ID PAHX_MOUSE Reviewed; 338 AA. AC O35386; O08527; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 76. DE RecName: Full=Phytanoyl-CoA dioxygenase, peroxisomal; DE EC=1.14.11.18; DE AltName: Full=Phytanoyl-CoA alpha-hydroxylase; DE Short=PhyH; DE AltName: Full=Phytanic acid oxidase; DE AltName: Full=Lupus nephritis-associated peptide 1; DE Flags: Precursor; GN Name=Phyh; Synonyms=Ln1, Lnap1, Pahx; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97467730; PubMed=9326939; DOI=10.1038/ng1097-185; RA Mihalik S.J., Morrell J.C., Kim D., Sachsteder K.A., Watkins P.A., RA Gould S.J.; RT "Identification of PAHX, a Refsum disease gene."; RL Nat. Genet. 17:185-189(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Kidney; RX MEDLINE=97112451; PubMed=8954131; DOI=10.1006/bbrc.1996.1805; RA Iwano M., Ueno M., Miyazaki M., Harada T., Nagai Y., Hirano M., RA Dohi Y., Akai Y., Kurioka H., Dohi K.; RT "Molecular cloning and expression of a novel peptide (LN1) gene: RT reduced expression in the renal cortex of lupus nephritis in MRL/lpr RT mouse."; RL Biochem. Biophys. Res. Commun. 229:355-360(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY, AND INTERACTION WITH PHYHIP. RX MEDLINE=20153698; PubMed=10686344; DOI=10.1016/S0169-328X(99)00304-6; RA Lee Z.H., Kim H.-H., Ahn K.Y., Seo K.H., Kim J.K., Bae C.S., Kim K.K.; RT "Identification of a brain specific protein that associates with a RT Refsum disease gene product, phytanoyl-CoA alpha-hydroxylase."; RL Brain Res. Mol. Brain Res. 75:237-247(2000). CC -!- FUNCTION: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA. CC -!- CATALYTIC ACTIVITY: Phytanoyl-CoA + 2-oxoglutarate + O(2) = 2- CC hydroxyphytanoyl-CoA + succinate + CO(2). CC -!- COFACTOR: Iron. CC -!- COFACTOR: Ascorbate. CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism. CC -!- SUBUNIT: Interacts specifically with the immunophilin FKBP52 and CC PHYHIP. CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues with CC significant levels detected in the embryonic and neonatal heart CC and liver. In the adult, significant levels are detected in the CC liver, kidney, heart, gut, brain and aorta. CC -!- DISEASE: Defects in Phyh are the cause of lupus nephritis, a CC severe autoimmune disease. Phyh could be involved in a reaction CC against the progression of the disease, because its expression is CC low in the early stage of the disease in the renal cortex of CC MRL/lpr mice. CC -!- SIMILARITY: Belongs to the PhyH family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF023463; AAB81835.1; -; mRNA. DR EMBL; D88670; BAA19003.1; -; mRNA. DR EMBL; BC002018; AAH02018.1; -; mRNA. DR IPI; IPI00129963; -. DR PIR; JC5242; JC5242. DR RefSeq; NP_034856.1; -. DR UniGene; Mm.391704; -. DR SMR; O35386; 44-322. DR PhosphoSite; O35386; -. DR Ensembl; ENSMUSG00000026664; Mus musculus. DR GeneID; 16922; -. DR KEGG; mmu:16922; -. DR MGI; MGI:891978; Phyh. DR HOGENOM; O35386; -. DR HOVERGEN; O35386; -. DR OMA; O35386; NIMFHGI. DR BRENDA; 1.14.11.18; 244. DR NextBio; 290972; -. DR ArrayExpress; O35386; -. DR Bgee; O35386; -. DR CleanEx; MM_PHYH; -. DR GermOnline; ENSMUSG00000026664; Mus musculus. DR GO; GO:0005777; C:peroxisome; TAS:MGI. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW. DR GO; GO:0048244; F:phytanoyl-CoA dioxygenase activity; IEA:EC. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR GO; GO:0001561; P:fatty acid alpha-oxidation; IDA:MGI. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR008775; Phytyl_CoA_dOase. DR Pfam; PF05721; PhyH; 1. PE 1: Evidence at protein level; KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Peroxisome; KW Transit peptide; Vitamin C. FT TRANSIT 1 30 Peroxisome (By similarity). FT CHAIN 31 338 Phytanoyl-CoA dioxygenase, peroxisomal. FT /FTId=PRO_0000024054. FT REGION 175 177 Alpha-ketoglutarate binding (By FT similarity). FT METAL 175 175 Iron (By similarity). FT METAL 177 177 Iron (By similarity). FT METAL 264 264 Iron (By similarity). FT BINDING 120 120 Alpha-ketoglutarate (By similarity). FT BINDING 157 157 Alpha-ketoglutarate (By similarity). FT BINDING 193 193 Alpha-ketoglutarate (By similarity). FT BINDING 266 266 Alpha-ketoglutarate (By similarity). FT BINDING 275 275 Alpha-ketoglutarate (By similarity). FT CONFLICT 2 2 N -> K (in Ref. 2; BAA19003). SQ SEQUENCE 338 AA; 38607 MW; 9363F4322D59360E CRC64; MNLTRAGARL QVLLGHLGRP SAPTIVAQPV SGLASPASFQ PEQFQYTLDN NVLTLEQRKF YEENGFLVIK NLVSDDDIQR FRAEFERICR EEVKPPGIVI MRDVALAKQD YMPSDRMVSK IQDFQEDEEL FRYCLLPEIL KYVECFTGPN IMALHGMLIN KPPDVGKKTS RHPLHQDLHY FPFRPSNLIV CAWTAMEHID RNNGCLVVLP GTHKGTLKPH DYPKWEGGVN KMYHGIQDYD PNSPRVHLVM EKGDTVFFHP LLIHGSGRNK TQGFRKAISC HFGSSDCQCI DVSGTSQENI AREVVEMAEK KYGFQGVMDF KDTWIFRSRL VKGERINI //