ID A0A093NAT2_PYGAD Unreviewed; 614 AA.
AC A0A093NAT2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-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 ORFNames=AS28_00144 {ECO:0000313|EMBL:KFW62083.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW62083.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW62083.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW62083.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL224621; KFW62083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093NAT2; -.
DR STRING; 9238.A0A093NAT2; -.
DR UniPathway; UPA00063; -.
DR Proteomes; UP000054081; Unassembled WGS sequence.
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, ECO:0000313|EMBL:KFW62083.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054081};
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 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..62
FT /note="Tudor"
FT /evidence="ECO:0000259|SMART:SM00333"
FT REGION 54..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 70971 MW; E3CC24ADD1E59DCB CRC64;
MPNRRFADGE VVMGRWPGSI LYYEVQVTSY DDVSHLYIVK YKDGTELALK ESDIRSQSSF
KHRKSQSSSS SPSRRSTSRS RSRSPGRPAK GRRRSSSQSR EHKDDKKKTI QETNLALLVL
VFLFKPSENN TRRYNGEPDS TERNDTSCII LEQKLKPELE IERVLEQYSL HPRKEEKKKE
ERHSEKKFFE AIKTIEKASP KTKELEFGGR IGTFMLIFFL PATVFYLLLM CKQDDPSLMN
FPPPLPALES LWEARVFGVF LLWFFLQALF YLLPIGKVVE GLPLSNGRKL QYRINGFYAF
ILTAAAIGAL LYFQFELHYL YDHFMQFAVS AAAFSMVLSI YLYIRSLKAP EEELAPGGNS
GYFVYDFFTG HELNPRIGSF DLKYFCELRP GLIGWVVINL AMLLAEMKIH NQSMPSLSMI
LVNSFQLLYV VDALWNEEAI LTTMDITHDG FGFMLAFGDL VWVPFVYSLQ AFYLVGHPTA
ISWPVAAAIT ILNCIGYYIF RSANSQKNNF RRNPADPKLA YLKFIPTATG KGLLVTGWWG
FVRHPNYLGD IIMALAWSLP CGFNHILPYF YVIYFICLLV HREARDEHHC KQKYGVAWER
YCQRVPYRIF PYIY
//
