Names & Taxonomy

Uniprot ID:
P07237
Entry Name:
PDIA1_HUMAN
Status:
reviewed
Protein Names:
Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Cellular thyroid hormone-binding protein) (Prolyl 4-hydroxylase subunit beta) (p55)
Gene Names:
P4HB ERBA2L PDI PDIA1 PO4DB
Gene Names Primary:
P4HB
Organism:
Homo sapiens (Human)

Structure

Length:
508
Sequence:
MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Endoplasmic reticulum

Function

Function:
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. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).
Catalytic Activity:
Catalyzes the rearrangement of -S-S- bonds in proteins.
Active Site:
ACT_SITE 53 53 Nucleophile.; ACT_SITE 56 56 Nucleophile.; ACT_SITE 397 397 Nucleophile.
Cross Reference Drug Bank:
DB03615
Gene Ontology Go:
endoplasmic reticulum
endoplasmic reticulum chaperone complex
endoplasmic reticulum lumen
endoplasmic reticulum-Golgi intermediate compartment
external side of plasma membrane
extracellular exosome
extracellular region
focal adhesion
melanosome
procollagen-proline 4-dioxygenase complex
endopeptidase activity
integrin binding
poly(A) RNA binding
procollagen-proline 4-dioxygenase activity
protein disulfide isomerase activity
protein heterodimerization activity
cell redox homeostasis
cellular response to hypoxia
extracellular matrix organization
lipoprotein metabolic process
peptidyl-proline hydroxylation to 4-hydroxy-L-proline
positive regulation of viral entry into host cell
proteolysis
regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
response to endoplasmic reticulum stress
response to reactive oxygen species
small molecule metabolic process
Gene Ontology Biological Process:
cell redox homeostasis
cellular response to hypoxia
extracellular matrix organization
lipoprotein metabolic process
peptidyl-proline hydroxylation to 4-hydroxy-L-proline
positive regulation of viral entry into host cell
proteolysis
regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
response to endoplasmic reticulum stress
response to reactive oxygen species
small molecule metabolic process
Gene Ontology Molecular Function:
endopeptidase activity
integrin binding
poly(A) RNA binding
procollagen-proline 4-dioxygenase activity
protein disulfide isomerase activity
protein heterodimerization activity
Gene Ontology Cellular Component:
endoplasmic reticulum
endoplasmic reticulum chaperone complex
endoplasmic reticulum-Golgi intermediate compartment
endoplasmic reticulum lumen
external side of plasma membrane
extracellular exosome
extracellular region
focal adhesion
melanosome
procollagen-proline 4-dioxygenase complex
Keywords:
3D-structure
Acetylation
Cell membrane
Chaperone
Complete proteome
Craniosynostosis
Direct protein sequencing
Disease mutation
Disulfide bond
Endoplasmic reticulum
Isomerase
Membrane
Osteogenesis imperfecta
Phosphoprotein
Redox-active center
Reference proteome
Repeat
Signal
Interacts With:
Q96HE7; Q8TCT9; Q13162; Q03518

Publication

PubMed ID:
3034602 3611107 2846539 14702039 15489334 1597478 9150948 12665801 2079031 1286669 9399589 3342239 1699755 10636893 11707400 11181151 12485997 12095988 12218051 12218052 12643545 15158710 14592831 15644496 17081065 21269460 21670307 23475612 24275569 26091039 25683117 26224785 25944712 8580850 8672469 10383197