ID   DIM_PEA                 Reviewed;         567 AA.
AC   P93472; Q9ATR0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Delta(24)-sterol reductase;
DE            EC=1.3.1.72;
DE   AltName: Full=Cell elongation protein diminuto;
GN   Name=DIM; Synonyms=LKB;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Alaska;
RA   Shimizu S., Mori H.;
RT   "A cDNA from Pisum sativum encoding the DIMINUTO homologue.";
RL   (er) Plant Gene Register PGR96-079(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND MUTAGENESIS OF ARG-24.
RC   STRAIN=cv. Torsdag;
RX   PubMed=11669574; DOI=10.1023/a:1011894812794;
RA   Schultz L., Kerckhoffs L.H., Klahre U., Yokota T., Reid J.B.;
RT   "Molecular characterization of the brassinosteroid-deficient lkb mutant in
RT   pea.";
RL   Plant Mol. Biol. 47:491-498(2001).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Torsdag;
RX   PubMed=10198111; DOI=10.1104/pp.119.4.1517;
RA   Nomura T., Kitasaka Y., Takatsuto S., Reid J.B., Fukami M., Yokota T.;
RT   "Brassinosteroid/Sterol synthesis and plant growth as affected by lka and
RT   lkb mutations of Pea.";
RL   Plant Physiol. 119:1517-1526(1999).
CC   -!- FUNCTION: Plays a critical role in the general process of plant cell
CC       elongation. {ECO:0000269|PubMed:10198111, ECO:0000269|PubMed:11669574}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lathosterol + NADP(+) = 5alpha-cholesta-7,24-dien-3beta-ol +
CC         H(+) + NADPH; Xref=Rhea:RHEA:13685, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16290, ChEBI:CHEBI:17168, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.3.1.72;
CC         Evidence={ECO:0000269|PubMed:10198111};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the apical region and root tips
CC       and lower levels in immature and mature internodes and leaves.
CC       {ECO:0000269|Ref.1}.
CC   -!- INDUCTION: Not induced by brassinolide. {ECO:0000269|PubMed:11669574}.
CC   -!- SIMILARITY: Belongs to the DIMINUTO family. {ECO:0000305}.
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DR   EMBL; D86494; BAA13096.1; -; mRNA.
DR   EMBL; AF325121; AAK15493.1; -; mRNA.
DR   PIR; T06575; T06575.
DR   AlphaFoldDB; P93472; -.
DR   SMR; P93472; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050614; F:delta24-sterol reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR040165; Diminuto-like.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR10801; PTHR10801; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Membrane; NADP; Oxidoreductase; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..567
FT                   /note="Delta(24)-sterol reductase"
FT                   /id="PRO_0000219496"
FT   TOPO_DOM        1..24
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..567
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          45..231
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   REGION          520..541
FT                   /note="Interaction with calmodulin"
FT                   /evidence="ECO:0000250"
FT   REGION          548..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         360
FT                   /note="S -> W (in strain: cv. Torsdag)"
FT   VARIANT         411
FT                   /note="S -> V (in strain: cv. Torsdag)"
FT   VARIANT         417
FT                   /note="I -> V (in strain: cv. Torsdag)"
FT   VARIANT         560
FT                   /note="P -> A (in strain: cv. Torsdag)"
FT   VARIANT         566
FT                   /note="P -> A (in strain: cv. Torsdag)"
FT   MUTAGEN         24
FT                   /note="R->K: In lkb; decreased activity."
FT                   /evidence="ECO:0000269|PubMed:11669574"
SQ   SEQUENCE   567 AA;  65975 MW;  7316A313ED88EF86 CRC64;
     MSDLEAPLRP KRKKIWVDYF VKFRWILVIF VVLPISFTLY FLTYLGDVRS EWKSFKTRQK
     EHDENVQKVV NRLKKRNPSK DGLVCTARKP WVAVGMRNVD YKRARHFEVD LSPFRNILDI
     DKERMIARVE PLVNMGQITR VTVPMNLALA VVAELDDLTV GGLINGYGIE GSSHKYGLFS
     DTVVAFEIIL ADGSLVKATK DNEYSDLFYA IPWSQGTLGL LVAAEVKLIP IKEYMKLTYK
     PVVGNLKDIA QAYSDSFAPR DGDQDNDEKV PDFVETMIYS PTRAVCMTGR YASKEEAKKK
     GNKINNVGWW YKTWFYQHAE TALKKGLFVE YIPTREYYHR HTRCLYWEGK LILPFGDQFS
     FRFLFGWLMP PKVSLLKATQ GEAIRNYYHE MHVIQDMLVP LYKVGDALEW SDREMEIYPI
     WLCPHKLFKL PIKTMIYPEA GFELQRRQGD TQNAQMFTDV GVYYAPGPVL RGEVFDGAEA
     VRKMESWMIE NHCFQPQYAV SELNEKNFWR MFDAGLYEHC RRKYGAVGTF MSVYYKCKKG
     RKTEKEVREA EQAHLDTAYP EVDQPPD