ID CP24_HUMAN STANDARD; PRT; 514 AA. AC Q07973; Q15807; DT 01-OCT-1996 (Rel. 34, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Cytochrome P450 24A1, mitochondrial precursor (EC 1.14.-.-) (P450- DE CC24) (Vitamin D(3) 24-hydroxylase) (1,25-dihydroxyvitamin D(3) 24- DE hydroxylase) (24-OHase). GN CYP24A1 OR CYP24. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93281615; PubMed=8506296; RA Chen K.-S., Prahl J.M., Deluca H.F.; RT "Isolation and expression of human 1,25-dihydroxyvitamin D3 24- RT hydroxylase cDNA."; RL Proc. Natl. Acad. Sci. U.S.A. 90:4543-4547(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [3] RP SEQUENCE OF 1-104 FROM N.A. RX MEDLINE=95359195; PubMed=7632726; RA Chen K.-S., DeLuca H.F.; RT "Cloning of the human 1 alpha,25-dihydroxyvitamin D-3 24-hydroxylase RT gene promoter and identification of two vitamin D-responsive RT elements."; RL Biochim. Biophys. Acta 1263:1-9(1995). RN [4] RP SEQUENCE OF 258-514 FROM N.A. RX MEDLINE=94091187; PubMed=8266831; RA Labuda M., Lemieux N., Tihy F., Prinster C., Glorieux F.H.; RT "Human 25-hydroxyvitamin D 24-hydroxylase cytochrome P450 subunit RT maps to a different chromosomal location than that of pseudovitamin RT D-deficient rickets."; RL J. Bone Miner. Res. 8:1397-1406(1993). CC -!- FUNCTION: Has a role in maintaining calcium homeostasis. Catalyzes CC the NADPH-dependent 24-hydroxylation of 25-hydroxyvitamin D(3) in CC the presence of adrenodoxin and NADPH-adrenodoxin reductase. CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L13286; AAA62379.1; -. DR EMBL; AL138805; CAB91829.1; -. DR EMBL; U60669; AAB03776.1; ALT_SEQ. DR EMBL; S67623; AAB29308.1; -. DR PIR; A47436; A47436. DR PIR; I55488; I55488. DR HSSP; P14779; 1JPZ. DR Genew; HGNC:2602; CYP24A1. DR MIM; 126065; -. DR GO; GO:0005489; F:electron transporter activity; TAS. DR GO; GO:0004497; F:monooxygenase activity; TAS. DR GO; GO:0019825; F:oxygen binding; TAS. DR GO; GO:0006118; P:electron transport; NAS. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Electron transport; Heme; KW Mitochondrion; Transit peptide. FT TRANSIT 1 35 Mitochondrion (By similarity). FT CHAIN 36 514 Cytochrome P450 24A1. FT METAL 462 462 Iron (heme axial ligand) (Potential). FT CONFLICT 68 68 G -> A (in Ref. 1). FT CONFLICT 124 125 AY -> V (in Ref. 1). FT CONFLICT 270 270 D -> G (in Ref. 1). FT CONFLICT 365 365 V -> R (in Ref. 1). FT CONFLICT 368 368 A -> E (in Ref. 1). FT CONFLICT 390 390 S -> G (in Ref. 1). FT CONFLICT 511 511 F -> S (in Ref. 4). SQ SEQUENCE 514 AA; 58875 MW; 8862F63771981195 CRC64; MSSPISKSRS LAAFLQQLRS PRQPPRLVTS TAYTSPQPRE VPVCPLTAGG ETQNAAALPG PTSWPLLGSL LQILWKGGLK KQHDTLVEYH KKYGKIFRMK LGSFESVHLG SPCLLEALYR TESAYPQRLE IKPWKAYRDY RKEGYGLLIL EGEDWQRVRS AFQKKLMKPG EVMKLDNKIN EVLADFMGRI DELCDERGHV EDLYSELNKW SFESICLVLY EKRFGLLQKN AGDEAVNFIM AIKTMMSTFG RMMVTPVELH KSLNTKVWQD HTLAWDTIFK SVKACIDNRL EKYSQQPSAD FLCDIYHQNR LSKKELYAAV TELQLAAVET TANSLMWILY NLSRNPQVQQ KLLKEIQSVL PENQVPRAED LRNMPYLKAC LKESMRLTPS VPFTTRTLDK ATVLGEYALP KGTVLMLNTQ VLGSSEDNFE DSSQFRPERW LQEKEKINPF AHLPFGVGKR MCIGRRLAEL QLHLALCWIV RKYDIQATDN EPVEMLHSGT LVPSRELPIA FCQR //