P4HA2

From Wikipedia, the free encyclopedia

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

Identifiers

P4HA2; 4-PH alpha 2

External IDs

OMIM: 600608 MGI: 894286 HomoloGene: 55806

Gene ontology
Molecular Function:	• procollagen-proline 4-dioxygenase activity • iron ion binding • protein binding • electron carrier activity • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors • L-ascorbic acid binding • metal ion binding
Cellular Component:	• endoplasmic reticulum
Biological Process:	• peptidyl-proline hydroxylation to 4-hydroxy-L-proline • protein metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001017973 (mRNA)
NP_001017973 (protein)

NM_011031 (mRNA)
NP_035161 (protein)

Location

Chr 5: 131.56 - 131.59 Mb

Chr 11: 53.94 - 53.98 Mb

Pubmed search

[1]

[2]

Procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide II, also known as P4HA2, is a human gene.^[1]

This gene encodes a component of prolyl 4-hydroxylase, a key enzyme in collagen synthesis composed of two identical alpha subunits and two beta subunits. The encoded protein is one of several different types of alpha subunits and provides the major part of the catalytic site of the active enzyme. In collagen and related proteins, prolyl 4-hydroxylase catalyzes the formation of 4-hydroxyproline that is essential to the proper three-dimensional folding of newly synthesized procollagen chains. Alternatively spliced transcript variants encoding different isoforms have been described.^[1]

[edit] References

^ ^a ^b Entrez Gene: P4HA2 procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide II.

[edit] Further reading

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.
Annunen P, Helaakoski T, Myllyharju J, et al. (1997). "Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer.". J. Biol. Chem. 272 (28): 17342–8. PMID 9211872.
Nokelainen M, Nissi R, Kukkola L, et al. (2001). "Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues.". Eur. J. Biochem. 268 (20): 5300–9. PMID 11606192.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Hieta R, Kukkola L, Permi P, et al. (2003). "The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides.". J. Biol. Chem. 278 (37): 34966–74. doi:10.1074/jbc.M303624200. PMID 12824157.
Kukkola L, Hieta R, Kivirikko KI, Myllyharju J (2004). "Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme.". J. Biol. Chem. 278 (48): 47685–93. doi:10.1074/jbc.M306806200. PMID 14500733.
Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region.". Genomics 83 (1): 153–67. PMID 14667819.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
Grimmer C, Balbus N, Lang U, et al. (2006). "Regulation of type II collagen synthesis during osteoarthritis by prolyl-4-hydroxylases: possible influence of low oxygen levels.". Am. J. Pathol. 169 (2): 491–502. PMID 16877351.
Koivunen P, Hirsilä M, Kivirikko KI, Myllyharju J (2006). "The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases.". J. Biol. Chem. 281 (39): 28712–20. doi:10.1074/jbc.M604628200. PMID 16885164.
Teodoro JG, Parker AE, Zhu X, Green MR (2006). "p53-mediated inhibition of angiogenesis through up-regulation of a collagen prolyl hydroxylase.". Science 313 (5789): 968–71. doi:10.1126/science.1126391. PMID 16917063.