ID   CP51A_HUMAN             Reviewed;         503 AA.
AC   Q16850; O00770; O00772; Q16784; Q8N1A8; Q99868;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 3.
DT   16-DEC-2008, entry version 80.
DE   RecName: Full=Cytochrome P450 51A1;
DE            EC=1.14.13.70;
DE   AltName: Full=CYPLI;
DE   AltName: Full=P450LI;
DE   AltName: Full=Sterol 14-alpha demethylase;
DE   AltName: Full=Lanosterol 14-alpha demethylase;
DE            Short=LDM;
DE   AltName: Full=P450-14DM;
DE            Short=P45014DM;
GN   Name=CYP51A1; Synonyms=CYP51;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=96201125; PubMed=8619637; DOI=10.1006/abbi.1996.0193;
RA   Stroemstedt M., Rozman D., Waterman M.R.;
RT   "The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-
RT   demethylase, a cytochrome P450 whose expression is regulated by
RT   oxysterols.";
RL   Arch. Biochem. Biophys. 329:73-81(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8797093;
RA   Aoyama Y., Noshiro M., Gotoh O., Imaoka S., Funae Y., Kurosawa N.,
RA   Horiuchi T., Yoshida Y.;
RT   "Sterol 14-demethylase P450 (P45014DM*) is one of the most ancient and
RT   conserved P450 species.";
RL   J. Biochem. 119:926-933(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   MEDLINE=96404948; PubMed=8809088; DOI=10.1006/abbi.1996.0416;
RA   Rozman D., Stroemstedt M., Waterman M.R.;
RT   "The three human cytochrome P450 lanosterol 14 alpha-demethylase
RT   (CYP51) genes reside on chromosomes 3, 7, and 13: structure of the two
RT   retrotransposed pseudogenes, association with a line-1 element, and
RT   evolution of the human CYP51 family.";
RL   Arch. Biochem. Biophys. 333:466-474(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=97131516; PubMed=8975714; DOI=10.1006/geno.1996.0640;
RA   Rozman D., Stroemstedt M., Tsui L.-C., Scherer S.W., Waterman M.R.;
RT   "Structure and mapping of the human lanosterol 14alpha-demethylase
RT   gene (CYP51) encoding the cytochrome P450 involved in cholesterol
RT   biosynthesis; comparison of exon/intron organization with other
RT   mammalian and fungal CYP genes.";
RL   Genomics 38:371-381(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes C14-demethylation of lanosterol; it transforms
CC       lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.
CC   -!- CATALYTIC ACTIVITY: Obtusifoliol + 3 O(2) + 3 NADPH = 4-alpha-
CC       methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3
CC       NADP(+) + 4 H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol
CC       from lanosterol: step 1/6.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane (Potential).
CC       Microsome membrane (Potential).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC       testis, ovary, adrenal, prostrate, liver, kidney and lung.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; U23942; AAB39951.1; ALT_INIT; mRNA.
DR   EMBL; D55653; BAA09512.1; ALT_INIT; mRNA.
DR   EMBL; U51692; AAC50951.1; -; Genomic_DNA.
DR   EMBL; U51684; AAC50951.1; JOINED; Genomic_DNA.
DR   EMBL; U51685; AAC50951.1; JOINED; Genomic_DNA.
DR   EMBL; U51686; AAC50951.1; JOINED; Genomic_DNA.
DR   EMBL; U51687; AAC50951.1; JOINED; Genomic_DNA.
DR   EMBL; U51688; AAC50951.1; JOINED; Genomic_DNA.
DR   EMBL; U51689; AAC50951.1; JOINED; Genomic_DNA.
DR   EMBL; U51690; AAC50951.1; JOINED; Genomic_DNA.
DR   EMBL; U51691; AAC50951.1; JOINED; Genomic_DNA.
DR   EMBL; AC000120; AAB46356.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC032322; AAH32322.1; ALT_INIT; mRNA.
DR   PIR; JC4759; JC4759.
DR   PIR; S68855; S68855.
DR   RefSeq; NP_000777.1; -.
DR   UniGene; Hs.417077; -.
DR   HSSP; P77901; 1E9X.
DR   PhosphoSite; Q16850; -.
DR   Ensembl; ENSG00000001630; Homo sapiens.
DR   GeneID; 1595; -.
DR   KEGG; hsa:1595; -.
DR   GeneCards; GC07M091579; -.
DR   H-InvDB; HIX0021935; -.
DR   HGNC; HGNC:2649; CYP51A1.
DR   MIM; 601637; gene.
DR   PharmGKB; PA27123; -.
DR   HOGENOM; Q16850; -.
DR   HOVERGEN; Q16850; -.
DR   BioCyc; MetaCyc:ENSG00000001630-MON; -.
DR   Reactome; REACT_602; Lipid and lipoprotein metabolism.
DR   DrugBank; DB00196; Fluconazole.
DR   DrugBank; DB01167; Itraconazole.
DR   DrugBank; DB01026; Ketoconazole.
DR   DrugBank; DB01110; Miconazole.
DR   DrugBank; DB00251; Terconazole.
DR   NextBio; 6556; -.
DR   ArrayExpress; Q16850; -.
DR   CleanEx; HS_CYP51A1; -.
DR   GermOnline; ENSG00000001630; Homo sapiens.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008398; F:sterol 14-demethylase activity; IEA:EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Cholesterol biosynthesis; Endoplasmic reticulum; Heme; Iron;
KW   Lipid synthesis; Membrane; Metal-binding; Microsome; Monooxygenase;
KW   NADP; Oxidoreductase; Polymorphism; Steroid biosynthesis;
KW   Sterol biosynthesis; Transmembrane.
FT   CHAIN         1    503       Cytochrome P450 51A1.
FT                                /FTId=PRO_0000051998.
FT   TRANSMEM     24     44       Potential.
FT   METAL       449    449       Iron (heme axial ligand) (By similarity).
FT   VARIANT      13     13       V -> A (in dbSNP:rs2229188).
FT                                /FTId=VAR_023470.
FT   CONFLICT    272    272       R -> T (in Ref. 4; AAC50951).
FT   CONFLICT    368    368       K -> R (in Ref. 4; AAC50951).
FT   CONFLICT    377    377       I -> V (in Ref. 6; AAH32322).
SQ   SEQUENCE   503 AA;  56806 MW;  4FCEC147FB4DED86 CRC64;
     MLLLGLLQAG GSVLGQAMEK VTGGNLLSML LIACAFTLSL VYLIRLAAGH LVQLPAGVKS
     PPYIFSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM VGKTFTYLLG SDAAALLFNS
     KNEDLNAEDV YSRLTTPVFG KGVAYDVPNP VFLEQKKMLK SGLNIAHFKQ HVSIIEKETK
     EYFESWGESG EKNVFEALSE LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFSHAAWL
     LPGWLPLPSF RRRDRAHREI KDIFYKAIQK RRQSQEKIDD ILQTLLDATY KDGRPLTDDE
     VAGMLIGLLL AGQHTSSTTS AWMGFFLARD KTLQKKCYLE QKTVCGENLP PLTYDQLKDL
     NLLDRCIKET LRLRPPIMIM MRMARTPQTV AGYTIPPGHQ VCVSPTVNQR LKDSWVERLD
     FNPDRYLQDN PASGEKFAYV PFGAGRHRCI GENFAYVQIK TIWSTMLRLY EFDLIDGYFP
     TVNYTTMIHT PENPVIRYKR RSK
//