDAESRK LCKKMKVDLS PKDKKIELFH YQDGAFHMQY 120
DRAVTLKSIV AFLKDPKGPP LWEEDPGAKD VVHIDSEKDF RRLLKREEKP LLMMFYAPWC 180
SMCKRIMPHF QKAATQVRGH IVLAGMNVYP SEFENIKEEY NVRGYPTICY FEKGRFLFPY 240
ENYGSTAEDI VEWLKNPLPP QPQVPETPWA DEGGSVYHLT DEDFDQFVKE HSSVLVMFHA 300
PWCGHCKKMK PEFESAAEVL HGDAESSGVL AAVDATVNEA LAGRFHISAF PTLKYFKNGE 360
QQAVPALRTK KKFIEWMQNP EAPPPPEPTW EEQQTSVLHL VGDNFRDTLK KKKHTLVMFY 420
APWCPHCKKV IPHFTATADA FKEDRKIACA AVDCVKDKNQ DLCQQEAVKA YPTFHYYHYG 480
KLVEKYESDR TELGFTSFIR TLREGDLKRL EKRREEL 517 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 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.
 GO:0006950; P:response to stress; IDA:UniProtKB. 
Interpro
 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.