P4HB

From Wikipedia, the free encyclopedia

Procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide

PDB rendering based on 1bjx.

Available structures: 1bjx, 1mek, 1x5c, 2bjx

Identifiers

Symbol(s)

P4HB; DSI; ERBA2L; GIT; PDI; PDIA1; PHDB; PO4DB; PO4HB; PROHB

External IDs

OMIM: 176790 MGI: 97464 HomoloGene: 55495

Gene ontology
Molecular Function:	• protein disulfide isomerase activity • procollagen-proline 4-dioxygenase activity • protein binding • electron carrier activity • protein disulfide oxidoreductase activity • isomerase activity
Cellular Component:	• extracellular region • endoplasmic reticulum • microsome • ER-Golgi intermediate compartment • cell surface • membrane
Biological Process:	• protein folding • peptidyl-proline hydroxylation to 4-hydroxy-L-proline • cell redox homeostasis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000918 (mRNA)
NP_000909 (protein)

NM_011032 (mRNA)
NP_035162 (protein)

Location

Chr 17: 77.39 - 77.41 Mb

Chr 11: 120.38 - 120.39 Mb

Pubmed search

[1]

[2]

Procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide, also known as P4HB, is a human gene.^[1]

This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex.^[1]

[edit] References

^ ^a ^b Entrez Gene: P4HB procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide.

[edit] Further reading

Pihlajaniemi T, Myllylä R, Kivirikko KI (1992). "Prolyl 4-hydroxylase and its role in collagen synthesis.". J. Hepatol. 13 Suppl 3: S2–7. PMID 1667665.
Wilkinson B, Gilbert HF (2004). "Protein disulfide isomerase.". Biochim. Biophys. Acta 1699 (1-2): 35–44. doi:10.1016/j.bbapap.2004.02.017. PMID 15158710.
Hochstrasser DF, Frutiger S, Paquet N, et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison.". Electrophoresis 13 (12): 992–1001. PMID 1286669.
Chessler SD, Byers PH (1992). "Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern.". J. Biol. Chem. 267 (11): 7751–7. PMID 1339453.
Vuori K, Myllylä R, Pihlajaniemi T, Kivirikko KI (1992). "Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity.". J. Biol. Chem. 267 (11): 7211–4. PMID 1559965.
Tasanen K, Oikarinen J, Kivirikko KI, Pihlajaniemi T (1992). "Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements.". J. Biol. Chem. 267 (16): 11513–9. PMID 1597478.
Bauw G, Rasmussen HH, van den Bulcke M, et al. (1990). "Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes.". Electrophoresis 11 (7): 528–36. doi:10.1002/elps.1150110703. PMID 1699755.
Ward LD, Hong J, Whitehead RH, Simpson RJ (1991). "Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis.". Electrophoresis 11 (10): 883–91. doi:10.1002/elps.1150111019. PMID 2079031.
Tasanen K, Parkkonen T, Chow LT, et al. (1988). "Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase.". J. Biol. Chem. 263 (31): 16218–24. PMID 2846539.
Koivu J, Myllylä R, Helaakoski T, et al. (1987). "A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase.". J. Biol. Chem. 262 (14): 6447–9. PMID 3032969.
Pihlajaniemi T, Helaakoski T, Tasanen K, et al. (1987). "Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene.". EMBO J. 6 (3): 643–9. PMID 3034602.
Morris JI, Varandani PT (1988). "Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase).". Biochim. Biophys. Acta 949 (2): 169–80. PMID 3342239.
Gosden JR, Middleton PG, Rout D, De Angelis C (1987). "Chromosomal localization of the human oncogene ERBA2.". Cytogenet. Cell Genet. 43 (3-4): 150–3. PMID 3467900.
Cheng SY, Gong QH, Parkison C, et al. (1987). "The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum.". J. Biol. Chem. 262 (23): 11221–7. PMID 3611107.
Helaakoski T, Annunen P, Vuori K, et al. (1995). "Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit.". Proc. Natl. Acad. Sci. U.S.A. 92 (10): 4427–31. PMID 7753822.
Shoulders CC, Brett DJ, Bayliss JD, et al. (1994). "Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein.". Hum. Mol. Genet. 2 (12): 2109–16. PMID 8111381.
Kemmink J, Darby NJ, Dijkstra K, et al. (1996). "Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase.". Protein Sci. 4 (12): 2587–93. PMID 8580850.
Kemmink J, Darby NJ, Dijkstra K, et al. (1996). "Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.". Biochemistry 35 (24): 7684–91. doi:10.1021/bi960335m. PMID 8672469.
Ji H, Reid GE, Moritz RL, et al. (1997). "A two-dimensional gel database of human colon carcinoma proteins.". Electrophoresis 18 (3-4): 605–13. doi:10.1002/elps.1150180344. PMID 9150948.