P4HA1
{{Short description|Protein-coding gene in the species Homo sapiens}}
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Prolyl 4-hydroxylase subunit alpha-1 is an enzyme that in humans is encoded by the P4HA1 gene.{{cite journal | vauthors = Pajunen L, Jones TA, Helaakoski T, Pihlajaniemi T, Solomon E, Sheer D, Kivirikko KI | title = Assignment of the gene coding for the alpha-subunit of prolyl 4-hydroxylase to human chromosome region 10q21.3-23.1 | journal = Am J Hum Genet | volume = 45 | issue = 6 | pages = 829–34 |date=Jan 1990 | pmid = 2556027 | pmc = 1683466 }}{{cite web | title = Entrez Gene: P4HA1 procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide I| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5033}}
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.
References
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Further reading
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- {{cite journal |vauthors=Helaakoski T, Vuori K, Myllylä R, etal |title=Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 12 |pages= 4392–6 |year= 1989 |pmid= 2543975 |doi= 10.1073/pnas.86.12.4392| pmc=287275 |doi-access=free |bibcode=1989PNAS...86.4392H }}
- {{cite journal |vauthors=Helaakoski T, Veijola J, Vuori K, etal |title=Structure and expression of the human gene for the alpha subunit of prolyl 4-hydroxylase. The two alternatively spliced types of mRNA correspond to two homologous exons the sequences of which are expressed in a variety of tissues. |journal=J. Biol. Chem. |volume=269 |issue= 45 |pages= 27847–54 |year= 1994 |doi=10.1016/S0021-9258(18)46864-0 |pmid= 7961714 |doi-access=free }}
- {{cite journal | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
- {{cite journal |vauthors=Annunen P, Helaakoski T, Myllyharju J, etal |title=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. |journal=J. Biol. Chem. |volume=272 |issue= 28 |pages= 17342–8 |year= 1997 |pmid= 9211872 |doi=10.1074/jbc.272.28.17342 |doi-access=free }}
- {{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
- {{cite journal |vauthors=Horelli-Kuitunen N, Kvist AP, Helaakoski T, etal |title=The order and transcriptional orientation of the human COL13A1 and P4HA genes on chromosome 10 long arm determined by high-resolution FISH. |journal=Genomics |volume=46 |issue= 2 |pages= 299–302 |year= 1998 |pmid= 9417920 |doi= 10.1006/geno.1997.5015 }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
- {{cite journal |vauthors=Deloukas P, Earthrowl ME, Grafham DV, etal |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375–81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 |bibcode=2004Natur.429..375D |doi-access= free }}
- {{cite journal |vauthors=Raveendran M, Senthil D, Utama B, etal |title=Cigarette suppresses the expression of P4Halpha and vascular collagen production. |journal=Biochem. Biophys. Res. Commun. |volume=323 |issue= 2 |pages= 592–8 |year= 2004 |pmid= 15369792 |doi= 10.1016/j.bbrc.2004.08.129 }}
- {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
- {{cite journal |vauthors=Fähling M, Mrowka R, Steege A, etal |title=Heterogeneous nuclear ribonucleoprotein-A2/B1 modulate collagen prolyl 4-hydroxylase, alpha (I) mRNA stability. |journal=J. Biol. Chem. |volume=281 |issue= 14 |pages= 9279–86 |year= 2006 |pmid= 16464861 |doi= 10.1074/jbc.M510925200 |doi-access= free }}
- {{cite journal |vauthors=Chen L, Shen YH, Wang X, etal |title=Human prolyl-4-hydroxylase alpha(I) transcription is mediated by upstream stimulatory factors. |journal=J. Biol. Chem. |volume=281 |issue= 16 |pages= 10849–55 |year= 2006 |pmid= 16488890 |doi= 10.1074/jbc.M511237200 | pmc=2819823 |doi-access=free }}
- {{cite journal |vauthors=Fähling M, Mrowka R, Steege A, etal |title=Translational control of collagen prolyl 4-hydroxylase-alpha(I) gene expression under hypoxia. |journal=J. Biol. Chem. |volume=281 |issue= 36 |pages= 26089–101 |year= 2006 |pmid= 16837461 |doi= 10.1074/jbc.M604939200 |doi-access= free }}
- {{cite journal |vauthors=Grimmer C, Balbus N, Lang U, etal |title=Regulation of type II collagen synthesis during osteoarthritis by prolyl-4-hydroxylases: possible influence of low oxygen levels. |journal=Am. J. Pathol. |volume=169 |issue= 2 |pages= 491–502 |year= 2006 |pmid= 16877351 |doi= 10.2353/ajpath.2006.050738| pmc=1698781 }}
- {{cite journal | vauthors=Koivunen P, Hirsilä M, Kivirikko KI, Myllyharju J |title=The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases. |journal=J. Biol. Chem. |volume=281 |issue= 39 |pages= 28712–20 |year= 2006 |pmid= 16885164 |doi= 10.1074/jbc.M604628200 |doi-access= free }}
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