P4HTM

Last updated
P4HTM
Identifiers
Aliases P4HTM , EGLN4, HIFPH4, P4H-TM, PH-4, PH4, PHD4, prolyl 4-hydroxylase, transmembrane, HIDEA
External IDs OMIM: 614584 MGI: 1921693 HomoloGene: 41765 GeneCards: P4HTM
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_017732
NM_177938
NM_177939

NM_028944
NM_001357465

RefSeq (protein)

NP_808807
NP_808808

NP_083220
NP_001344394

Location (UCSC) Chr 3: 48.99 – 49.01 Mb Chr 9: 108.46 – 108.47 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Prolyl 4-hydroxylase, transmembrane is a protein that in humans is encoded by the P4HTM gene. [5]

Contents

Function

The product of this gene belongs to the family of prolyl 4-hydroxylases. This protein is a prolyl hydroxylase that may be involved in the degradation of hypoxia-inducible transcription factors under normoxia. It plays a role in adaptation to hypoxia and may be related to cellular oxygen sensing. Alternatively spliced variants encoding different isoforms have been identified.

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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.

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Hypoxia-inducible factor-asparagine dioxygenase (EC 1.14.11.30, HIF hydroxylase) is an enzyme with systematic name hypoxia-inducible factor-L-asparagine, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating). This enzyme catalyses the following chemical reaction:

hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2

Alpha-ketoglutarate-dependent hydroxylases are a major class of non-heme iron proteins that catalyse a wide range of reactions. These reactions include hydroxylation reactions, demethylations, ring expansions, ring closures, and desaturations. Functionally, the αKG-dependent hydroxylases are comparable to cytochrome P450 enzymes. Both use O2 and reducing equivalents as cosubstrates and both generate water.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000178467 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000006675 - 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.
  5. "Entrez Gene: Prolyl 4-hydroxylase, transmembrane" . Retrieved 2017-10-03.

Further reading


This article incorporates text from the United States National Library of Medicine, which is in the public domain.