ID A0A091KJP8_9GRUI Unreviewed; 614 AA.
AC A0A091KJP8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=N324_06285 {ECO:0000313|EMBL:KFP39425.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP39425.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP39425.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP39425.1};
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; KK743345; KFP39425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091KJP8; -.
DR UniPathway; UPA00063; -.
DR Proteomes; UP000053330; 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:KFP39425.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053330};
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 207..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..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 53..144
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..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 70767 MW; FC940B95B29CD999 CRC64;
MPNRRFADGE VVMGRWPGSV LYYEVQVTSY DDVSHLYTVK YKDGTELALK ESDIRSQSSF
KHRKSQSSSS SPSRRSSSRS RSRSPGRPAK GRRRSSSQSR EHKDDKKKTI QETNLALPVF
SFNQKPSENN TRRYNGEPDS TERNDTSCLI LEQKLKPDLE VERVLEQYSL RPRKEEKKKE
EIYSEKKVFE TIKTIEKASS KTKELEFGGR IGAFTLIFFL PATVFYLLLM CKQDDPSLMN
FPPPLPALES LWEPRVFGVV LLWFFLQALF YLLPIGKVVE GLPLSNGRKL QYRINGFYAF
VLTAAAIGTL LYFQFELHYL YDHFMQFAVS AAAFSVGLSI FLYIRSLKAP EEELAPGGNS
GYFVYDFFTG HELNPRIGSF DLKYFCELRP GLIGWVVINL AMLLAEMKIH NQSMPSLSMV
LVNSFQLLYV VDALWNEEAV LTTMDITHDG FGFMLVFGDL VWVPFVYSLQ AFYLVGHPTA
VSWPVAAAIT ILNCIGYYIF RRANSQKNSF RRNPSDPKLA YLKFIPTATG KGLLVTGWWG
FVRHPNYLGD IIMALAWSLP CGFNHILPYF YVIYFICLLV HREARDEHHC KQKYGLAWER
YCQRVPYRIF PYIY
//
