CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011990
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein disulfide-isomerase A2 
Protein Synonyms/Alias
 Pancreas-specific protein disulfide isomerase; PDIp 
Gene Name
 PDIA2 
Gene Synonyms/Alias
 PDIP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
479GRKVIEYKSTRDLETacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins. 
Sequence Annotation
 DOMAIN 27 152 Thioredoxin 1.
 DOMAIN 367 496 Thioredoxin 2.
 MOTIF 522 525 Prevents secretion from ER (Potential).
 ACT_SITE 71 71 Nucleophile (By similarity).
 ACT_SITE 74 74 Nucleophile (By similarity).
 ACT_SITE 418 418 Nucleophile (By similarity).
 ACT_SITE 421 421 Nucleophile (By similarity).
 CARBOHYD 127 127 N-linked (GlcNAc...).
 CARBOHYD 284 284 N-linked (GlcNAc...).
 CARBOHYD 516 516 N-linked (GlcNAc...).
 DISULFID 18 18 Interchain.
 DISULFID 71 74 Redox-active (By similarity).
 DISULFID 418 421 Redox-active (By similarity).  
Keyword
 Alternative splicing; Chaperone; Complete proteome; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase; Lipid-binding; Polymorphism; Redox-active center; Reference proteome; Repeat; Signal; Steroid-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 525 AA 
Protein Sequence
MSRQLLPVLL LLLLRASCPW GQEQGARSPS EEPPEEEIPK EDGILVLSRH TLGLALREHP 60
ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESMVVTLAKV DGPAQRELAE EFGVTEYPTL 120
KFFRNGNRTH PEEYTGPRDA EGIAEWLRRR VGPSAMRLED EAAAQALIGG RDLVVIGFFQ 180
DLQDEDVATF LALAQDALDM TFGLTDRPRL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL 240
GLDLGDLSRF LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLAGFGEA 300
APRFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV DGGPVTAASI 360
TAFCHAVLNG QVKPYLLSQE IPPDWDQRPV KTLVGKNFEQ VAFDETKNVF VKFYAPWCTH 420
CKEMAPAWEA LAEKYQDHED IIIAELDATA NELDAFAVHG FPTLKYFPAG PGRKVIEYKS 480
TRDLETFSKF LDNGGVLPTE EPPEEPAAPF PEPPANSTMG SKEEL 525 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:HGNC.
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0003756; F:protein disulfide isomerase activity; TAS:ProtInc.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
 GO:0097194; P:execution phase of apoptosis; IMP:BHF-UCL.
 GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
 GO:0006621; P:protein retention in ER lumen; TAS:ProtInc.
 GO:0034976; P:response to endoplasmic reticulum stress; IMP:BHF-UCL. 
Interpro
 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.