ID   ST7R_ARATH              Reviewed;         432 AA.
AC   Q9LDU6; Q38930;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=7-dehydrocholesterol reductase;
DE            Short=7-DHC reductase;
DE            EC=1.3.1.21;
DE   AltName: Full=Protein DWARF 5;
DE   AltName: Full=Sterol Delta(7)-reductase;
GN   Name=DWF5; Synonyms=ST7R; OrderedLocusNames=At1g50430;
GN   ORFNames=F11F12.21;
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], AND CHARACTERIZATION.
RC   TISSUE=Seedling;
RX   PubMed=8631902; DOI=10.1074/jbc.271.18.10866;
RA   Lecain E., Chenivesse X., Spagnoli R., Pompon D.;
RT   "Cloning by metabolic interference in yeast and enzymatic characterization
RT   of Arabidopsis thaliana sterol delta 7-reductase.";
RL   J. Biol. Chem. 271:10866-10873(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE, AND MUTAGENESIS OF ASP-257.
RC   STRAIN=cv. Wassilewskija-2;
RX   PubMed=10758495; DOI=10.1046/j.1365-313x.2000.00693.x;
RA   Choe S., Tanaka A., Noguchi T., Fujioka S., Takatsuto S., Ross A.S.,
RA   Tax F.E., Yoshida S., Feldmann K.A.;
RT   "Lesions in the sterol delta reductase gene of Arabidopsis cause dwarfism
RT   due to a block in brassinosteroid biosynthesis.";
RL   Plant J. 21:431-443(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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: Production of cholesterol by reduction of C7-C8 double bond
CC       of 7-dehydrocholesterol (7-DHC). Lesions in the gene coding for the
CC       enzyme cause dwarfism.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH;
CC         Xref=Rhea:RHEA:23984, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113,
CC         ChEBI:CHEBI:17759, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.21;
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- INTERACTION:
CC       Q9LDU6; Q8VZW1: NIP1-1; NbExp=2; IntAct=EBI-4439540, EBI-4424378;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
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=Q9LDU6-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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DR   EMBL; U49398; AAC49278.1; -; mRNA.
DR   EMBL; AF239701; AAF63498.1; -; Genomic_DNA.
DR   EMBL; AC012561; AAF87888.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32547.1; -; Genomic_DNA.
DR   EMBL; AY099589; AAM20440.1; -; mRNA.
DR   EMBL; BT000245; AAN15564.1; -; mRNA.
DR   PIR; F96540; F96540.
DR   RefSeq; NP_175460.1; NM_103926.5. [Q9LDU6-1]
DR   AlphaFoldDB; Q9LDU6; -.
DR   SMR; Q9LDU6; -.
DR   BioGRID; 26690; 6.
DR   IntAct; Q9LDU6; 5.
DR   STRING; 3702.Q9LDU6; -.
DR   iPTMnet; Q9LDU6; -.
DR   SwissPalm; Q9LDU6; -.
DR   PaxDb; 3702-AT1G50430-1; -.
DR   ProteomicsDB; 228341; -. [Q9LDU6-1]
DR   EnsemblPlants; AT1G50430.1; AT1G50430.1; AT1G50430. [Q9LDU6-1]
DR   GeneID; 841465; -.
DR   Gramene; AT1G50430.1; AT1G50430.1; AT1G50430. [Q9LDU6-1]
DR   KEGG; ath:AT1G50430; -.
DR   Araport; AT1G50430; -.
DR   TAIR; AT1G50430; DWF5.
DR   eggNOG; KOG1435; Eukaryota.
DR   InParanoid; Q9LDU6; -.
DR   OrthoDB; 275939at2759; -.
DR   PhylomeDB; Q9LDU6; -.
DR   BioCyc; ARA:AT1G50430-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G50430-MONOMER; -.
DR   BRENDA; 1.3.1.21; 399.
DR   UniPathway; UPA00062; -.
DR   PRO; PR:Q9LDU6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LDU6; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009918; F:sterol delta7 reductase activity; IMP:TAIR.
DR   GO; GO:0016132; P:brassinosteroid biosynthetic process; IMP:TAIR.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009826; P:unidimensional cell growth; TAS:TAIR.
DR   Gene3D; 1.20.120.1630; -; 1.
DR   InterPro; IPR001171; ERG24_DHCR-like.
DR   InterPro; IPR018083; Sterol_reductase_CS.
DR   PANTHER; PTHR21257:SF38; 7-DEHYDROCHOLESTEROL REDUCTASE; 1.
DR   PANTHER; PTHR21257; DELTA(14)-STEROL REDUCTASE; 1.
DR   Pfam; PF01222; ERG4_ERG24; 1.
DR   PROSITE; PS01017; STEROL_REDUCT_1; 1.
DR   PROSITE; PS01018; STEROL_REDUCT_2; 1.
DR   Genevisible; Q9LDU6; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cholesterol biosynthesis; Cholesterol metabolism;
KW   Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   NADP; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..432
FT                   /note="7-dehydrocholesterol reductase"
FT                   /id="PRO_0000207509"
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         257
FT                   /note="D->N: In DWF5-4; dwarf plant."
FT                   /evidence="ECO:0000269|PubMed:10758495"
FT   CONFLICT        117
FT                   /note="Y -> H (in Ref. 1; AAC49278)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="N -> K (in Ref. 1; AAC49278)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        391..392
FT                   /note="Missing (in Ref. 1; AAC49278)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   432 AA;  49591 MW;  5458E495BE1EF4B0 CRC64;
     MAETVHSPIV TYASMLSLLA FCPPFVILLW YTMVHQDGSV TQTFGFFWEN GVQGLINIWP
     RPTLIAWKII FCYGAFEAIL QLLLPGKRVE GPISPAGNRP VYKANGLAAY FVTLATYLGL
     WWFGIFNPAI VYDHLGEIFS ALIFGSFIFC VLLYIKGHVA PSSSDSGSCG NLIIDFYWGM
     ELYPRIGKSF DIKVFTNCRF GMMSWAVLAV TYCIKQYEIN GKVSDSMLVN TILMLVYVTK
     FFWWEAGYWN TMDIAHDRAG FYICWGCLVW VPSVYTSPGM YLVNHPVELG TQLAIYILVA
     GILCIYINYD CDRQRQEFRR TNGKCLVWGR APSKIVASYT TTSGETKTSL LLTSGWWGLA
     RHFHYVPEIL SAFFWTVPAL FDNFLAYFYV IFLTLLLFDR AKRDDDRCRS KYGKYWKLYC
     EKVKYRIIPG IY
//