Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01308
Entry Name
UniProt Accession
Theoretical PI
4.76
Molecular Weight
57116.37
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Protein disulfide-isomerase
Protein Synonyms/Alias
PDI; 5.3.4.1; Cellular thyroid hormone-binding protein; Prolyl 4-hydroxylase subunit beta; p55;
Gene Name
P4HB
Gene Synonyms/Alias
ERBA2L; PDI; PDIA1; PO4DB;
Created Date
01-APR-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
8
Canonical
MLRRALLCLAVAALV
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
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.
Sequence Annotation
Domain: 18 134 Thioredoxin 1.
Domain: 349 475 Thioredoxin 2.
Motif: 505 508 Prevents secretion from ER.
Active site: 53 53 Nucleophile.
Active site: 56 56 Nucleophile.
Active site: 397 397 Nucleophile.
Active site: 400 400 Nucleophile.
Functional site: 54 54 Contributes to redox potential value.
Functional site: 55 55 Contributes to redox potential value.
Functional site: 120 120 Lowers pKa of C-terminal Cys of firstactive site.
Functional site: 398 398 Contributes to redox potential value.
Functional site: 399 399 Contributes to redox potential value.
Functional site: 461 461 Lowers pKa of C-terminal Cys of secondactive site.
Modified residue: 200 200 N6-acetyllysine.
Modified residue: 222 222 N6-succinyllysine.
Modified residue: 271 271 N6-succinyllysine.
Protein Length
508 AA.
Protein Sequence
(Canonical)
MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA PWCGHCKALA  60
PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP TIKFFRNGDT ASPKEYTAGR  120
EADDIVNWLK KRTGPAATTL PDGAAAESLV ESSEVAVIGF FKDVESDSAK QFLQAAEAID  180
DIPFGITSNS DVFSKYQLDK DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF  240
TEQTAPKIFG GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR  300
ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK IKPHLMSQEL  360
PEDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC KQLAPIWDKL GETYKDHENI  420
VIAKMDSTAN EVEAVKVHSF PTLKFFPASA DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD  480
DDDLEDLEEA EEPDMEEDDD QKAVKDEL                                     508
FASTA
(Canonical)
>LipidDB-9606-01308|P07237
MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALA
PEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGR
EADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAID
DIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEF
TEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQR
ILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQEL
PEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENI
VIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGD
DDDLEDLEEAEEPDMEEDDDQKAVKDEL
Gene Ontology
GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL
GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome
GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB
GO:0005576; C:extracellular region; NAS:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0016222; C:procollagen-proline 4-dioxygenase complex; IDA:MGI
GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB
GO:0004656; F:procollagen-proline 4-dioxygenase activity; TAS:ProtInc
GO:0003756; F:protein disulfide isomerase activity; IBA:RefGenome
GO:0045454; P:cell redox homeostasis; IEA:InterPro
GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL
GO:0030198; P:extracellular matrix organization; TAS:Reactome
GO:0042157; P:lipoprotein metabolic process; TAS:Reactome
GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:MGI
GO:0006457; P:protein folding; IBA:RefGenome
GO:1902175; P:regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL
GO:0034976; P:response to endoplasmic reticulum stress; IMP:BHF-UCL
GO:0044281; P:small molecule metabolic process; TAS:Reactome
Interpro
InterPro; IPR005788; Disulphide_isomerase
InterPro; IPR005792; Prot_disulphide_isomerase
InterPro; IPR012336; Thioredoxin-like_fold
InterPro; IPR017937; Thioredoxin_CS
InterPro; IPR013766; Thioredoxin_domain
Pfam
Pfam; PF00085; Thioredoxin;
SMART
PROSITE
PROSITE; PS00014; ER_TARGET;
PROSITE; PS00194; THIOREDOXIN_1;
PROSITE; PS51352; THIOREDOXIN_2;
PRINTS