ID A0A2Y9GAJ9_NEOSC Unreviewed; 618 AA.
AC A0A2Y9GAJ9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Delta(14)-sterol reductase LBR {ECO:0000256|ARBA:ARBA00017801};
DE EC=1.3.1.70 {ECO:0000256|ARBA:ARBA00012413};
DE AltName: Full=3-beta-hydroxysterol Delta (14)-reductase {ECO:0000256|ARBA:ARBA00032210};
DE AltName: Full=C-14 sterol reductase {ECO:0000256|ARBA:ARBA00030165};
DE AltName: Full=Integral nuclear envelope inner membrane protein {ECO:0000256|ARBA:ARBA00029624};
DE AltName: Full=Lamin-B receptor {ECO:0000256|ARBA:ARBA00030798};
DE AltName: Full=Sterol C14-reductase {ECO:0000256|ARBA:ARBA00031227};
GN Name=LBR {ECO:0000313|RefSeq:XP_021535135.1};
OS Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Neomonachus.
OX NCBI_TaxID=29088 {ECO:0000313|Proteomes:UP000248481, ECO:0000313|RefSeq:XP_021535135.1};
RN [1] {ECO:0000313|RefSeq:XP_021535135.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_021535135.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001086};
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:0000256|ARBA:ARBA00000573};
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:0000256|ARBA:ARBA00001598};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004770}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus inner membrane
CC {ECO:0000256|ARBA:ARBA00004473}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004473}.
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family.
CC {ECO:0000256|ARBA:ARBA00005402}.
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DR RefSeq; XP_021535135.1; XM_021679460.2.
DR AlphaFoldDB; A0A2Y9GAJ9; -.
DR STRING; 29088.A0A2Y9GAJ9; -.
DR KEGG; nsu:110571361; -.
DR InParanoid; A0A2Y9GAJ9; -.
DR OrthoDB; 275939at2759; -.
DR UniPathway; UPA00063; -.
DR Proteomes; UP000248481; Chromosome 6.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050613; F:delta14-sterol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd20381; Tudor_LBR; 1.
DR Gene3D; 1.20.120.1630; -; 1.
DR Gene3D; 2.30.30.140; -; 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 PANTHER; PTHR21257; DELTA(14)-STEROL REDUCTASE; 1.
DR PANTHER; PTHR21257:SF52; DELTA(14)-STEROL REDUCTASE LBR; 1.
DR Pfam; PF01222; ERG4_ERG24; 1.
DR Pfam; PF09465; LBR_tudor; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS01017; STEROL_REDUCT_1; 1.
DR PROSITE; PS01018; STEROL_REDUCT_2; 1.
PE 3: Inferred from homology;
KW Cholesterol biosynthesis {ECO:0000256|ARBA:ARBA00022778};
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000248481};
KW Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 485..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 566..585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..62
FT /note="Tudor"
FT /evidence="ECO:0000259|SMART:SM00333"
FT REGION 52..105
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..90
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 70184 MW; 378E60C562093EA4 CRC64;
MPSRKFADGE VVRGRWPGSS LYYEVEILSH DSHSQLYTVK YKDGTELELK ENDIKPLTSF
RQRKSGSTSS SPSRRRGSRS RSRSRSPGRP PRSSRRSASA SHQADIKEMR KEVLEVKLTP
LVLKPFGNSI SRYNGEPERT ERDGLPHRNT EEKFHLSEES SYISTQYSLR PRREEIKLKD
IDSKEENIVA TKGSTLLKTS EGPATQTEGL EFGGVPGVFL IMLGLPAFLF LLLLMCKQKE
PSLLNFPPPL PALSDLWETR VFGVYLLWFL LQALFYLLPV GKVVEGMPLT DGRRLKYRLN
GFYALLLTAA AIGAAVFWGL PLLFVYQHFL QLVLAAFAFT VALSTYLAVR AAGAPPAALA
PASSGNAIYD FFIGRELNPR IGTFDLKYFC ELRPGLIGWV VVNLVMLLAE MKLQDRAAPS
LAMILVNSFQ LLYVVDALWN EEALLTTMDI THDGFGFMLA FGDLVWVPFI YSFQAFYLVN
HPNEVSWPMA SLIIALKLCG YVIFRCANSQ KNAFRKNPSD PKLAHLKTIH TSTGKNLLVS
GWWGFVRHPN YLGDLIMALA WSLPCGFKHI LPYFYVIYFA MLLVHREARD ERQCRTKYGR
AWEQYRQRVP YRIVPYVY
//
