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CP51A_PONAB
ID   CP51A_PONAB             Reviewed;         509 AA.
AC   Q5RE72;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 3.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Lanosterol 14-alpha demethylase {ECO:0000250|UniProtKB:Q16850};
DE            Short=LDM;
DE            EC=1.14.14.154 {ECO:0000250|UniProtKB:Q16850, ECO:0000250|UniProtKB:Q64654};
DE   AltName: Full=CYPLI;
DE   AltName: Full=Cytochrome P450 51A1;
DE   AltName: Full=Cytochrome P450-14DM;
DE            Short=Cytochrome P45014DM;
DE   AltName: Full=Cytochrome P450LI;
DE   AltName: Full=Sterol 14-alpha demethylase;
GN   Name=CYP51A1 {ECO:0000250|UniProtKB:Q16850};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: A cytochrome P450 monooxygenase involved in sterol
CC       biosynthesis. Catalyzes 14-alpha demethylation of lanosterol and 24,25-
CC       dihydrolanosterol likely through sequential oxidative conversion of 14-
CC       alpha methyl group to hydroxymethyl, then to carboxylaldehyde, followed
CC       by the formation of the delta 14,15 double bond in the sterol core and
CC       concomitant release of formic acid. Mechanistically, uses molecular
CC       oxygen inserting one oxygen atom into a substrate, and reducing the
CC       second into a water molecule, with two electrons provided by NADPH via
CC       cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
CC       {ECO:0000250|UniProtKB:Q16850, ECO:0000250|UniProtKB:Q64654}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--
CC         hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4
CC         H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154;
CC         Evidence={ECO:0000250|UniProtKB:Q16850,
CC         ECO:0000250|UniProtKB:Q64654};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029;
CC         Evidence={ECO:0000250|UniProtKB:Q16850,
CC         ECO:0000250|UniProtKB:Q64654};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC         4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4
CC         H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154;
CC         Evidence={ECO:0000250|UniProtKB:Q16850,
CC         ECO:0000250|UniProtKB:Q64654};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287;
CC         Evidence={ECO:0000250|UniProtKB:Q16850,
CC         ECO:0000250|UniProtKB:Q64654};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=24,25-dihydrolanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein
CC         reductase] = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + 4
CC         H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:45960, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:28113, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:78904;
CC         Evidence={ECO:0000250|UniProtKB:Q16850,
CC         ECO:0000250|UniProtKB:Q64654};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45961;
CC         Evidence={ECO:0000250|UniProtKB:Q16850,
CC         ECO:0000250|UniProtKB:Q64654};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q16850};
CC   -!- ACTIVITY REGULATION: Inhibited by azalanstat. Inhibited by azole
CC       antifungal agents ketoconazole, itraconazole and fluconazole.
CC       {ECO:0000250|UniProtKB:Q64654}.
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC       lanosterol: step 1/6. {ECO:0000250|UniProtKB:Q64654}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q64654}; Single-pass membrane protein
CC       {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:Q64654};
CC       Single-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; CR857665; CAH89935.1; -; mRNA.
DR   RefSeq; NP_001124908.1; NM_001131436.1.
DR   AlphaFoldDB; Q5RE72; -.
DR   SMR; Q5RE72; -.
DR   STRING; 9601.ENSPPYP00000019976; -.
DR   PRIDE; Q5RE72; -.
DR   Ensembl; ENSPPYT00000020764; ENSPPYP00000019976; ENSPPYG00000017824.
DR   GeneID; 100171776; -.
DR   KEGG; pon:100171776; -.
DR   CTD; 1595; -.
DR   eggNOG; KOG0684; Eukaryota.
DR   GeneTree; ENSGT00930000151026; -.
DR   HOGENOM; CLU_001570_15_0_1; -.
DR   InParanoid; Q5RE72; -.
DR   OrthoDB; 572303at2759; -.
DR   TreeFam; TF105091; -.
DR   UniPathway; UPA00770; UER00754.
DR   Proteomes; UP000001595; Chromosome 7.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cholesterol biosynthesis; Cholesterol metabolism; Endoplasmic reticulum;
KW   Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW   Microsome; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..509
FT                   /note="Lanosterol 14-alpha demethylase"
FT                   /id="PRO_0000377745"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         455
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   509 AA;  57317 MW;  D46858B128CBDE99 CRC64;
     MAAAAGMMLL GLLQAGGSVL GQAMEKVTGG NLLSMLLIAC AFTLSLVYLF RLAVGHLVQL
     PAGAKSPPYI FSPIPFLGHA IAFGKSPIEF LENAYEKYGP VFSFTMVGKT FTYLLGSDAA
     ALLFNSKNED LNAEDVYSRL TTPVFGKGVA YDVPNPVFLE QKKMLKSGLN IAHFKQHVSI
     IEKETKEYFE SWGESGEKNV FEALSELIIL TASHCLHGKE VRSQLNEKVA QLYADLDGGF
     SHAAWLLPGW LPLPSFRRRD RAHREIKDIF YKAIQKRRQS QEKIDDILQT LLDATYKDGR
     PLTDDEVAGM LIGLLLAGQH TSSTTSAWMG FFLARDKTLQ EKCYLEQKTV CGENLPPLTY
     DQLKDLNLLD RCIKETLRLR PPIMIMMRMA RTPQTVAGYT IPPGHQVCVS PTVNQRLKDS
     WVERLDFNPD RYLQDNPASG EKFAYVPFGA GRHRCIGENF AYVQIKTIWS TMLRLYEFDL
     IDGYFPTVNY TTMIHTPENP VIRYKRRSK
 
 
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