P4HA1

P4HA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1TJC, 2V5F, 2YQ8, 4BT8, 4BT9, 4BTA, 4BTB
Identifiers
Aliases	P4HA1, P4HA, prolyl 4-hydroxylase subunit alpha 1
External IDs	OMIM: 176710; MGI: 97463; HomoloGene: 30998; GeneCards: P4HA1; OMA:P4HA1 - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10q22.1 Start 73,007,217 bp End 73,096,974 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 B4 Start 59,159,118 bp End 59,209,126 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cartilage tissue Achilles tendon tibia ventricular zone pericardium stromal cell of endometrium periodontal fiber gastrocnemius muscle tibialis anterior muscle triceps brachii muscle Top expressed in calvaria epithelium of lens stroma of bone marrow right lung lobe dermis body of femur cumulus cell sciatic nerve yolk sac umbilical cord More reference expression data BioGPS More reference expression data
Gene ontology Molecular function iron ion binding L-ascorbic acid binding oxidoreductase activity protein binding oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen dioxygenase activity procollagen-proline 4-dioxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen metal ion binding identical protein binding Cellular component procollagen-proline 4-dioxygenase complex endoplasmic reticulum mitochondrion membrane intracellular membrane-bounded organelle endoplasmic reticulum lumen Biological process peptidyl-proline hydroxylation to 4-hydroxy-L-proline collagen fibril organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5033 18451 Ensembl ENSG00000122884 ENSMUSG00000019916 UniProt P13674 Q60715 RefSeq (mRNA) NM_001142596 NM_000917 NM_001017962 NM_001142595 NM_011030 NM_001316370 NM_001316371 RefSeq (protein) NP_000908 NP_001017962 NP_001136067 NP_001136068 NP_001303299 NP_001303300 NP_035160 Location (UCSC) Chr 10: 73.01 – 73.1 Mb Chr 10: 59.16 – 59.21 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Prolyl 4-hydroxylase subunit alpha-1 is an enzyme that in humans is encoded by the P4HA1 gene.

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.

Further reading

• Helaakoski T, Vuori K, Myllylä R, et al. (1989). "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". Proc. Natl. Acad. Sci. U.S.A. 86 (12): 4392–6. doi:10.1073/pnas.86.12.4392. PMC 287275. PMID 2543975.
• Helaakoski T, Veijola J, Vuori K, et al. (1994). "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". J. Biol. Chem. 269 (45): 27847–54. PMID 7961714.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• 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. doi:10.1074/jbc.272.28.17342. PMID 9211872.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Horelli-Kuitunen N, Kvist AP, Helaakoski T, et al. (1998). "The order and transcriptional orientation of the human COL13A1 and P4HA genes on chromosome 10 long arm determined by high-resolution FISH". Genomics. 46 (2): 299–302. doi:10.1006/geno.1997.5015. PMID 9417920.
• 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. PMC 139241. PMID 12477932.
• Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10". Nature. 429 (6990): 375–81. doi:10.1038/nature02462. PMID 15164054.
• Raveendran M, Senthil D, Utama B, et al. (2004). "Cigarette suppresses the expression of P4Halpha and vascular collagen production". Biochem. Biophys. Res. Commun. 323 (2): 592–8. doi:10.1016/j.bbrc.2004.08.129. PMID 15369792.
• 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. PMC 528928. PMID 15489334.
• Fähling M, Mrowka R, Steege A, et al. (2006). "Heterogeneous nuclear ribonucleoprotein-A2/B1 modulate collagen prolyl 4-hydroxylase, alpha (I) mRNA stability". J. Biol. Chem. 281 (14): 9279–86. doi:10.1074/jbc.M510925200. PMID 16464861.
• Chen L, Shen YH, Wang X, et al. (2006). "Human prolyl-4-hydroxylase alpha(I) transcription is mediated by upstream stimulatory factors". J. Biol. Chem. 281 (16): 10849–55. doi:10.1074/jbc.M511237200. PMC 2819823. PMID 16488890.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Fähling M, Mrowka R, Steege A, et al. (2006). "Translational control of collagen prolyl 4-hydroxylase-alpha(I) gene expression under hypoxia". J. Biol. Chem. 281 (36): 26089–101. doi:10.1074/jbc.M604939200. PMID 16837461.
• 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. doi:10.2353/ajpath.2006.050738. PMC 1698781. 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.