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
Gene location (Human)
Chr.	Chromosome 10 (human)
End	73,096,974 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	59,209,126 bp
RNA expression pattern
	Top expressed in
	Achilles tendon; ; tibia; ; pericardium; ; stromal cell of endometrium; ; periodontal fiber; ; gastrocnemius muscle; ; tibialis anterior muscle; ; triceps brachii muscle; ; biceps brachii; ; deltoid muscle;
	Top expressed in
	calvaria; ; right lung lobe; ; dermis; ; body of femur; ; cumulus cell; ; sciatic nerve; ; yolk sac; ; belly cord; ; placenta; ; proximal tubule;
	More reference expression data
	; ;
	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
	5033
	18451
	ENSG00000122884
	ENSMUSG00000019916
	P13674
	Q60715
	NM_001142596 ; NM_000917 ; NM_001017962 ; NM_001142595
	NM_011030 ; NM_001316370 ; NM_001316371
	NP_000908 ; NP_001017962 ; NP_001136067 ; NP_001136068
	NP_001303299 ; NP_001303300 ; NP_035160
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 18, 2022

Prolyl 4-hydroxylase subunit alpha-1 is an enzyme that in humans is encoded by the P4HA1 gene.^[5]^[6]

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.^[6]

Related Research Articles

Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion, identified by Diaz and colleagues in 1990.

Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases. These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid, Fe²⁺, and ascorbate. This particular enzyme catalyzes the formation of (2S, 4R)-4-hydroxyproline, a compound that represents the most prevalent post-translational modification in the human proteome.

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit is an enzyme that in humans is encoded by the PPP1CC gene.

Laminin subunit alpha-3 is a protein that in humans is encoded by the LAMA3 gene.

Hypoxia-inducible factor prolyl hydroxylase 2 (HIF-PH2), or prolyl hydroxylase domain-containing protein 2 (PHD2), is an enzyme encoded by the EGLN1 gene. It is also known as Egl nine homolog 1. PHD2 is a α-ketoglutarate/2-oxoglutarate-dependent hydroxylase, a superfamily non-haem iron-containing proteins. In humans, PHD2 is one of the three isoforms of hypoxia-inducible factor-proline dioxygenase, which is also known as HIF prolyl-hydroxylase.

Eukaryotic translation initiation factor 2 subunit 2 (eIF2β) is a protein that in humans is encoded by the EIF2S2 gene.

Phosphoenolpyruvate carboxykinase 1 (soluble), also known as PCK1, is an enzyme which in humans is encoded by the PCK1 gene.

Collagen alpha-1(XI) chain is a protein that in humans is encoded by the COL11A1 gene.

Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS gene.

2-Oxoisovalerate dehydrogenase subunit beta, mitochondrial is an enzyme that in humans is encoded by the BCKDHB gene.

Voltage-gated potassium channel subunit beta-1 is a protein that in humans is encoded by the KCNAB1 gene.

Mediator of RNA polymerase II transcription subunit 17 is an enzyme that in humans is encoded by the MED17 gene.

Collagen alpha-1(XIII) chain is a protein that in humans is encoded by the COL13A1 gene.

Collagen alpha-1(XIX) chain is a protein that in humans is encoded by the COL19A1 gene.

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 is a protein that in humans is encoded by the GNG3 gene.

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 is an enzyme that in humans is encoded by the PLOD3 gene.

52 kDa repressor of the inhibitor of the protein kinase is an enzyme that in humans is encoded by the PRKRIR gene.

Prolyl 4-hydroxylase subunit alpha-2 is an enzyme that in humans is encoded by the P4HA2 gene.

Prolyl 3-hydroxylase 3 is an enzyme that in humans is encoded by the LEPREL2 gene.

Prolyl 4-hydroxylase, transmembrane is a protein that in humans is encoded by the P4HTM gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000122884 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000019916 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Pajunen L, Jones TA, Helaakoski T, Pihlajaniemi T, Solomon E, Sheer D, Kivirikko KI (Jan 1990). "Assignment of the gene coding for the alpha-subunit of prolyl 4-hydroxylase to human chromosome region 10q21.3-23.1". Am J Hum Genet. 45 (6): 829–34. PMC 1683466 . PMID 2556027.
1 2 "Entrez Gene: P4HA1 procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide I".

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. doi: 10.1016/S0021-9258(18)46864-0 . 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004Natur.429..375D. 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.
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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000122884 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000019916 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2556027-5] Pajunen L, Jones TA, Helaakoski T, Pihlajaniemi T, Solomon E, Sheer D, Kivirikko KI (Jan 1990). "Assignment of the gene coding for the alpha-subunit of prolyl 4-hydroxylase to human chromosome region 10q21.3-23.1". Am J Hum Genet. 45 (6): 829–34. PMC 1683466 . PMID 2556027.

[entrez-6] 1 2 "Entrez Gene: P4HA1 procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide I".

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P4HA1

Related Research Articles

References

Further reading