Protein disulfide-isomerase

Details

Name
Protein disulfide-isomerase
Synonyms
  • 5.3.4.1
  • Cellular thyroid hormone-binding protein
  • ERBA2L
  • p55
  • PDI
  • PDIA1
  • PO4DB
  • Prolyl 4-hydroxylase subunit beta
Gene Name
P4HB
Organism
Humans
Amino acid sequence
>lcl|BSEQ0019291|Protein disulfide-isomerase
MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALA
PEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGR
EADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAID
DIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEF
TEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQR
ILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQEL
PEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENI
VIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGD
DDDLEDLEEAEEPDMEEDDDQKAVKDEL
Number of residues
508
Molecular Weight
57115.795
Theoretical pI
4.49
GO Classification
Functions
endopeptidase activity / integrin binding / poly(A) RNA binding / procollagen-proline 4-dioxygenase activity / protein disulfide isomerase activity / protein heterodimerization activity
Processes
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 / protein folding / proteolysis / regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / response to endoplasmic reticulum stress / response to reactive oxygen species / small molecule metabolic process
Components
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
General Function
Protein heterodimerization activity
Specific 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).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Endoplasmic reticulum
Gene sequence
>lcl|BSEQ0019292|Protein disulfide-isomerase (P4HB)
ATGCTGCGCCGCGCTCTGCTGTGCCTGGCCGTGGCCGCCCTGGTGCGCGCCGACGCCCCC
GAGGAGGAGGACCACGTCCTGGTGCTGCGGAAAAGCAACTTCGCGGAGGCGCTGGCGGCC
CACAAGTACCTGCTGGTGGAGTTCTATGCCCCTTGGTGTGGCCACTGCAAGGCTCTGGCC
CCTGAGTATGCCAAAGCCGCTGGGAAGCTGAAGGCAGAAGGTTCCGAGATCAGGTTGGCC
AAGGTGGACGCCACGGAGGAGTCTGACCTGGCCCAGCAGTACGGCGTGCGCGGCTATCCC
ACCATCAAGTTCTTCAGGAATGGAGACACGGCTTCCCCCAAGGAATATACAGCTGGCAGA
GAGGCTGATGACATCGTGAACTGGCTGAAGAAGCGCACGGGCCCGGCTGCCACCACCCTG
CCTGACGGCGCAGCTGCAGAGTCCTTGGTGGAGTCCAGCGAGGTGGCTGTCATCGGCTTC
TTCAAGGACGTGGAGTCGGACTCTGCCAAGCAGTTTTTGCAGGCAGCAGAGGCCATCGAT
GACATACCATTTGGGATCACTTCCAACAGTGACGTGTTCTCCAAATACCAGCTCGACAAA
GATGGGGTTGTCCTCTTTAAGAAGTTTGATGAAGGCCGGAACAACTTTGAAGGGGAGGTC
ACCAAGGAGAACCTGCTGGACTTTATCAAACACAACCAGCTGCCCCTTGTCATCGAGTTC
ACCGAGCAGACAGCCCCGAAGATTTTTGGAGGTGAAATCAAGACTCACATCCTGCTGTTC
TTGCCCAAGAGTGTGTCTGACTATGACGGCAAACTGAGCAACTTCAAAACAGCAGCCGAG
AGCTTCAAGGGCAAGATCCTGTTCATCTTCATCGACAGCGACCACACCGACAACCAGCGC
ATCCTCGAGTTCTTTGGCCTGAAGAAGGAAGAGTGCCCGGCCGTGCGCCTCATCACCCTG
GAGGAGGAGATGACCAAGTACAAGCCCGAATCGGAGGAGCTGACGGCAGAGAGGATCACA
GAGTTCTGCCACCGCTTCCTGGAGGGCAAAATCAAGCCCCACCTGATGAGCCAGGAGCTG
CCGGAGGACTGGGACAAGCAGCCTGTCAAGGTGCTTGTTGGGAAGAACTTTGAAGACGTG
GCTTTTGATGAGAAAAAAAACGTCTTTGTGGAGTTCTATGCCCCATGGTGTGGTCACTGC
AAACAGTTGGCTCCCATTTGGGATAAACTGGGAGAGACGTACAAGGACCATGAGAACATC
GTCATCGCCAAGATGGACTCGACTGCCAACGAGGTGGAGGCCGTCAAAGTGCACAGCTTC
CCCACACTCAAGTTCTTTCCTGCCAGTGCCGACAGGACGGTCATTGATTACAACGGGGAA
CGCACGCTGGATGGTTTTAAGAAATTCCTGGAGAGCGGTGGCCAGGATGGGGCAGGGGAT
GATGACGATCTCGAGGACCTGGAAGAAGCAGAGGAGCCAGACATGGAGGAAGACGATGAT
CAGAAAGCTGTGAAAGATGAACTGTAA
Chromosome Location
17
Locus
17q25
External Identifiers
ResourceLink
UniProtKB IDP07237
UniProtKB Entry NamePDIA1_HUMAN
GenBank Gene IDX05130
GenAtlas IDP4HB
HGNC IDHGNC:8548
General References
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  14. Mezghrani A, Courageot J, Mani JC, Pugniere M, Bastiani P, Miquelis R: Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent thyroglobulin/PDI interactions determine a novel PDI function in the post-endoplasmic reticulum of thyrocytes. J Biol Chem. 2000 Jan 21;275(3):1920-9. [PubMed:10636893]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03615Ribostamycinapproved, experimentalunknownDetails
DB09130Copperapproved, investigationalunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB11638Artenimolexperimental, investigationalunknownligandDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownDetails