SCP9_ARATH
ID SCP9_ARATH Reviewed; 437 AA.
AC O64811;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Serine carboxypeptidase-like 9;
DE AltName: Full=Sinapoylglucose--sinapoylglucose O-sinapoyltransferase;
DE Short=SST;
DE EC=2.3.1.103;
DE AltName: Full=Sinapoylglucose--sinapoylglucose acyltransferase;
DE Flags: Precursor;
GN Name=SCPL9; Synonyms=SST; OrderedLocusNames=At2g23010; ORFNames=F21P24.7;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Catalyzes the formation of 1,2-bis-O-sinapoyl beta-D-
CC glucoside and an unidentified compound 1.
CC {ECO:0000269|PubMed:17600138}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O64811-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:15908604}.
CC -!- DISRUPTION PHENOTYPE: Decreased levels of 1,2-disinapoyl-glucose due to
CC a partial redundancy with SCPL8 and SCPL13.
CC {ECO:0000269|PubMed:17600138}.
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}.
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DR EMBL; AC004401; AAC17818.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07397.1; -; Genomic_DNA.
DR PIR; E84619; E84619.
DR RefSeq; NP_179884.1; NM_127866.3. [O64811-1]
DR AlphaFoldDB; O64811; -.
DR SMR; O64811; -.
DR STRING; 3702.AT2G23010.1; -.
DR ESTHER; arath-SCP9; Carboxypeptidase_S10.
DR MEROPS; S10.A12; -.
DR PaxDb; O64811; -.
DR PRIDE; O64811; -.
DR ProteomicsDB; 232750; -. [O64811-1]
DR EnsemblPlants; AT2G23010.1; AT2G23010.1; AT2G23010. [O64811-1]
DR GeneID; 816832; -.
DR Gramene; AT2G23010.1; AT2G23010.1; AT2G23010. [O64811-1]
DR KEGG; ath:AT2G23010; -.
DR Araport; AT2G23010; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; O64811; -.
DR OMA; STEVWIR; -.
DR PhylomeDB; O64811; -.
DR BioCyc; ARA:AT2G23010-MON; -.
DR BioCyc; MetaCyc:AT2G23010-MON; -.
DR PRO; PR:O64811; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64811; baseline and differential.
DR Genevisible; O64811; 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:0047158; F:sinapoylglucose-sinapoylglucose O-sinapoyltransferase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..437
FT /note="Serine carboxypeptidase-like 9"
FT /id="PRO_0000274623"
FT ACT_SITE 175
FT /evidence="ECO:0000250"
FT ACT_SITE 362
FT /evidence="ECO:0000250"
FT ACT_SITE 415
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 243..257
FT /evidence="ECO:0000250"
FT DISULFID 281..293
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 49756 MW; 9E976FDB66E204B1 CRC64;
MSLILKFMLL ILLVSSHHVR SGSIVKFLPG FKGPLPFELE TGYIGIGEEE NVQFFYYFIK
SDKNPQEDPL IIWLNGGPGC SCLSGLFFEN GPLALKNKVY NGSVPSLVST TYSWTKTANI
IFLDQPVGSG FSYSKTPIER TSDTSEVKKI HEFLQKWLIK HPQFLSNPFY VVGDSYSGMI
VPALVHEISK GNYICCNPPI NLQGYVLGNP ITHIEFEQNF RIPYAHGMSL ISDELYESLK
RICKGNYFSV DPSNKKCLKL VEEYHKCTDN INSHHTLIAN CDDSNTQHIS PDCYYYPYHL
VECWANNESV REALHVDKGS IGEWIRDHRG IPYKSDIRSS IPYHMNNSIN GYRSLIFSGD
HDITMPFQAT QAWIKSLNYS IIDDWRPWMI KGQIAGYTRT YSNKMTFATV KGGGHTAEYL
PEESSIMFQR WISGQPL
