ID   A0A0C4DFL7_HUMAN        Unreviewed;       509 AA.
AC   A0A0C4DFL7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   13-FEB-2019, entry version 35.
DE   SubName: Full=Lanosterol 14-alpha demethylase {ECO:0000313|Ensembl:ENSP00000003100};
GN   Name=CYP51A1 {ECO:0000313|Ensembl:ENSP00000003100};
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 {ECO:0000313|Ensembl:ENSP00000003100, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000003100, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   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   [2] {ECO:0000213|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [3] {ECO:0000213|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [4] {ECO:0000213|PubMed:25944712}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [5] {ECO:0000313|Ensembl:ENSP00000003100}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|RuleBase:RU000461, ECO:0000256|SAAS:SAAS00578476}.
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DR   EMBL; AC000120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_000777.1; NM_000786.3.
DR   UniGene; Hs.417077; -.
DR   ProteinModelPortal; A0A0C4DFL7; -.
DR   SMR; A0A0C4DFL7; -.
DR   EPD; A0A0C4DFL7; -.
DR   jPOST; A0A0C4DFL7; -.
DR   MaxQB; A0A0C4DFL7; -.
DR   PeptideAtlas; A0A0C4DFL7; -.
DR   PRIDE; A0A0C4DFL7; -.
DR   Ensembl; ENST00000003100; ENSP00000003100; ENSG00000001630.
DR   GeneID; 1595; -.
DR   KEGG; hsa:1595; -.
DR   CTD; 1595; -.
DR   EuPathDB; HostDB:ENSG00000001630.15; -.
DR   HGNC; HGNC:2649; CYP51A1.
DR   OpenTargets; ENSG00000001630; -.
DR   eggNOG; KOG0684; Eukaryota.
DR   eggNOG; COG2124; LUCA.
DR   GeneTree; ENSGT00930000151026; -.
DR   KO; K05917; -.
DR   OMA; APIHSIM; -.
DR   OrthoDB; 572303at2759; -.
DR   PhylomeDB; A0A0C4DFL7; -.
DR   ChiTaRS; CYP51A1; human.
DR   GenomeRNAi; 1595; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000001630; Expressed in 98 organ(s), highest expression level in adrenal tissue.
DR   ExpressionAtlas; A0A0C4DFL7; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:Ensembl.
DR   GO; GO:0033488; P:cholesterol biosynthetic process via 24,25-dihydrolanosterol; IEA:Ensembl.
DR   GO; GO:1900222; P:negative regulation of amyloid-beta clearance; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Heme {ECO:0000256|RuleBase:RU000461, ECO:0000256|SAAS:SAAS01092997};
KW   Iron {ECO:0000256|RuleBase:RU000461, ECO:0000256|SAAS:SAAS01092997};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461,
KW   ECO:0000256|SAAS:SAAS01092997};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461,
KW   ECO:0000256|SAAS:SAAS00966021};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461,
KW   ECO:0000256|SAAS:SAAS00966021};
KW   Proteomics identification {ECO:0000213|EPD:A0A0C4DFL7,
KW   ECO:0000213|MaxQB:A0A0C4DFL7, ECO:0000213|PeptideAtlas:A0A0C4DFL7};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    509       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002178490.
FT   TRANSMEM     31     50       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   509 AA;  57278 MW;  F9145DDB65F94091 CRC64;
     MAAAAGMLLL GLLQAGGSVL GQAMEKVTGG NLLSMLLIAC AFTLSLVYLI RLAAGHLVQL
     PAGVKSPPYI FSPIPFLGHA IAFGKSPIEF LENAYEKYGP VFSFTMVGKT FTYLLGSDAA
     ALLFNSKNED LNAEDVYSRL TTPVFGKGVA YDVPNPVFLE QKKMLKSGLN IAHFKQHVSI
     IEKETKEYFE SWGESGEKNV FEALSELIIL TASHCLHGKE IRSQLNEKVA QLYADLDGGF
     SHAAWLLPGW LPLPSFRRRD RAHREIKDIF YKAIQKRRQS QEKIDDILQT LLDATYKDGR
     PLTDDEVAGM LIGLLLAGQH TSSTTSAWMG FFLARDKTLQ KKCYLEQKTV CGENLPPLTY
     DQLKDLNLLD RCIKETLRLR PPIMIMMRMA RTPQTVAGYT IPPGHQVCVS PTVNQRLKDS
     WVERLDFNPD RYLQDNPASG EKFAYVPFGA GRHRCIGENF AYVQIKTIWS TMLRLYEFDL
     IDGYFPTVNY TTMIHTPENP VIRYKRRSK
//