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UniProtKB/Swiss-Prot entry Q16850


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

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Entry information
Entry name CP51A_HUMAN
Primary accession number Q16850
Secondary accession numbers O00770 O00772 Q16784 Q8N1A8 Q99868
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on December 15, 1998 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 76)
Name and origin of the protein
Protein name Cytochrome P450 51A1
Synonyms EC 1.14.13.70
CYPLI
P450LI
Sterol 14-alpha demethylase
Lanosterol 14-alpha demethylase
LDM
P450-14DM
P45014DM
Gene name
Name: CYP51A1
Synonyms: CYP51
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1006/abbi.1996.0193; PubMed=8619637 [NCBI, ExPASy, EBI, Israel, Japan]
Stroemstedt M., Rozman D., Waterman M.R.;
"The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols.";
Arch. Biochem. Biophys. 329:73-81(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8797093 [NCBI, ExPASy, EBI, Israel, Japan]
Aoyama Y., Noshiro M., Gotoh O., Imaoka S., Funae Y., Kurosawa N., Horiuchi T., Yoshida Y.;
"Sterol 14-demethylase P450 (P45014DM*) is one of the most ancient and conserved P450 species.";
J. Biochem. 119:926-933(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
DOI=10.1006/abbi.1996.0416; PubMed=8809088 [NCBI, ExPASy, EBI, Israel, Japan]
Rozman D., Stroemstedt M., Waterman M.R.;
"The three human cytochrome P450 lanosterol 14 alpha-demethylase (CYP51) genes reside on chromosomes 3, 7, and 13: structure of the two retrotransposed pseudogenes, association with a line-1 element, and evolution of the human CYP51 family.";
Arch. Biochem. Biophys. 333:466-474(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/geno.1996.0640; PubMed=8975714 [NCBI, ExPASy, EBI, Israel, Japan]
Rozman D., Stroemstedt M., Tsui L.-C., Scherer S.W., Waterman M.R.;
"Structure and mapping of the human lanosterol 14alpha-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes.";
Genomics 38:371-381(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
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
U23942; AAB39951.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D55653; BAA09512.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51692; AAC50951.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51684; AAC50951.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51685; AAC50951.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51686; AAC50951.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51687; AAC50951.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51688; AAC50951.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51689; AAC50951.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51690; AAC50951.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51691; AAC50951.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC000120; AAB46356.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032322; AAH32322.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC4759; JC4759.
S68855; S68855.
RefSeq NP_000777.1; -.
UniGene Hs.417077
3D structure databases
HSSP P77901; 1E9X. [HSSP ENTRY / PDB]
ModBase Q16850.
Enzyme and pathway databases
BioCyc MetaCyc:ENSG00000001630-MON; -.
Reactome REACT_602; Lipid and lipoprotein metabolism.
Organism-specific databases
H-InvDB HIX0021935; -.
HGNC HGNC:2649; CYP51A1.
GenAtlas CYP51A1.
MIM 601637; gene. [NCBI / EBI]
PharmGKB PA27123; -.
GeneCards Q16850.
Gene expression databases
ArrayExpress Q16850; -.
CleanEx HS_CYP51A1; -.
GermOnline ENSG00000001630; Homo sapiens.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from experiment from Reactome).
GO:0008398; Molecular function: sterol 14-demethylase activity (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR001128; Cyt_P450.
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.
BLOCKS Q16850.
Genome annotation databases
Ensembl ENSG00000001630; Homo sapiens. [Contig view]
GeneID 1595; -.
KEGG hsa:1595; -.
Phylogenomic databases
HOGENOM Q16850; -.
HOVERGEN Q16850; -.
Other
DrugBank DB00196; Fluconazole.
DB01167; Itraconazole.
DB01026; Ketoconazole.
DB01110; Miconazole.
DB00251; Terconazole.
SOURCE CYP51A1; Homo sapiens.
ProtoNet Q16850.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cholesterol biosynthesis; Endoplasmic reticulum; Heme; Iron; Lipid synthesis; Membrane; Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; Polymorphism; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   503  503     Cytochrome P450 51A1. PRO_0000051998
TRANSMEM   24    44  21     Potential. 
METAL   449   449        Iron (heme axial ligand) (By similarity). 
VARIANT   13    13  1     V -> A (in dbSNP:rs2229188 [NCBI]). VAR_023470 
CONFLICT   272   272        R -> T (in Ref. 4; AAC50951). 
CONFLICT   368   368        K -> R (in Ref. 4; AAC50951). 
CONFLICT   377   377        I -> V (in Ref. 6; AAH32322). 
Sequence information
Length: 503 AA [This is the length of the unprocessed precursor] Molecular weight: 56806 Da [This is the MW of the unprocessed precursor] CRC64: 4FCEC147FB4DED86 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLLLGLLQAG GSVLGQAMEK VTGGNLLSML LIACAFTLSL VYLIRLAAGH LVQLPAGVKS 

        70         80         90        100        110        120 
PPYIFSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM VGKTFTYLLG SDAAALLFNS 

       130        140        150        160        170        180 
KNEDLNAEDV YSRLTTPVFG KGVAYDVPNP VFLEQKKMLK SGLNIAHFKQ HVSIIEKETK 

       190        200        210        220        230        240 
EYFESWGESG EKNVFEALSE LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFSHAAWL 

       250        260        270        280        290        300 
LPGWLPLPSF RRRDRAHREI KDIFYKAIQK RRQSQEKIDD ILQTLLDATY KDGRPLTDDE 

       310        320        330        340        350        360 
VAGMLIGLLL AGQHTSSTTS AWMGFFLARD KTLQKKCYLE QKTVCGENLP PLTYDQLKDL 

       370        380        390        400        410        420 
NLLDRCIKET LRLRPPIMIM MRMARTPQTV AGYTIPPGHQ VCVSPTVNQR LKDSWVERLD 

       430        440        450        460        470        480 
FNPDRYLQDN PASGEKFAYV PFGAGRHRCI GENFAYVQIK TIWSTMLRLY EFDLIDGYFP 

       490        500 
TVNYTTMIHT PENPVIRYKR RSK 

Q16850 in FASTA format

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View entry in raw text format (no links)
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