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Protein

Phytanoyl-CoA dioxygenase, peroxisomal

Gene

Phyh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.

Catalytic activityi

Phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201Alpha-ketoglutarateBy similarity
Binding sitei157 – 1571Alpha-ketoglutarateBy similarity
Metal bindingi175 – 1751IronBy similarity
Metal bindingi177 – 1771IronBy similarity
Binding sitei193 – 1931Alpha-ketoglutarateBy similarity
Metal bindingi264 – 2641IronBy similarity
Binding sitei266 – 2661Alpha-ketoglutarateBy similarity
Binding sitei275 – 2751Alpha-ketoglutarateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Enzyme and pathway databases

ReactomeiR-MMU-389599. Alpha-oxidation of phytanate.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
Phytanoyl-CoA dioxygenase, peroxisomal (EC:1.14.11.18)
Alternative name(s):
Lupus nephritis-associated peptide 1
Phytanic acid oxidase
Phytanoyl-CoA alpha-hydroxylase
Short name:
PhyH
Gene namesi
Name:Phyh
Synonyms:Ln1, Lnap1, Pahx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:891978. Phyh.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
  • peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Involvement in diseasei

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030PeroxisomeBy similarityAdd
BLAST
Chaini31 – 338308Phytanoyl-CoA dioxygenase, peroxisomalPRO_0000024054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-succinyllysineCombined sources
Modified residuei108 – 1081N6-succinyllysineCombined sources
Modified residuei231 – 2311N6-succinyllysineCombined sources
Modified residuei252 – 2521N6-succinyllysineCombined sources

Proteomic databases

EPDiO35386.
PaxDbiO35386.
PRIDEiO35386.

PTM databases

iPTMnetiO35386.
PhosphoSiteiO35386.
SwissPalmiO35386.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiO35386.
CleanExiMM_PHYH.
ExpressionAtlasiO35386. baseline and differential.
GenevisibleiO35386. MM.

Interactioni

Subunit structurei

Interacts specifically with the immunophilin FKBP52 and PHYHIP.1 Publication

Protein-protein interaction databases

BioGridi201185. 1 interaction.
IntActiO35386. 2 interactions.
MINTiMINT-1864642.
STRINGi10090.ENSMUSP00000027975.

Structurei

3D structure databases

ProteinModelPortaliO35386.
SMRiO35386. Positions 44-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 1773Alpha-ketoglutarate bindingBy similarity

Sequence similaritiesi

Belongs to the PhyH family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IPBI. Eukaryota.
COG5285. LUCA.
HOGENOMiHOG000007341.
HOVERGENiHBG000392.
InParanoidiO35386.
KOiK00477.
OMAiWTAMERV.
OrthoDBiEOG7NGQC7.
PhylomeDBiO35386.
TreeFamiTF313667.

Family and domain databases

InterProiIPR008775. Phytyl_CoA_dOase.
[Graphical view]
PfamiPF05721. PhyH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35386-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLTRAGARL QVLLGHLGRP SAPTIVAQPV SGLASPASFQ PEQFQYTLDN
60 70 80 90 100
NVLTLEQRKF YEENGFLVIK NLVSDDDIQR FRAEFERICR EEVKPPGIVI
110 120 130 140 150
MRDVALAKQD YMPSDRMVSK IQDFQEDEEL FRYCLLPEIL KYVECFTGPN
160 170 180 190 200
IMALHGMLIN KPPDVGKKTS RHPLHQDLHY FPFRPSNLIV CAWTAMEHID
210 220 230 240 250
RNNGCLVVLP GTHKGTLKPH DYPKWEGGVN KMYHGIQDYD PNSPRVHLVM
260 270 280 290 300
EKGDTVFFHP LLIHGSGRNK TQGFRKAISC HFGSSDCQCI DVSGTSQENI
310 320 330
AREVVEMAEK KYGFQGVMDF KDTWIFRSRL VKGERINI
Length:338
Mass (Da):38,607
Last modified:January 1, 1998 - v1
Checksum:i9363F4322D59360E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21N → K in BAA19003 (PubMed:8954131).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023463 mRNA. Translation: AAB81835.1.
D88670 mRNA. Translation: BAA19003.1.
BC002018 mRNA. Translation: AAH02018.1.
CCDSiCCDS15660.1.
PIRiJC5242.
RefSeqiNP_034856.1. NM_010726.2.
UniGeneiMm.391704.

Genome annotation databases

EnsembliENSMUST00000027975; ENSMUSP00000027975; ENSMUSG00000026664.
GeneIDi16922.
KEGGimmu:16922.
UCSCiuc008ifd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023463 mRNA. Translation: AAB81835.1.
D88670 mRNA. Translation: BAA19003.1.
BC002018 mRNA. Translation: AAH02018.1.
CCDSiCCDS15660.1.
PIRiJC5242.
RefSeqiNP_034856.1. NM_010726.2.
UniGeneiMm.391704.

3D structure databases

ProteinModelPortaliO35386.
SMRiO35386. Positions 44-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201185. 1 interaction.
IntActiO35386. 2 interactions.
MINTiMINT-1864642.
STRINGi10090.ENSMUSP00000027975.

PTM databases

iPTMnetiO35386.
PhosphoSiteiO35386.
SwissPalmiO35386.

Proteomic databases

EPDiO35386.
PaxDbiO35386.
PRIDEiO35386.

Protocols and materials databases

DNASUi16922.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027975; ENSMUSP00000027975; ENSMUSG00000026664.
GeneIDi16922.
KEGGimmu:16922.
UCSCiuc008ifd.2. mouse.

Organism-specific databases

CTDi5264.
MGIiMGI:891978. Phyh.

Phylogenomic databases

eggNOGiENOG410IPBI. Eukaryota.
COG5285. LUCA.
HOGENOMiHOG000007341.
HOVERGENiHBG000392.
InParanoidiO35386.
KOiK00477.
OMAiWTAMERV.
OrthoDBiEOG7NGQC7.
PhylomeDBiO35386.
TreeFamiTF313667.

Enzyme and pathway databases

UniPathwayiUPA00199.
ReactomeiR-MMU-389599. Alpha-oxidation of phytanate.

Miscellaneous databases

NextBioi290972.
PROiO35386.
SOURCEiSearch...

Gene expression databases

BgeeiO35386.
CleanExiMM_PHYH.
ExpressionAtlasiO35386. baseline and differential.
GenevisibleiO35386. MM.

Family and domain databases

InterProiIPR008775. Phytyl_CoA_dOase.
[Graphical view]
PfamiPF05721. PhyH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH PHYHIP.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Liver and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-108; LYS-231 AND LYS-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPAHX_MOUSE
AccessioniPrimary (citable) accession number: O35386
Secondary accession number(s): O08527
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.