Reviewed, UniProtKB/Swiss-Prot O35386 (PAHX_MOUSE)

Names and origin

Protein names

Recommended name:
    Phytanoyl-CoA dioxygenase, peroxisomal
    EC=1.14.11.18
Alternative name(s):
    Phytanoyl-CoA alpha-hydroxylase
      Short name=PhyH
    Phytanic acid oxidase
    Lupus nephritis-associated peptide 1

Gene names

Name:	Phyh
Synonyms:	Ln1, Lnap1, Pahx

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
Catalytic activity	Phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2.
Cofactor	Iron. Ascorbate.
Pathway	Lipid metabolism; fatty acid metabolism.
Subunit structure	Interacts specifically with the immunophilin FKBP52 and PHYHIP. Ref.4
Subcellular location	Peroxisome.
Tissue specificity	Ubiquitously expressed in all tissues with significant levels detected in the embryonic and neonatal heart and liver. In the adult, significant levels are detected in the liver, kidney, heart, gut, brain and aorta. Ref.4
Involvement in disease	Defects in Phyh are the cause of lupus nephritis, a severe autoimmune disease. Phyh could be involved in a reaction against the progression of the disease, because its expression is low in the early stage of the disease in the renal cortex of MRL/lpr mice.
Sequence similarities	Belongs to the PhyH family.

Ontologies

Keywords
Cellular component	Peroxisome
Domain	Transit peptide
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	fatty acid alpha-oxidation Ref.1 Inferred from direct assay. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Ref.1 Traceable author statement. Source: MGI
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW phytanoyl-CoA dioxygenase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 30	30	Peroxisome By similarity
	Chain	31 – 338	308	Phytanoyl-CoA dioxygenase, peroxisomal		PRO_0000024054
Regions
	Region	175 – 177	3	Alpha-ketoglutarate binding By similarity
Sites
	Metal binding	175	1	Iron By similarity
	Metal binding	177	1	Iron By similarity
	Metal binding	264	1	Iron By similarity
	Binding site	120	1	Alpha-ketoglutarate By similarity
	Binding site	157	1	Alpha-ketoglutarate By similarity
	Binding site	193	1	Alpha-ketoglutarate By similarity
	Binding site	266	1	Alpha-ketoglutarate By similarity
	Binding site	275	1	Alpha-ketoglutarate By similarity
Experimental info
	Sequence conflict	2	1	N → K in BAA19003. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O35386-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 9363F4322D59360E	FASTA	338	38,607
	10 20 30 40 50 60 MNLTRAGARL QVLLGHLGRP SAPTIVAQPV SGLASPASFQ PEQFQYTLDN NVLTLEQRKF 70 80 90 100 110 120 YEENGFLVIK NLVSDDDIQR FRAEFERICR EEVKPPGIVI MRDVALAKQD YMPSDRMVSK 130 140 150 160 170 180 IQDFQEDEEL FRYCLLPEIL KYVECFTGPN IMALHGMLIN KPPDVGKKTS RHPLHQDLHY 190 200 210 220 230 240 FPFRPSNLIV CAWTAMEHID RNNGCLVVLP GTHKGTLKPH DYPKWEGGVN KMYHGIQDYD 250 260 270 280 290 300 PNSPRVHLVM EKGDTVFFHP LLIHGSGRNK TQGFRKAISC HFGSSDCQCI DVSGTSQENI 310 320 330 AREVVEMAEK KYGFQGVMDF KDTWIFRSRL VKGERINI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of PAHX, a Refsum disease gene." Mihalik S.J., Morrell J.C., Kim D., Sachsteder K.A., Watkins P.A., Gould S.J. Nat. Genet. 17:185-189(1997) [PubMed: 9326939] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning and expression of a novel peptide (LN1) gene: reduced expression in the renal cortex of lupus nephritis in MRL/lpr mouse." Iwano M., Ueno M., Miyazaki M., Harada T., Nagai Y., Hirano M., Dohi Y., Akai Y., Kurioka H., Dohi K. Biochem. Biophys. Res. Commun. 229:355-360(1996) [PubMed: 8954131] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Kidney.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Mammary gland.
[4]	"Identification of a brain specific protein that associates with a Refsum disease gene product, phytanoyl-CoA alpha-hydroxylase." Lee Z.H., Kim H.-H., Ahn K.Y., Seo K.H., Kim J.K., Bae C.S., Kim K.K. Brain Res. Mol. Brain Res. 75:237-247(2000) [PubMed: 10686344] [Abstract] Cited for: TISSUE SPECIFICITY, INTERACTION WITH PHYHIP.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF023463 mRNA. Translation: AAB81835.1. D88670 mRNA. Translation: BAA19003.1. BC002018 mRNA. Translation: AAH02018.1.
IPI	IPI00129963.
PIR	JC5242.
RefSeq	NP_034856.1.
UniGene	Mm.391704
3D structure databases
SMR	O35386. Positions 44-322.
ModBase	Search...
PTM databases
PhosphoSite	O35386.
Genome annotation databases
Ensembl	ENSMUSG00000026664. Mus musculus. [Contig view]
GeneID	16922.
KEGG	mmu:16922.
Organism-specific databases
MGI	MGI:891978. Phyh.
Phylogenomic databases
HOGENOM	O35386.
HOVERGEN	O35386.
OMA	O35386. NIMFHGI.
Enzyme and pathway databases
BRENDA	1.14.11.18. 244.
Gene expression databases
ArrayExpress	O35386.
Bgee	O35386.
CleanEx	MM_PHYH.
GermOnline	ENSMUSG00000026664. Mus musculus.
Family and domain databases
InterPro	IPR008775. Phytyl_CoA_dOase. [Graphical view]
Pfam	PF05721. PhyH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	290972.
SOURCE	Search...

Entry information

Entry name

PAHX_MOUSE

Accession

Primary (citable) accession number: O35386
Secondary accession number(s): O08527

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)