SCP19_ARATH
ID SCP19_ARATH Reviewed; 465 AA.
AC Q8VZU3; Q941P1; Q9FXX7; Q9LXC8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine carboxypeptidase-like 19 {ECO:0000303|PubMed:15908604};
DE AltName: Full=Protein SINAPOYLGLUCOSE ACCUMULATOR 2 {ECO:0000303|PubMed:11696189};
DE AltName: Full=Sinapoylglucose--choline O-sinapoyltransferase {ECO:0000303|PubMed:12657648};
DE Short=SCT {ECO:0000303|PubMed:12657648};
DE EC=2.3.1.91 {ECO:0000269|PubMed:12657648};
DE Contains:
DE RecName: Full=Serine carboxypeptidase-like 19 chain A;
DE Contains:
DE RecName: Full=Serine carboxypeptidase-like 19 chain B;
DE Flags: Precursor;
GN Name=SCPL19 {ECO:0000303|PubMed:15908604};
GN Synonyms=SCT {ECO:0000303|PubMed:12657648},
GN SNG2 {ECO:0000303|PubMed:11696189};
GN OrderedLocusNames=At5g09640 {ECO:0000312|Araport:AT5G09640};
GN ORFNames=F17I14.170 {ECO:0000312|EMBL:CAB89366.1},
GN MTH16.5 {ECO:0000312|EMBL:BAB09519.1};
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], FUNCTION, DISRUPTION PHENOTYPE, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11696189; DOI=10.1046/j.1365-313x.2001.01123.x;
RA Shirley A.M., McMichael C.M., Chapple C.;
RT "The sng2 mutant of Arabidopsis is defective in the gene encoding the
RT serine carboxypeptidase-like protein sinapoylglucose:choline
RT sinapoyltransferase.";
RL Plant J. 28:83-94(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND
RP GLYCOSYLATION.
RX PubMed=12657648; DOI=10.1074/jbc.m302362200;
RA Shirley A.M., Chapple C.;
RT "Biochemical characterization of sinapoylglucose:choline
RT sinapoyltransferase, a serine carboxypeptidase-like protein that functions
RT as an acyltransferase in plant secondary metabolism.";
RL J. Biol. Chem. 278:19870-19877(2003).
RN [7]
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 [8]
RP FUNCTION, AND 3D-STRUCTURE MODELING.
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 [9]
RP FUNCTION.
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 [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18515127; DOI=10.1016/j.plaphy.2008.04.014;
RA Huang J., Rozwadowski K., Bhinu V.S., Schafer U., Hannoufa A.;
RT "Manipulation of sinapine, choline and betaine accumulation in Arabidopsis
RT seed: towards improving the nutritional value of the meal and enhancing the
RT seedling performance under environmental stresses in oilseed crops.";
RL Plant Physiol. Biochem. 46:647-654(2008).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22762247; DOI=10.1111/j.1365-313x.2012.05096.x;
RA Lee S., Kaminaga Y., Cooper B., Pichersky E., Dudareva N., Chapple C.;
RT "Benzoylation and sinapoylation of glucosinolate R-groups in Arabidopsis.";
RL Plant J. 72:411-422(2012).
CC -!- FUNCTION: Involved in plants secondary metabolism. Functions as
CC acyltransferase to form the sinapate ester sinapoylcholine also known
CC as sinapine. Able to convert in vitro benzoylglucose into
CC benzoylcholine. {ECO:0000269|PubMed:11696189,
CC ECO:0000269|PubMed:12657648, ECO:0000269|PubMed:17094968,
CC ECO:0000269|PubMed:17600138, ECO:0000269|PubMed:18515127,
CC ECO:0000269|PubMed:22762247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(trans-sinapoyl)-beta-D-glucose + choline = D-glucose + O-
CC sinapoylcholine; Xref=Rhea:RHEA:12024, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:16353, ChEBI:CHEBI:16546; EC=2.3.1.91;
CC Evidence={ECO:0000269|PubMed:12657648};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12025;
CC Evidence={ECO:0000269|PubMed:12657648};
CC -!- ACTIVITY REGULATION: Slightly inhibited by phenylmethylsulfonyl
CC fluoride (PMSF). {ECO:0000269|PubMed:11696189}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 mM for sinapoylglucose {ECO:0000269|PubMed:12657648};
CC KM=0.41 mM for feruloylglucose {ECO:0000269|PubMed:12657648};
CC KM=0.1 mM for caffeoylglucose {ECO:0000269|PubMed:12657648};
CC KM=1.9 mM for p-coumaroylglucose {ECO:0000269|PubMed:12657648};
CC KM=3.2 mM for choline {ECO:0000269|PubMed:12657648};
CC KM=19 mM for N,N-dimethylethanolamine {ECO:0000269|PubMed:12657648};
CC KM=245 mM for 2-methylaminoethanol {ECO:0000269|PubMed:12657648};
CC KM=25 mM for neopentyl alcohol {ECO:0000269|PubMed:12657648};
CC KM=105 mM for Tris {ECO:0000269|PubMed:12657648};
CC Vmax=2.8 nmol/sec/mg enzyme with sinapoylglucose as substrate
CC {ECO:0000269|PubMed:12657648};
CC Vmax=1.8 nmol/sec/mg enzyme with feruloylglucose as substrate
CC {ECO:0000269|PubMed:12657648};
CC Vmax=0.75 nmol/sec/mg enzyme with caffeoylglucose as substrate
CC {ECO:0000269|PubMed:12657648};
CC Vmax=3.3 nmol/sec/mg enzyme with p-coumaroylglucose as substrate
CC {ECO:0000269|PubMed:12657648};
CC Vmax=2.5 nmol/sec/mg enzyme with choline as substrate
CC {ECO:0000269|PubMed:12657648};
CC Vmax=1.7 nmol/sec/mg enzyme with N,N-dimethylethanolamine as
CC substrate {ECO:0000269|PubMed:12657648};
CC Vmax=1.2 nmol/sec/mg enzyme with 2-methylaminoethanol as substrate
CC {ECO:0000269|PubMed:12657648};
CC Vmax=0.45 nmol/sec/mg enzyme with neopentyl alcohol as substrate
CC {ECO:0000269|PubMed:12657648};
CC Vmax=0.32 nmol/sec/mg enzyme with Tris as substrate
CC {ECO:0000269|PubMed:12657648};
CC Note=Measured in vitro at pH 7.0 and 30 degrees Celsius.;
CC -!- SUBUNIT: Heterodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers, and at lower levels
CC in young leaves and seedlings. Expressed in mature seeds and detected
CC in expanding siliques. {ECO:0000269|PubMed:11696189,
CC ECO:0000269|PubMed:15908604, ECO:0000269|PubMed:18515127}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12657648}.
CC -!- DISRUPTION PHENOTYPE: Plants accumulate sinapoylglucose and contain low
CC levels of sinapoylcholine and increased levels of choline. Decreased
CC levels of both benzoylated and sinapoylated glucosinolates.
CC {ECO:0000269|PubMed:11696189, ECO:0000269|PubMed:18515127,
CC ECO:0000269|PubMed:22762247}.
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=BAB09519.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB89366.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY033947; AAK52316.1; -; mRNA.
DR EMBL; AB020752; BAB09519.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL353994; CAB89366.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91420.1; -; Genomic_DNA.
DR EMBL; AY063833; AAL36189.1; -; mRNA.
DR EMBL; AY091309; AAM14248.1; -; mRNA.
DR PIR; T49934; T49934.
DR RefSeq; NP_568215.2; NM_121001.2.
DR AlphaFoldDB; Q8VZU3; -.
DR SMR; Q8VZU3; -.
DR STRING; 3702.AT5G09640.1; -.
DR ESTHER; arath-SCP19; Carboxypeptidase_S10.
DR MEROPS; S10.A18; -.
DR PaxDb; Q8VZU3; -.
DR PRIDE; Q8VZU3; -.
DR ProteomicsDB; 232741; -.
DR EnsemblPlants; AT5G09640.1; AT5G09640.1; AT5G09640.
DR GeneID; 830823; -.
DR Gramene; AT5G09640.1; AT5G09640.1; AT5G09640.
DR KEGG; ath:AT5G09640; -.
DR Araport; AT5G09640; -.
DR TAIR; locus:2144751; AT5G09640.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q8VZU3; -.
DR OMA; DQCISEI; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q8VZU3; -.
DR BioCyc; ARA:AT5G09640-MON; -.
DR BRENDA; 2.3.1.91; 399.
DR PRO; PR:Q8VZU3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZU3; baseline and differential.
DR Genevisible; Q8VZU3; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0047202; F:sinapoylglucose-choline O-sinapoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016752; F:sinapoyltransferase activity; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0019748; P:secondary metabolic process; IMP:TAIR.
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; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..291
FT /note="Serine carboxypeptidase-like 19 chain A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000274633"
FT PROPEP 292..317
FT /note="Linker peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000274634"
FT CHAIN 318..465
FT /note="Serine carboxypeptidase-like 19 chain B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000274635"
FT ACT_SITE 178
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT ACT_SITE 389
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT ACT_SITE 443
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT BINDING 77..79
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT BINDING 177..179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT BINDING 439..443
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 82..353
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250|UniProtKB:P52708"
FT DISULFID 246..260
FT /evidence="ECO:0000250|UniProtKB:P52708"
FT DISULFID 284..320
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250|UniProtKB:P52708"
FT CONFLICT 192
FT /note="S -> L (in Ref. 1; AAK52316)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="Missing (in Ref. 1; AAK52316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 52579 MW; FE503DC4216753B1 CRC64;
MRNLSFIVLF LLTLFFIHHL VDASLLVKSL PGFEGPLPFE LETGYVSIGE SGDVELFYYF
VKSERNPEND PLMIWLTGGP GCSSICGLLF ANGPLAFKGD EYNGTVPPLE LTSFSWTKVA
NILYLEAPAG SGYSYAKTRR AFESSDTKQM HQIDQFLRSW FVKHPEFISN PFYVGGDSYS
GKIVPGAVQQ ISLGNEKGLT PLINIQGYVL GNPVTDKNIE TNYRVPFAHG MGLISDELFE
SLERSCGGKF FNVDPSNARC SNNLQAYDHC MSEIYSEHIL LRNCKVDYVL ADTPNIRTDR
RRVMKEFSVN DSSSLPPPSC FTYRYFLSAF WANDENVRRA LGVKKEVGKW NRCNSQNIPY
TFEIFNAVPY HVNNSLKGFR SLIYSGDHDS MVPFSSTQAW IRALNYSIVD DWRPWMMSSN
QVAGYTRTYA NKMTFATIKG GGHTAEYTPD QCSLMFRRWI DGEPL
