LSS_BOVIN
ID LSS_BOVIN Reviewed; 732 AA.
AC P84466; Q2EMV7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Lanosterol synthase;
DE EC=5.4.99.7 {ECO:0000269|PubMed:14678783};
DE AltName: Full=2,3-epoxysqualene--lanosterol cyclase;
DE AltName: Full=Oxidosqualene--lanosterol cyclase;
DE Short=OSC;
GN Name=LSS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Chang C.-H., Huang C.-Y., Ko C.-Y., Wu T.-K.;
RT "Molecular cloning and active-site mapping of oxidosqualene-lanosterol
RT cyclase from bovine liver.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 163-174; 247-258 AND 493-506, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000269|PubMed:14678783};
RX PubMed=14678783; DOI=10.1016/j.abb.2003.09.036;
RA Wu T.-K., Huang C.-Y., Ko C.-Y., Chang C.-H., Chen Y.-J., Liao H.-K.;
RT "Purification, tandem mass characterization, and inhibition studies of
RT oxidosqualene-lanosterol cyclase enzyme from bovine liver.";
RL Arch. Biochem. Biophys. 421:42-53(2004).
CC -!- FUNCTION: Key enzyme in the cholesterol biosynthesis pathway. Catalyzes
CC the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that
CC forms the sterol nucleus (PubMed:14678783). Through the production of
CC lanosterol may regulate lens protein aggregation and increase
CC transparency (By similarity). {ECO:0000250|UniProtKB:P48449,
CC ECO:0000269|PubMed:14678783}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = lanosterol; Xref=Rhea:RHEA:14621,
CC ChEBI:CHEBI:15441, ChEBI:CHEBI:16521; EC=5.4.99.7;
CC Evidence={ECO:0000269|PubMed:14678783};
CC -!- ACTIVITY REGULATION: Inhibited by the benzophenone containing OSC
CC inhibitor Ro48-8071 and to a lesser extent by other benzophene
CC containing inhibitors. {ECO:0000269|PubMed:14678783}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for (3S)-2,3-oxidosqualine {ECO:0000269|PubMed:14678783};
CC pH dependence:
CC Optimum pH is 7.4. Active from pH 5.0 to 10.0.
CC {ECO:0000269|PubMed:14678783};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. Active from 25 to 50
CC degrees Celsius. {ECO:0000269|PubMed:14678783};
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC farnesyl diphosphate: step 3/3. {ECO:0000269|PubMed:14678783}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48449}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P48449}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P48449}.
CC -!- TISSUE SPECIFICITY: Detected in the liver (at protein level).
CC {ECO:0000269|PubMed:14678783}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000250|UniProtKB:P48449}.
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DR EMBL; DQ372933; ABD24094.1; -; mRNA.
DR RefSeq; NP_001040029.1; NM_001046564.1.
DR AlphaFoldDB; P84466; -.
DR SMR; P84466; -.
DR STRING; 9913.ENSBTAP00000025201; -.
DR PaxDb; P84466; -.
DR PRIDE; P84466; -.
DR GeneID; 615906; -.
DR KEGG; bta:615906; -.
DR CTD; 4047; -.
DR eggNOG; KOG0497; Eukaryota.
DR InParanoid; P84466; -.
DR OrthoDB; 365003at2759; -.
DR SABIO-RK; P84466; -.
DR UniPathway; UPA00767; UER00753.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0000250; F:lanosterol synthase activity; IDA:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006694; P:steroid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd02892; SQCY_1; 1.
DR InterPro; IPR032696; SQ_cyclase_C.
DR InterPro; IPR032697; SQ_cyclase_N.
DR InterPro; IPR018333; Squalene_cyclase.
DR InterPro; IPR002365; Terpene_synthase_CS.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11764; PTHR11764; 1.
DR Pfam; PF13243; SQHop_cyclase_C; 1.
DR Pfam; PF13249; SQHop_cyclase_N; 1.
DR SFLD; SFLDG01016; Prenyltransferase_Like_2; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR TIGRFAMs; TIGR01787; squalene_cyclas; 1.
DR PROSITE; PS01074; TERPENE_SYNTHASES; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endoplasmic reticulum; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome; Repeat;
KW Steroid biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT CHAIN 2..732
FT /note="Lanosterol synthase"
FT /id="PRO_0000072658"
FT REPEAT 124..165
FT /note="PFTB 1"
FT REPEAT 483..528
FT /note="PFTB 2"
FT REPEAT 560..600
FT /note="PFTB 3"
FT REPEAT 612..663
FT /note="PFTB 4"
FT REPEAT 670..712
FT /note="PFTB 5"
FT ACT_SITE 455
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 732 AA; 83184 MW; B06289C2FE03B4B2 CRC64;
MTEGTCLRRR GGPYKTEPAT DLSRWRLSNQ VGRQTWTYSQ EEDPVREQSG LEAHLLGLDT
KSFFKDLPKA HTACRGALNG VTFYAALQTE DGHWAGDYGG PLFLLPGLLI TCHVANIPLP
AGYREEIIRY LRSVQLPDGG WGLHIEDKST VFGTALNYVS LRILGVGPDD PDLVRARNLL
HKKGGAVFIP SWGKFWLAVL NVYSWEGLNT LFPEMWLFPD WMPAHPSTIW CHCRQVYLPM
AYCYSTRLSA EEGPLVQSLR QELYLEDYSC IDWAAHRNSV APDDLYTPHS WLLHVVYAIL
NLYERHHSTS LRQWATQKLY EHIAADDRFT KCISIGPISK TINMLVRWHV DGPASAVFQE
HVSRIPDYLW LGLDGMKMQG TNGSQIWDTA FAIQALLEAR AQHRPEFWSC LRKAHEYLRI
SQVPDNFPDY QKYYRHMSKG GFSFSTLDCG WIVADCTAEA LKSILLLQEK CPFVSNHVPR
ERLFDTVAVL LSLRNPDGGF ATYETKRGGH LLELLNPSEV FGDIMIDYTY VECTSAVMQA
LKTFHKQFPD HRAGEIRETL EQGLQFCRQK QRPDGSWEGS WGVCFTYGAW FGLEAFACMG
HTYHNGVACA EISRACDFLL SRQMADGGWG EDFESCKQRR YVQSAQSQIH NTCWALMGLM
AVRHPDVAAL ERGVSYLLEK QLPNGDWPQE NISGVFNKSC AISYTSYRNV FPIWTLGRFS
RLHPDPALAG HP
