ST7R_ARATH
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 03-AUG-2022, entry version 149.
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; 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.AT1G50430.1; -.
DR iPTMnet; Q9LDU6; -.
DR SwissPalm; Q9LDU6; -.
DR PaxDb; Q9LDU6; -.
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; locus:2008071; AT1G50430.
DR eggNOG; KOG1435; Eukaryota.
DR InParanoid; Q9LDU6; -.
DR PhylomeDB; Q9LDU6; -.
DR BioCyc; ARA:AT1G50430-MON; -.
DR BioCyc; MetaCyc:AT1G50430-MON; -.
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 Genevisible; Q9LDU6; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
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:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; TAS:TAIR.
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; 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
