SCE3_BRANA
ID SCE3_BRANA Reviewed; 389 AA.
AC Q3ZFI4;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Sinapine esterase {ECO:0000305};
DE Short=BnSCE3 {ECO:0000303|PubMed:16756759};
DE EC=3.1.1.49 {ECO:0000269|PubMed:18036206};
DE AltName: Full=Lipase 2 {ECO:0000303|PubMed:16756759};
DE Short=BnLIP2 {ECO:0000303|PubMed:16756759};
DE Flags: Precursor;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000312|EMBL:AAX58135.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16756759; DOI=10.5483/bmbrep.2006.39.3.297;
RA Ling H., Zhao J., Zuo K., Qiu C., Yao H., Qin J., Sun X., Tang K.;
RT "Isolation and expression analysis of a GDSL-like lipase gene from Brassica
RT napus L.";
RL J. Biochem. Mol. Biol. 39:297-303(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=18036206; DOI=10.1111/j.1365-313x.2007.03374.x;
RA Clauss K., Baumert A., Nimtz M., Milkowski C., Strack D.;
RT "Role of a GDSL lipase-like protein as sinapine esterase in Brassicaceae.";
RL Plant J. 53:802-813(2008).
RN [3]
RP FUNCTION, AND OVEREXPRESSION.
RX PubMed=21248075; DOI=10.1104/pp.110.169821;
RA Clauss K., von Roepenack-Lahaye E., Boettcher C., Roth M.R., Welti R.,
RA Erban A., Kopka J., Scheel D., Milkowski C., Strack D.;
RT "Overexpression of sinapine esterase BnSCE3 in oilseed rape seeds triggers
RT global changes in seed metabolism.";
RL Plant Physiol. 155:1127-1145(2011).
CC -!- FUNCTION: Sinapine esterase that catalyzes that hydrolysis of sinapine,
CC releasing choline and sinapate. Sinapine (O-sinapoylcholine) is the
CC predominant phenolic compound in a complex group of sinapate esters in
CC seeds of oilseed rape (B.napus). Sinapine has antinutritive activity
CC and prevents the use of seed protein for food and feed. Shows broad
CC substrate specificity towards various other choline esters, including
CC phosphatidylcholine. {ECO:0000269|PubMed:18036206,
CC ECO:0000269|PubMed:21248075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-sinapoylcholine = choline + E-sinapate + H(+);
CC Xref=Rhea:RHEA:10016, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16353, ChEBI:CHEBI:30023; EC=3.1.1.49;
CC Evidence={ECO:0000269|PubMed:18036206};
CC -!- ACTIVITY REGULATION: Inhibited by PMSF. {ECO:0000269|PubMed:18036206}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for sinapine {ECO:0000269|PubMed:18036206};
CC KM=11 uM for cinnamoylcholine {ECO:0000269|PubMed:18036206};
CC KM=101 uM for 3-phenylpropionylcholine {ECO:0000269|PubMed:18036206};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues or organs of the mature
CC seedlings. Not expressed in roots of mature seedlings.
CC {ECO:0000269|PubMed:16756759}.
CC -!- DEVELOPMENTAL STAGE: Expressed during reproductive growth and strongly
CC expressed during seed germination. Expression is not detected until 3
CC days after germination, and subsequently becomes stronger. Not present
CC in root of seedlings growing at different stages.
CC {ECO:0000269|PubMed:16756759}.
CC -!- MISCELLANEOUS: Overexpression in seeds induces a strong decrease of
CC sinapine levels together with an increase of choline. Seeds display
CC higher weight, size and water content and a fraction of seeds display
CC morphological alterations, characterized by large cavities near the
CC embryonic tissue. Seed quality parameters, such as fiber and
CC glucosinolate levels, and agronomically important traits, such as oil
CC and protein contents, differ only slightly, except that amounts of
CC hemicellulose and cellulose are higher. Seedlings are larger and young
CC seedlings exhibit longer hypocotyls. Metabolic profiles of transgenic
CC seeds indicate that, besides suppression of sinapine accumulation,
CC other differences in primary and secondary metabolism are observed.
CC {ECO:0000269|PubMed:21248075}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AY870270; AAX58135.1; -; mRNA.
DR RefSeq; NP_001302718.1; NM_001315789.1.
DR AlphaFoldDB; Q3ZFI4; -.
DR SMR; Q3ZFI4; -.
DR GeneID; 106358067; -.
DR KEGG; bna:106358067; -.
DR BRENDA; 3.1.1.49; 944.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050285; F:sinapine esterase activity; IDA:UniProtKB.
DR CDD; cd01837; SGNH_plant_lipase_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR035669; SGNH_plant_lipase-like.
DR Pfam; PF00657; Lipase_GDSL; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..389
FT /note="Sinapine esterase"
FT /id="PRO_0000430709"
FT ACT_SITE 41
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q00017"
FT ACT_SITE 345
FT /evidence="ECO:0000250|UniProtKB:Q00017"
FT ACT_SITE 348
FT /evidence="ECO:0000250|UniProtKB:Q00017"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 389 AA; 43319 MW; 8490F94765BAF6B6 CRC64;
MASSLKKLIT SFLLFFFYTI IVASSEPSCR RYKSIISFGD SIADTGNYLH LSDVNHPPQA
AFLPYGETFF SVPTGRDSDG RLIIDFIAEF LGLPYVPPYF GSQNVSFEQG VNFAVYGATA
LDRAFFIEKG IVSDFTNVSL SVQLNTFKQI LPTLCASSSR DCREMLGDSL ILMGESGGND
YNYPFFEDKS INEIKELTPL IIKAISDAIV DLIDLGGKTF LVPGSFPVGC SAAYLTLFQT
AKEKDYDPLT GCLPWLNDFG KHHDEQLKTE IRRLRKLYPH VNIMYADYYN SLYRLYQKPT
KYGFKNRPLA ACCGVGGQYN FTIGEECGYE GVGYCQNPSE YINWDGYHIT EAAHQKMAHG
ILNGPYATPA FNWSCLDAAS VDNESSFGS
