ERG24_ARATH
ID ERG24_ARATH Reviewed; 369 AA.
AC Q9LDR4; Q9LD62;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Delta(14)-sterol reductase;
DE EC=1.3.1.70 {ECO:0000305|PubMed:10859166, ECO:0000305|PubMed:10859167};
DE AltName: Full=C-14 sterol reductase;
DE AltName: Full=Protein FACKEL {ECO:0000303|PubMed:10859166};
DE AltName: Full=Sterol C14-reductase;
GN Name=FK; OrderedLocusNames=At3g52940; ORFNames=F8J2_111;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10859166;
RA Schrick K., Mayer U., Horrichs A., Kuhnt C., Bellini C., Dangl J.,
RA Schmidt J., Juergens G.;
RT "FACKEL is a sterol C-14 reductase required for organized cell division and
RT expansion in Arabidopsis embryogenesis.";
RL Genes Dev. 14:1471-1484(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10859167;
RA Jang J.-C., Fujioka S., Tasaka M., Seto H., Takatsuto S., Ishii A.,
RA Aida M., Yoshida S., Sheen J.;
RT "A critical role of sterols in embryonic patterning and meristem
RT programming revealed by the fackel mutants of Arabidopsis thaliana.";
RL Genes Dev. 14:1485-1497(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-
CC 8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Required
CC for cell division and expansion and is involved in proper organization
CC of the embryo. {ECO:0000269|PubMed:10859166,
CC ECO:0000269|PubMed:10859167}.
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:0000305|PubMed:10859166, ECO:0000305|PubMed:10859167};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18562;
CC Evidence={ECO:0000305|PubMed:10859167};
CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC lanosterol: step 2/6.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LDR4-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF81279.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC01296.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF256535; AAF82282.1; -; mRNA.
DR EMBL; AF256536; AAF82283.1; -; Genomic_DNA.
DR EMBL; AF257178; AAF81279.1; ALT_INIT; mRNA.
DR EMBL; AF263244; AAF82768.1; -; Genomic_DNA.
DR EMBL; AL132969; CAC01296.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE79013.1; -; Genomic_DNA.
DR EMBL; AY064964; AAL38381.1; -; mRNA.
DR EMBL; AY133650; AAM91480.1; -; mRNA.
DR RefSeq; NP_566975.1; NM_115154.3. [Q9LDR4-1]
DR AlphaFoldDB; Q9LDR4; -.
DR SMR; Q9LDR4; -.
DR STRING; 3702.AT3G52940.1; -.
DR PaxDb; Q9LDR4; -.
DR PRIDE; Q9LDR4; -.
DR ProteomicsDB; 220638; -. [Q9LDR4-1]
DR EnsemblPlants; AT3G52940.1; AT3G52940.1; AT3G52940. [Q9LDR4-1]
DR GeneID; 824460; -.
DR Gramene; AT3G52940.1; AT3G52940.1; AT3G52940. [Q9LDR4-1]
DR KEGG; ath:AT3G52940; -.
DR Araport; AT3G52940; -.
DR TAIR; locus:2085146; AT3G52940.
DR eggNOG; KOG1435; Eukaryota.
DR HOGENOM; CLU_015631_0_1_1; -.
DR InParanoid; Q9LDR4; -.
DR OMA; GWIILNC; -.
DR PhylomeDB; Q9LDR4; -.
DR BioCyc; ARA:AT3G52940-MON; -.
DR BioCyc; MetaCyc:AT3G52940-MON; -.
DR BRENDA; 1.3.1.70; 399.
DR UniPathway; UPA00770; UER00755.
DR PRO; PR:Q9LDR4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LDR4; baseline and differential.
DR Genevisible; Q9LDR4; AT.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0050613; F:delta14-sterol reductase activity; IMP:TAIR.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001171; ERG24_DHCR-like.
DR InterPro; IPR018083; Sterol_reductase_CS.
DR Pfam; PF01222; ERG4_ERG24; 1.
DR PROSITE; PS01017; STEROL_REDUCT_1; 1.
DR PROSITE; PS01018; STEROL_REDUCT_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..369
FT /note="Delta(14)-sterol reductase"
FT /id="PRO_0000207499"
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 265
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 289
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 294
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 301..302
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 341
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 345..349
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 356
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ SEQUENCE 369 AA; 41913 MW; F18674BCF27C0502 CRC64;
MLLDMDLGVL LPSLQSVYVL VFYFVYLAVA GEILPGKVIR GVLLSDGSQL RYRCNGLLAL
ILLVAILGIC AKLGIVSPLV VADRGLELLS ATFIFCVLVT LALYVTGRSS SNKGSSLKPH
VSGNLVHDWW FGIQLNPQFM SIDLKFFFVR AGMMGWLLIN LSILAKSVQD GSLSQSMILY
QIFCALYILD YFVHEEYMTS TWDIIAERLG FMLVFGDLLW IPFTFSIQGW WLLHNKVELT
VPAIVVNCLV FLIGYMVFRG ANKQKHIFKK NPKTPIWGKP PVVVGGKLLV SGYWGIARHC
NYLGDLMLAL SFSLPCGISS PVPYFYPIYL LILLIWRERR DEVRCAEKYK EIWAEYLRLV
PWRILPYVY
