ID A0A6J3QXD3_TURTR Unreviewed; 594 AA.
AC A0A6J3QXD3;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
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_033707066.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033707066.1};
RN [1] {ECO:0000313|RefSeq:XP_033707066.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_033707066.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_033707066.1; XM_033851175.1.
DR AlphaFoldDB; A0A6J3QXD3; -.
DR UniPathway; UPA00063; -.
DR Proteomes; UP000245320; Chromosome 1.
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; 2.
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:UP000245320};
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 218..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..62
FT /note="Tudor"
FT /evidence="ECO:0000259|SMART:SM00333"
FT REGION 53..111
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"
SQ SEQUENCE 594 AA; 68304 MW; 0128C69F057A13E2 CRC64;
MPSRKFADGE VVRGRWPGSS LYYEVEILSH DSNSQLYNVR YKDGTELELK ESDIKPLTSF
RQRKSGSTSS SPSRRRGSRS RSRSRSPGRP PKGSRPSVSA SHQAHIKEAK KEARKEILEV
KLTPLVLKPF GNSINRYNGE PEHIERNDIP HKNTQEKFPL SQESSYILTQ YSLHPRREEV
KLKEIDSKEE KIVTKGPTSL RTFEVTATQQ KDLEFGGVPG VFLITLGLPA FLFLLLLMCK
QEEPSLLNFP PPLPALYDLW ETRVFGAYLL WFFLQALFYL LPIGKVVEGT PLTDGRRLKY
RLNGFYAFIL TSVLVGASLF WDVELYYVYS HFLQCALAAT VFSVVLSVYL YARALKAPRD
ELSPASSGNA VYDFFIGREL NPRIGTFDLK YFCELRPGLI GWVVINLVML LAEMKLQHRT
VPSLAMILVN SFQLLYVVDA LWNEEALLTT MDIIHDGFGF MLAFGDLVWV PFIYSFQAFY
LVSHPNELSW PMASLIIALK HLKTIHTSTG KNLLVSGWWG FVRHPNYLGD LIMALAWSLP
CGFNHVLPYF YVIYFTILLV HREARDERHC RKKYGLAWEK YCQRVPYRIF PYIY
//
