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Serine carboxypeptidase-like 8 (Protein SINAPOYLGLUCOSE ACCUMULATOR 1) (Sinapoylglucose--malate O-sinapoyltransferase) (SMT) (EC 2.3.1.92) (Sinapoylglucose--sinapoylglucose O-sinapoyltransferase) (EC 2.3.1.103)

 SCP8_ARATH              Reviewed;         433 AA.
Q8RUW5; O64809; Q3EBV9; Q9ASY4;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
30-AUG-2017, entry version 101.
RecName: Full=Serine carboxypeptidase-like 8;
AltName: Full=Protein SINAPOYLGLUCOSE ACCUMULATOR 1;
AltName: Full=Sinapoylglucose--malate O-sinapoyltransferase;
Short=SMT;
EC=2.3.1.92;
AltName: Full=Sinapoylglucose--sinapoylglucose O-sinapoyltransferase;
EC=2.3.1.103;
Flags: Precursor;
Name=SCPL8; Synonyms=SMT, SNG1; OrderedLocusNames=At2g22990;
ORFNames=F21P24.5, T20K9.18;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-36, FUNCTION,
DISRUPTION PHENOTYPE, ENZYME REGULATION, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia; TISSUE=Seedling;
PubMed=10948250; DOI=10.1105/tpc.12.8.1295;
Lehfeldt C., Shirley A.M., Meyer K., Ruegger M.O., Cusumano J.C.,
Viitanen P.V., Strack D., Chapple C.;
"Cloning of the SNG1 gene of Arabidopsis reveals a role for a serine
carboxypeptidase-like protein as an acyltransferase in secondary
metabolism.";
Plant Cell 12:1295-1306(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
PROTEIN SEQUENCE OF 20-25, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
AND GLYCOSYLATION.
PubMed=12012238; DOI=10.1007/s00425-001-0716-y;
Hause B., Meyer K., Viitanen P.V., Chapple C., Strack D.;
"Immunolocalization of 1- O-sinapoylglucose:malate sinapoyltransferase
in Arabidopsis thaliana.";
Planta 215:26-32(2002).
[6]
GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
PubMed=15908604; DOI=10.1104/pp.104.057950;
Fraser C.M., Rider L.W., Chapple C.;
"An expression and bioinformatics analysis of the Arabidopsis serine
carboxypeptidase-like gene family.";
Plant Physiol. 138:1136-1148(2005).
[7]
FUNCTION, 3D-STRUCTURE MODELING, MUTAGENESIS OF ASN-73;
172-ASP--SER-175; SER-173; LYS-268; HIS-272; ARG-322; ASP-358 AND
HIS-411, AND ENZYME REGULATION.
PubMed=17094968; DOI=10.1016/j.febslet.2006.10.046;
Stehle F., Brandt W., Milkowski C., Strack D.;
"Structure determinants and substrate recognition of serine
carboxypeptidase-like acyltransferases from plant secondary
metabolism.";
FEBS Lett. 580:6366-6374(2006).
[8]
FUNCTION.
PubMed=17600138; DOI=10.1104/pp.107.098970;
Fraser C.M., Thompson M.G., Shirley A.M., Ralph J., Schoenherr J.A.,
Sinlapadech T., Hall M.C., Chapple C.;
"Related Arabidopsis serine carboxypeptidase-like sinapoylglucose
acyltransferases display distinct but overlapping substrate
specificities.";
Plant Physiol. 144:1986-1999(2007).
[9]
FUNCTION.
PubMed=19695650; DOI=10.1016/j.phytochem.2009.07.023;
Stehle F., Brandt W., Stubbs M.T., Milkowski C., Strack D.;
"Sinapoyltransferases in the light of molecular evolution.";
Phytochemistry 70:1652-1662(2009).
[10]
FUNCTION.
STRAIN=cv. Columbia, cv. Pna-10, and cv. Pna-17;
PubMed=19969522; DOI=10.1093/mp/ssp090;
Li X., Bergelson J., Chapple C.;
"The ARABIDOPSIS accession Pna-10 is a naturally occurring sng1
deletion mutant.";
Mol. Plant 3:91-100(2010).
-!- FUNCTION: Involved in plants secondary metabolism. Functions as
acyltransferase to form the sinapate ester sinapoylmalate. Also
capable of catalyzing the formation of 1,2-bis-O-sinapoyl beta-D-
glucoside. {ECO:0000269|PubMed:10948250,
ECO:0000269|PubMed:17094968, ECO:0000269|PubMed:17600138,
ECO:0000269|PubMed:19695650, ECO:0000269|PubMed:19969522}.
-!- CATALYTIC ACTIVITY: 1-O-sinapoyl-beta-D-glucose + (S)-malate = D-
glucose + sinapoyl-(S)-malate.
-!- CATALYTIC ACTIVITY: 2 1-O-sinapoyl beta-D-glucoside = D-glucose +
1,2-bis-O-sinapoyl beta-D-glucoside.
-!- ENZYME REGULATION: 95% inhibition by diisopropyl fluorophosphate
(DFP) and 30% by phenylmethylsulfonyl fluoride (PMSF).
{ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:17094968}.
-!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:12012238}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8RUW5-1; Sequence=Displayed;
Name=2;
IsoId=Q8RUW5-2; Sequence=VSP_027464;
Note=Derived from EST data. May be due to a competing donor
splice site. No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in seedlings. Expressed in
leaves, stems, flowers and siliques, and at low levels in roots.
{ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:12012238,
ECO:0000269|PubMed:15908604}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12012238}.
-!- DISRUPTION PHENOTYPE: Plants do not contain sinapoylmalate and
accumulate its biosynthetic precursor, sinapoylglucose.
{ECO:0000269|PubMed:10948250}.
-!- MISCELLANEOUS: In cv. Pna-10, this protein SCP8 and the adjacent
SCP10 are not present due to a natural 13-kb deletion
(PubMed:19969522). {ECO:0000305|PubMed:19969522}.
-!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
-!- CAUTION: Was classified as a serine carboxypeptidase-like (SCPL)
protein solely on the basis of the overall sequence similarity
(PubMed:15908604) but it has been shown that it belongs to a class
of enzymes that catalyze acyltransferase reactions
(PubMed:17600138). {ECO:0000305|PubMed:15908604,
ECO:0000305|PubMed:17600138}.
-!- SEQUENCE CAUTION:
Sequence=AAC17816.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAK32769.1; Type=Frameshift; Positions=260; Evidence={ECO:0000305};
Sequence=AAM15006.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAN28819.1; Type=Erroneous termination; Positions=260; Note=Translated as Glu.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF275313; AAF78760.1; -; mRNA.
EMBL; AC004401; AAC17816.2; ALT_SEQ; Genomic_DNA.
EMBL; AC004786; AAM15006.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002685; AEC07390.1; -; Genomic_DNA.
EMBL; CP002685; AEC07393.1; -; Genomic_DNA.
EMBL; AF361601; AAK32769.1; ALT_FRAME; mRNA.
EMBL; AY035052; AAK59557.1; -; mRNA.
EMBL; AY051060; AAK93737.1; -; mRNA.
EMBL; AY143880; AAN28819.1; ALT_SEQ; mRNA.
PIR; C84619; C84619.
RefSeq; NP_850034.1; NM_179703.2. [Q8RUW5-1]
RefSeq; NP_850035.1; NM_179704.1. [Q8RUW5-2]
UniGene; At.24365; -.
PDB; 2DRF; Model; -; B=20-433.
PDBsum; 2DRF; -.
ProteinModelPortal; Q8RUW5; -.
SMR; Q8RUW5; -.
STRING; 3702.AT2G22990.3; -.
ESTHER; arath-SCP8; Carboxypeptidase_S10.
MEROPS; S10.A14; -.
PaxDb; Q8RUW5; -.
EnsemblPlants; AT2G22990.1; AT2G22990.1; AT2G22990. [Q8RUW5-1]
EnsemblPlants; AT2G22990.3; AT2G22990.3; AT2G22990. [Q8RUW5-2]
GeneID; 816830; -.
Gramene; AT2G22990.1; AT2G22990.1; AT2G22990.
Gramene; AT2G22990.3; AT2G22990.3; AT2G22990.
KEGG; ath:AT2G22990; -.
Araport; AT2G22990; -.
TAIR; locus:2045374; AT2G22990.
eggNOG; KOG1282; Eukaryota.
eggNOG; COG2939; LUCA.
HOGENOM; HOG000198297; -.
InParanoid; Q8RUW5; -.
KO; K09757; -.
OMA; HCANSLQ; -.
PhylomeDB; Q8RUW5; -.
BioCyc; ARA:AT2G22990-MONOMER; -.
BRENDA; 2.3.1.92; 399.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q8RUW5; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q8RUW5; baseline and differential.
Genevisible; Q8RUW5; AT.
GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
GO; GO:0016754; F:sinapoylglucose-malate O-sinapoyltransferase activity; IDA:TAIR.
GO; GO:0047158; F:sinapoylglucose-sinapoylglucose O-sinapoyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0009698; P:phenylpropanoid metabolic process; IDA:TAIR.
GO; GO:0006508; P:proteolysis; IEA:InterPro.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR001563; Peptidase_S10.
PANTHER; PTHR11802; PTHR11802; 1.
Pfam; PF00450; Peptidase_S10; 1.
PRINTS; PR00724; CRBOXYPTASEC.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Alternative splicing;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Reference proteome; Signal; Transferase; Vacuole.
SIGNAL 1 19 {ECO:0000269|PubMed:10948250,
ECO:0000269|PubMed:12012238}.
CHAIN 20 433 Serine carboxypeptidase-like 8.
/FTId=PRO_0000274622.
ACT_SITE 173 173 {ECO:0000250}.
ACT_SITE 358 358 {ECO:0000250}.
ACT_SITE 411 411 {ECO:0000250}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 342 342 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 418 418 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 78 323 {ECO:0000250}.
DISULFID 241 255 {ECO:0000250}.
DISULFID 279 289 {ECO:0000250}.
VAR_SEQ 408 433 GGGHTAEYRPNETFIMFQRWISGQPL -> ASVDTRQSIDQ
TRPLSCSKGGSVANPCNKRLMTFTYNYLPTNIHVKRSCLC
(in isoform 2). {ECO:0000305}.
/FTId=VSP_027464.
MUTAGEN 73 73 N->A: 87% reduction of activity.
{ECO:0000269|PubMed:17094968}.
MUTAGEN 172 175 DSYS->ESYA: 85% reduction of activity.
{ECO:0000269|PubMed:17094968}.
MUTAGEN 173 173 S->A: Total loss of activity.
{ECO:0000269|PubMed:17094968}.
MUTAGEN 268 268 K->E: 25% reduction of activity.
{ECO:0000269|PubMed:17094968}.
MUTAGEN 272 272 H->D: 78% reduction of activity.
{ECO:0000269|PubMed:17094968}.
MUTAGEN 322 322 R->E: 99% reduction of activity.
{ECO:0000269|PubMed:17094968}.
MUTAGEN 358 358 D->A: 80% reduction of activity.
{ECO:0000269|PubMed:17094968}.
MUTAGEN 411 411 H->A: Total loss of activity.
{ECO:0000269|PubMed:17094968}.
SEQUENCE 433 AA; 49439 MW; 67234085A5FBAF0C CRC64;
MSLKIKFLLL LVLYHHVDSA SIVKFLPGFE GPLPFELETG YIGIGEDENV QFFYYFIKSE
NNPKEDPLLI WLNGGPGCSC LGGIIFENGP VGLKFEVFNG SAPSLFSTTY SWTKMANIIF
LDQPVGSGFS YSKTPIDKTG DISEVKRTHE FLQKWLSRHP QYFSNPLYVV GDSYSGMIVP
ALVQEISQGN YICCEPPINL QGYMLGNPVT YMDFEQNFRI PYAYGMGLIS DEIYEPMKRI
CNGNYYNVDP SNTQCLKLTE EYHKCTAKIN IHHILTPDCD VTNVTSPDCY YYPYHLIECW
ANDESVREAL HIEKGSKGKW ARCNRTIPYN HDIVSSIPYH MNNSISGYRS LIYSGDHDIA
VPFLATQAWI RSLNYSPIHN WRPWMINNQI AGYTRAYSNK MTFATIKGGG HTAEYRPNET
FIMFQRWISG QPL


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