PHYD1_MOUSE
ID PHYD1_MOUSE Reviewed; 291 AA.
AC Q9DB26; A2AQZ4; Q80V68;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phytanoyl-CoA dioxygenase domain-containing protein 1 {ECO:0000250|UniProtKB:Q5SRE7};
DE Short=Protein PHYHD1 {ECO:0000250|UniProtKB:Q5SRE7};
DE EC=1.14.11.- {ECO:0000250|UniProtKB:Q5SRE7};
GN Name=Phyhd1 {ECO:0000312|MGI:MGI:3612860};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: 2-oxoglutarate(2OG)-dependent dioxygenase that catalyzes the
CC conversion of 2-oxoglutarate to succinate and CO(2) in an iron-
CC dependent manner. However, does not couple 2OG turnover to the
CC hydroxylation of acyl-coenzyme A derivatives, implying that it is not
CC directly involved in phytanoyl coenzyme-A metabolism. Does not show
CC detectable activity towards fatty acid CoA thioesters.
CC {ECO:0000250|UniProtKB:Q5SRE7}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q5SRE7};
CC -!- SIMILARITY: Belongs to the PhyH family. PHYHD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI32272.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI32274.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB23937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23715.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK005293; BAB23937.1; ALT_INIT; mRNA.
DR EMBL; AK138607; BAE23715.1; ALT_INIT; mRNA.
DR EMBL; AL845258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039982; AAH39982.1; -; mRNA.
DR EMBL; BC132271; AAI32272.1; ALT_INIT; mRNA.
DR EMBL; BC132273; AAI32274.1; ALT_INIT; mRNA.
DR CCDS; CCDS57163.1; -.
DR RefSeq; NP_001239497.1; NM_001252568.2.
DR RefSeq; NP_001239499.1; NM_001252570.1.
DR RefSeq; NP_001268758.1; NM_001281829.1.
DR RefSeq; NP_758471.1; NM_172267.4.
DR AlphaFoldDB; Q9DB26; -.
DR SMR; Q9DB26; -.
DR STRING; 10090.ENSMUSP00000088663; -.
DR iPTMnet; Q9DB26; -.
DR PhosphoSitePlus; Q9DB26; -.
DR SwissPalm; Q9DB26; -.
DR jPOST; Q9DB26; -.
DR MaxQB; Q9DB26; -.
DR PaxDb; Q9DB26; -.
DR PRIDE; Q9DB26; -.
DR ProteomicsDB; 288204; -.
DR Antibodypedia; 2006; 142 antibodies from 25 providers.
DR DNASU; 227696; -.
DR Ensembl; ENSMUST00000113645; ENSMUSP00000109275; ENSMUSG00000079484.
DR Ensembl; ENSMUST00000154647; ENSMUSP00000121371; ENSMUSG00000079484.
DR GeneID; 227696; -.
DR KEGG; mmu:227696; -.
DR UCSC; uc008jbv.3; mouse.
DR CTD; 254295; -.
DR MGI; MGI:3612860; Phyhd1.
DR VEuPathDB; HostDB:ENSMUSG00000079484; -.
DR eggNOG; KOG3290; Eukaryota.
DR GeneTree; ENSGT00390000006287; -.
DR HOGENOM; CLU_048953_0_0_1; -.
DR InParanoid; Q9DB26; -.
DR OMA; KYSEDNW; -.
DR OrthoDB; 1316775at2759; -.
DR PhylomeDB; Q9DB26; -.
DR TreeFam; TF300011; -.
DR BioGRID-ORCS; 227696; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Phyhd1; mouse.
DR PRO; PR:Q9DB26; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DB26; protein.
DR Bgee; ENSMUSG00000079484; Expressed in cortex of kidney and 57 other tissues.
DR ExpressionAtlas; Q9DB26; baseline and differential.
DR Genevisible; Q9DB26; MM.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; 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; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..291
FT /note="Phytanoyl-CoA dioxygenase domain-containing protein
FT 1"
FT /id="PRO_0000313634"
FT BINDING 102
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 141
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 156..158
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 158
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 174
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 248
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 257
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5SRE7"
SQ SEQUENCE 291 AA; 32517 MW; 7CA9823E4E6BF8B3 CRC64;
MACLSPSQLK KFQEDGFLLL EGFFTADECV AMQQRIGEIV AEMDVPLHCR TEFSTQEDEQ
LQTQGKTDYF LSSGDKIRFF FEKGVFDEKG NFLVPPEKSI NKIGHALHAH DPVFRSITHS
PKVQALVRSL GLQMPVVVQS MYIFKQPHFG GEVSPHQDAT FLYTEPLGRV LGLWIAMEDA
MLENGCLWFI PGSHTRGVSR RMIRAPSDSG PGTSFLGSDP AWASNLFVPL PVRRGGLVLI
HGEVVHKSEQ NHSDHSRQAY TVHLMEAAGT VWSPGNWLQP TPELPFPPLY S
