SCP8_ARATH
ID SCP8_ARATH Reviewed; 433 AA.
AC Q8RUW5; O64809; Q3EBV9; Q9ASY4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Serine carboxypeptidase-like 8 {ECO:0000303|PubMed:15908604};
DE AltName: Full=Protein SINAPOYLGLUCOSE ACCUMULATOR 1 {ECO:0000303|PubMed:10948250};
DE AltName: Full=Sinapoylglucose--malate O-sinapoyltransferase {ECO:0000303|PubMed:12012238, ECO:0000303|PubMed:17094968};
DE Short=SMT {ECO:0000303|PubMed:12012238};
DE EC=2.3.1.92 {ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:17600138};
DE AltName: Full=Sinapoylglucose--sinapoylglucose O-sinapoyltransferase {ECO:0000303|PubMed:17094968};
DE EC=2.3.1.103 {ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:17600138};
DE Flags: Precursor;
GN Name=SCPL8 {ECO:0000303|PubMed:15908604};
GN Synonyms=SMT {ECO:0000303|PubMed:12012238},
GN SNG1 {ECO:0000303|PubMed:10948250};
GN OrderedLocusNames=At2g22990 {ECO:0000312|Araport:AT2G22990};
GN ORFNames=F21P24.5 {ECO:0000312|EMBL:AAC17816.2},
GN T20K9.18 {ECO:0000312|EMBL:AAM15006.1};
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], PROTEIN SEQUENCE OF 20-36, FUNCTION, DISRUPTION
RP PHENOTYPE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=10948250; DOI=10.2307/3871130;
RA Lehfeldt C., Shirley A.M., Meyer K., Ruegger M.O., Cusumano J.C.,
RA Viitanen P.V., Strack D., Chapple C.;
RT "Cloning of the SNG1 gene of Arabidopsis reveals a role for a serine
RT carboxypeptidase-like protein as an acyltransferase in secondary
RT metabolism.";
RL Plant Cell 12:1295-1306(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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).
RN [5]
RP PROTEIN SEQUENCE OF 20-25, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RX PubMed=12012238; DOI=10.1007/s00425-001-0716-y;
RA Hause B., Meyer K., Viitanen P.V., Chapple C., Strack D.;
RT "Immunolocalization of 1- O-sinapoylglucose:malate sinapoyltransferase in
RT Arabidopsis thaliana.";
RL Planta 215:26-32(2002).
RN [6]
RP GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=15908604; DOI=10.1104/pp.104.057950;
RA Fraser C.M., Rider L.W., Chapple C.;
RT "An expression and bioinformatics analysis of the Arabidopsis serine
RT carboxypeptidase-like gene family.";
RL Plant Physiol. 138:1136-1148(2005).
RN [7]
RP FUNCTION, 3D-STRUCTURE MODELING, MUTAGENESIS OF ASN-73; 172-ASP--SER-175;
RP SER-173; LYS-268; HIS-272; ARG-322; ASP-358 AND HIS-411, AND ACTIVITY
RP REGULATION.
RX PubMed=17094968; DOI=10.1016/j.febslet.2006.10.046;
RA Stehle F., Brandt W., Milkowski C., Strack D.;
RT "Structure determinants and substrate recognition of serine
RT carboxypeptidase-like acyltransferases from plant secondary metabolism.";
RL FEBS Lett. 580:6366-6374(2006).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=17600138; DOI=10.1104/pp.107.098970;
RA Fraser C.M., Thompson M.G., Shirley A.M., Ralph J., Schoenherr J.A.,
RA Sinlapadech T., Hall M.C., Chapple C.;
RT "Related Arabidopsis serine carboxypeptidase-like sinapoylglucose
RT acyltransferases display distinct but overlapping substrate
RT specificities.";
RL Plant Physiol. 144:1986-1999(2007).
RN [9]
RP FUNCTION.
RX PubMed=19695650; DOI=10.1016/j.phytochem.2009.07.023;
RA Stehle F., Brandt W., Stubbs M.T., Milkowski C., Strack D.;
RT "Sinapoyltransferases in the light of molecular evolution.";
RL Phytochemistry 70:1652-1662(2009).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia, cv. Pna-10, and cv. Pna-17;
RX PubMed=19969522; DOI=10.1093/mp/ssp090;
RA Li X., Bergelson J., Chapple C.;
RT "The ARABIDOPSIS accession Pna-10 is a naturally occurring sng1 deletion
RT mutant.";
RL Mol. Plant 3:91-100(2010).
CC -!- FUNCTION: Involved in plants secondary metabolism. Functions as
CC acyltransferase to form the sinapate ester sinapoylmalate. Also capable
CC of catalyzing the formation of 1,2-bis-O-sinapoyl beta-D-glucoside.
CC {ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:17094968,
CC ECO:0000269|PubMed:17600138, ECO:0000269|PubMed:19695650,
CC ECO:0000269|PubMed:19969522}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + 1-O-(trans-sinapoyl)-beta-D-glucose = D-glucose +
CC sinapoyl (S)-malate; Xref=Rhea:RHEA:12625, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15589, ChEBI:CHEBI:16546, ChEBI:CHEBI:57426; EC=2.3.1.92;
CC Evidence={ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:17600138,
CC ECO:0000269|PubMed:19969522};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12626;
CC Evidence={ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:17600138,
CC ECO:0000269|PubMed:19969522};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1-O-(trans-sinapoyl)-beta-D-glucose = 1,2-di-O-sinapoyl
CC beta-D-glucose + D-glucose; Xref=Rhea:RHEA:22664, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:16546, ChEBI:CHEBI:27993; EC=2.3.1.103;
CC Evidence={ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:17600138,
CC ECO:0000269|PubMed:19969522};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22665;
CC Evidence={ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:17600138,
CC ECO:0000269|PubMed:19969522};
CC -!- ACTIVITY REGULATION: 95% inhibition by diisopropyl fluorophosphate
CC (DFP) and 30% by phenylmethylsulfonyl fluoride (PMSF).
CC {ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:17094968}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:12012238}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RUW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RUW5-2; Sequence=VSP_027464;
CC -!- TISSUE SPECIFICITY: Highly expressed in seedlings. Expressed in leaves,
CC stems, flowers and siliques, and at low levels in roots.
CC {ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:12012238,
CC ECO:0000269|PubMed:15908604}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12012238}.
CC -!- DISRUPTION PHENOTYPE: Plants do not contain sinapoylmalate and
CC accumulate its biosynthetic precursor, sinapoylglucose.
CC {ECO:0000269|PubMed:10948250, ECO:0000269|PubMed:17600138,
CC ECO:0000269|PubMed:19969522}.
CC -!- MISCELLANEOUS: In cv. Pna-10, this protein SCP8 and the adjacent SCP10
CC are not present due to a natural 13-kb deletion (PubMed:19969522).
CC {ECO:0000305|PubMed:19969522}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- CAUTION: Was classified as a serine carboxypeptidase-like (SCPL)
CC protein solely on the basis of the overall sequence similarity
CC (PubMed:15908604) but it has been shown that it belongs to a class of
CC enzymes that catalyze acyltransferase reactions (PubMed:17600138).
CC {ECO:0000305|PubMed:15908604, ECO:0000305|PubMed:17600138}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17816.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK32769.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM15006.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAN28819.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF275313; AAF78760.1; -; mRNA.
DR EMBL; AC004401; AAC17816.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004786; AAM15006.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07390.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07393.1; -; Genomic_DNA.
DR EMBL; AF361601; AAK32769.1; ALT_FRAME; mRNA.
DR EMBL; AY035052; AAK59557.1; -; mRNA.
DR EMBL; AY051060; AAK93737.1; -; mRNA.
DR EMBL; AY143880; AAN28819.1; ALT_SEQ; mRNA.
DR PIR; C84619; C84619.
DR RefSeq; NP_850034.1; NM_179703.2. [Q8RUW5-1]
DR RefSeq; NP_850035.1; NM_179704.1. [Q8RUW5-2]
DR AlphaFoldDB; Q8RUW5; -.
DR SMR; Q8RUW5; -.
DR STRING; 3702.AT2G22990.3; -.
DR ESTHER; arath-SCP8; Carboxypeptidase_S10.
DR MEROPS; S10.A14; -.
DR PaxDb; Q8RUW5; -.
DR EnsemblPlants; AT2G22990.1; AT2G22990.1; AT2G22990. [Q8RUW5-1]
DR EnsemblPlants; AT2G22990.3; AT2G22990.3; AT2G22990. [Q8RUW5-2]
DR GeneID; 816830; -.
DR Gramene; AT2G22990.1; AT2G22990.1; AT2G22990. [Q8RUW5-1]
DR Gramene; AT2G22990.3; AT2G22990.3; AT2G22990. [Q8RUW5-2]
DR KEGG; ath:AT2G22990; -.
DR Araport; AT2G22990; -.
DR TAIR; locus:2045374; AT2G22990.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q8RUW5; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q8RUW5; -.
DR BioCyc; ARA:AT2G22990-MON; -.
DR BRENDA; 2.3.1.92; 399.
DR PRO; PR:Q8RUW5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RUW5; baseline and differential.
DR Genevisible; Q8RUW5; AT.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0016754; F:sinapoylglucose-malate O-sinapoyltransferase activity; IDA:TAIR.
DR GO; GO:0047158; F:sinapoylglucose-sinapoylglucose O-sinapoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IDA:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0019748; P:secondary metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Reference proteome; Signal; Transferase;
KW Vacuole.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:10948250,
FT ECO:0000269|PubMed:12012238"
FT CHAIN 20..433
FT /note="Serine carboxypeptidase-like 8"
FT /id="PRO_0000274622"
FT ACT_SITE 173
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT ACT_SITE 358
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT ACT_SITE 411
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 78..323
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT DISULFID 241..255
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT DISULFID 279..289
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT VAR_SEQ 408..433
FT /note="GGGHTAEYRPNETFIMFQRWISGQPL -> ASVDTRQSIDQTRPLSCSKGGS
FT VANPCNKRLMTFTYNYLPTNIHVKRSCLC (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_027464"
FT MUTAGEN 73
FT /note="N->A: 87% reduction of activity."
FT /evidence="ECO:0000269|PubMed:17094968"
FT MUTAGEN 172..175
FT /note="DSYS->ESYA: 85% reduction of activity."
FT /evidence="ECO:0000269|PubMed:17094968"
FT MUTAGEN 173
FT /note="S->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:17094968"
FT MUTAGEN 268
FT /note="K->E: 25% reduction of activity."
FT /evidence="ECO:0000269|PubMed:17094968"
FT MUTAGEN 272
FT /note="H->D: 78% reduction of activity."
FT /evidence="ECO:0000269|PubMed:17094968"
FT MUTAGEN 322
FT /note="R->E: 99% reduction of activity."
FT /evidence="ECO:0000269|PubMed:17094968"
FT MUTAGEN 358
FT /note="D->A: 80% reduction of activity."
FT /evidence="ECO:0000269|PubMed:17094968"
FT MUTAGEN 411
FT /note="H->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:17094968"
SQ 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
