LBR_CHICK
ID LBR_CHICK Reviewed; 637 AA.
AC P23913;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Delta(14)-sterol reductase LBR;
DE Short=Delta-14-SR;
DE EC=1.3.1.70 {ECO:0000250|UniProtKB:Q14739};
DE AltName: Full=3-beta-hydroxysterol Delta (14)-reductase {ECO:0000250|UniProtKB:Q14739};
DE AltName: Full=C-14 sterol reductase;
DE Short=C14SR;
DE AltName: Full=Integral nuclear envelope inner membrane protein {ECO:0000303|PubMed:2170422};
DE AltName: Full=Lamin-B receptor {ECO:0000303|PubMed:2170422};
DE AltName: Full=Sterol C14-reductase;
GN Name=LBR;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=2170422; DOI=10.1083/jcb.111.4.1535;
RA Worman H.J., Evans C.D., Blobel G.;
RT "The lamin B receptor of the nuclear envelope inner membrane: a polytopic
RT protein with eight potential transmembrane domains.";
RL J. Cell Biol. 111:1535-1542(1990).
RN [2]
RP STRUCTURE BY NMR OF 1-62, AND DOMAIN TUDOR.
RX PubMed=22052904; DOI=10.1074/jbc.m111.281303;
RA Liokatis S., Edlich C., Soupsana K., Giannios I., Panagiotidou P.,
RA Tripsianes K., Sattler M., Georgatos S.D., Politou A.S.;
RT "Solution structure and molecular interactions of lamin B receptor tudor
RT domain.";
RL J. Biol. Chem. 287:1032-1042(2012).
CC -!- FUNCTION: Catalyzes the reduction of the C14-unsaturated bond of
CC lanosterol, as part of the metabolic pathway leading to cholesterol
CC biosynthesis (By similarity). Anchors the lamina and the
CC heterochromatin to the inner nuclear membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q14739, ECO:0000250|UniProtKB:Q3U9G9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-cholest-8,14-dien-3beta-ol + H(+) + NADPH = 5alpha-
CC cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46456,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16608, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:86131;
CC Evidence={ECO:0000250|UniProtKB:Q14739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) =
CC 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH;
CC Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813,
CC ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70;
CC Evidence={ECO:0000250|UniProtKB:Q14739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-8,14-cholestadien-3beta-ol + H(+) + NADPH = 4,4-
CC dimethyl-5alpha-cholest-8-en-3beta-ol + NADP(+);
CC Xref=Rhea:RHEA:46812, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78904, ChEBI:CHEBI:87044;
CC Evidence={ECO:0000250|UniProtKB:Q14739};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC -!- SUBUNIT: Interacts with DNA (By similarity). Interaction with DNA is
CC sequence independent with higher affinity for supercoiled and relaxed
CC circular DNA than linear DNA (By similarity).
CC {ECO:0000250|UniProtKB:Q14739}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:2170422}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim.
CC {ECO:0000250|UniProtKB:Q14739}.
CC -!- DOMAIN: The Tudor domain may not recognize methylation marks, but
CC rather bind unassembled free histone H3. {ECO:0000269|PubMed:22052904}.
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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DR EMBL; Y00822; CAA68758.1; -; mRNA.
DR PIR; A36427; A36427.
DR RefSeq; NP_990673.1; NM_205342.1.
DR PDB; 2L8D; NMR; -; A=1-62.
DR PDBsum; 2L8D; -.
DR AlphaFoldDB; P23913; -.
DR BMRB; P23913; -.
DR SMR; P23913; -.
DR IntAct; P23913; 1.
DR MINT; P23913; -.
DR STRING; 9031.ENSGALP00000015128; -.
DR iPTMnet; P23913; -.
DR PaxDb; P23913; -.
DR PRIDE; P23913; -.
DR GeneID; 396285; -.
DR KEGG; gga:396285; -.
DR CTD; 3930; -.
DR VEuPathDB; HostDB:geneid_396285; -.
DR eggNOG; KOG1435; Eukaryota.
DR InParanoid; P23913; -.
DR OrthoDB; 532774at2759; -.
DR PhylomeDB; P23913; -.
DR UniPathway; UPA00063; -.
DR PRO; PR:P23913; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0050613; F:delta14-sterol reductase activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
DR GO; GO:0006695; P:cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030223; P:neutrophil differentiation; ISS:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR CDD; cd04508; TUDOR; 1.
DR InterPro; IPR001171; ERG24_DHCR-like.
DR InterPro; IPR019023; Lamin-B_rcpt_of_tudor.
DR InterPro; IPR018083; Sterol_reductase_CS.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF01222; ERG4_ERG24; 1.
DR Pfam; PF09465; LBR_tudor; 1.
DR SMART; SM00333; TUDOR; 1.
DR PROSITE; PS01017; STEROL_REDUCT_1; 1.
DR PROSITE; PS01018; STEROL_REDUCT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm;
KW DNA-binding; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Nucleus; Oxidoreductase; Phosphoprotein; Receptor;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..637
FT /note="Delta(14)-sterol reductase LBR"
FT /id="PRO_0000207511"
FT TOPO_DOM 1..205
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..62
FT /note="Tudor"
FT REGION 57..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..97
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 96
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2L8D"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2L8D"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:2L8D"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:2L8D"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2L8D"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:2L8D"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2L8D"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2L8D"
SQ SEQUENCE 637 AA; 73498 MW; 69D299002DB8ECE0 CRC64;
MPNRKYADGE VVMGRWPGSV LYYEVQVTSY DDASHLYTVK YKDGTELALK ESDIRLQSSF
KQRKSQSSSS SPSRRSRSRS RSRSPGRPAK GRRRSSSHSR EHKEDKKKII QETSLAPPKP
SENNTRRYNG EPDSTERNDT SSKLLEQQKL KPDVEMERVL DQYSLRSRRE EKKKEEIYAE
KKIFEAIKTP EKPSSKTKEL EFGGRFGTFM LMFFLPATVL YLVLMCKQDD PSLMNFPPLP
ALESLWETKV FGVFLLWFFF QALFYLLPIG KVVEGLPLSN PRKLQYRING FYAFLLTAAA
IGTLLYFQFE LHYLYDHFVQ FAVSAAAFSM ALSIYLYIRS LKAPEEDLAP GGNSGYLVYD
FFTGHELNPR IGSFDLKYFC ELRPGLIGWV VINLAMLLAE MKIHNQSMPS LSMILVNSFQ
LLYVVDALWN EEAVLTTMDI THDGFGFMLA FGDLVWVPFV YSLQAFYLVG HPIAISWPVA
AAITILNCIG YYIFRSANSQ KNNFRRNPAD PKLSYLKVIP TATGKGLLVT GWWGFVRHPN
YLGDIIMALA WSLPCGFNHI LPYFYVIYFI CLLVHREARD EHHCKKKYGL AWERYCQRVP
YTHISLHLLE HSTYLICKLK YTSHLCTWSV CYLGFKH
