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UniProtKB/Swiss-Prot entry O43174


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CP26A_HUMAN
Primary accession number O43174
Secondary accession number Q5VXI0
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on December 16, 2008 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 74)
Name and origin of the protein
Protein name Cytochrome P450 26A1
Synonyms EC 1.14.-.-
Retinoic acid-metabolizing cytochrome
P450 retinoic acid-inactivating 1
P450RAI
hP450RAI
Retinoic acid 4-hydroxylase
Gene name
Name: CYP26A1
Synonyms: CYP26, P450RAI1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.272.30.18538; PubMed=9228017 [NCBI, ExPASy, EBI, Israel, Japan]
White J.A., Beckett-Jones B., Guo Y.-D., Dilworth F.J., Bonasoro J., Jones G., Petkovich M.;
"cDNA cloning of human retinoic acid-metabolizing enzyme (hP450RAI) identifies a novel family of cytochromes P450.";
J. Biol. Chem. 272:18538-18541(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9716180 [NCBI, ExPASy, EBI, Israel, Japan]
Sonneveld E., van den Brink C.E., van der Leede B.M., Schulkes R.K., Petkovich M., van der Burg B., van der Saag P.T.;
"Human retinoic acid (RA) 4-hydroxylase (CYP26) is highly specific for all-trans-RA and can be induced through RA receptors in human breast and colon carcinoma cells.";
Cell Growth Differ. 9:629-637(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
TISSUE SPECIFICITY.
DOI=10.1006/bbrc.1998.9659; PubMed=9826557 [NCBI, ExPASy, EBI, Israel, Japan]
Trofimova-Griffin M.E., Juchau M.R.;
"Expression of cytochrome P450RAI (CYP26) in human fetal hepatic and cephalic tissues.";
Biochem. Biophys. Res. Commun. 252:487-491(1998).
Comments
  • FUNCTION: Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18-hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA.
  • COFACTOR: Heme group (By similarity).
  • SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
  • TISSUE SPECIFICITY: Highest levels in adult liver, heart, pituitary gland, adrenal gland, placenta and regions of the brain.
  • INDUCTION: By retinoic acid.
  • SIMILARITY: Belongs to the cytochrome P450 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF005418; AAB88881.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL358613; CAH72803.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471066; EAW50079.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00304967; -.
RefSeq NP_000774.2; -.
UniGene Hs.150595
3D structure databases
HSSP P14779; 1JPZ. [HSSP ENTRY / PDB]
ModBase O43174.
Enzyme and pathway databases
Reactome REACT_13433; Biological oxidations.
Organism-specific databases
GeneCards GC10P094823; -.
HGNC HGNC:2603; CYP26A1.
GenAtlas CYP26A1.
HPA CAB015447; -.
MIM 602239; gene. [NCBI / EBI]
PharmGKB PA27098; -.
Gene expression databases
ArrayExpress O43174; -.
Bgee O43174; -.
CleanEx HS_CYP26A1; -.
GermOnline ENSG00000095596; Homo sapiens.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792; Cellular component: microsome (inferred from direct assay from UniProtKB).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (non-traceable author statement from UniProtKB).
GO:0019825; Molecular function: oxygen binding (traceable author statement from ProtInc).
GO:0008401; Molecular function: retinoic acid 4-hydroxylase activity (inferred from direct assay from UniProtKB).
GO:0001972; Molecular function: retinoic acid binding (inferred from direct assay from UniProtKB).
GO:0048387; Biological process: negative regulation of retinoic acid receptor signaling pathway (traceable author statement from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0034653; Biological process: retinoic acid catabolic process (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001128; Cyt_P450.
IPR017973; Cyt_P450_C.
IPR017972; Cyt_P450_CS.
IPR002403; Cyt_P450_E_grp-IV.
Graphical view of domain structure.
Gene3D G3DSA:1.10.630.10; Cyt_P450; 1.
PANTHER PTHR19383; Cyt_P450; 1.
Pfam PF00067; p450; 1.
Pfam graphical view of domain structure.
PRINTS PR00465; EP450IV.
PR00385; P450.
PROSITE PS00086; CYTOCHROME_P450; 1.
Proteomic databases
PRIDE O43174; -.
Genome annotation databases
Ensembl ENSG00000095596; Homo sapiens. [Contig view]
GeneID 1592; -.
Phylogenomic databases
HOGENOM O43174; -.
HOVERGEN O43174; -.
OMA O43174; QRKKVIM.
Other
SOURCE CYP26A1; Homo sapiens.
ProtoNet O43174.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   497  497     Cytochrome P450 26A1. PRO_0000051980
METAL   442   442        Iron (heme axial ligand) (Potential). 
CONFLICT   104   105        EH -> DD (in Ref. 1; AAB88881). 
Sequence information
Length: 497 AA [This is the length of the unprocessed precursor] Molecular weight: 56199 Da [This is the MW of the unprocessed precursor] CRC64: 834318FA493E76D4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGLPALLASA LCTFVLPLLL FLAAIKLWDL YCVSGRDRSC ALPLPPGTMG FPFFGETLQM 

        70         80         90        100        110        120 
VLQRRKFLQM KRRKYGFIYK THLFGRPTVR VMGADNVRRI LLGEHRLVSV HWPASVRTIL 

       130        140        150        160        170        180 
GSGCLSNLHD SSHKQRKKVI MRAFSREALE CYVPVITEEV GSSLEQWLSC GERGLLVYPE 

       190        200        210        220        230        240 
VKRLMFRIAM RILLGCEPQL AGDGDSEQQL VEAFEEMTRN LFSLPIDVPF SGLYRGMKAR 

       250        260        270        280        290        300 
NLIHARIEQN IRAKICGLRA SEAGQGCKDA LQLLIEHSWE RGERLDMQAL KQSSTELLFG 

       310        320        330        340        350        360 
GHETTASAAT SLITYLGLYP HVLQKVREEL KSKGLLCKSN QDNKLDMEIL EQLKYIGCVI 

       370        380        390        400        410        420 
KETLRLNPPV PGGFRVALKT FELNGYQIPK GWNVIYSICD THDVAEIFTN KEEFNPDRFM 

       430        440        450        460        470        480 
LPHPEDASRF SFIPFGGGLR SCVGKEFAKI LLKIFTVELA RHCDWQLLNG PPTMKTSPTV 

       490 
YPVDNLPARF THFHGEI 

O43174 in FASTA format

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