SCP13_ARATH
ID SCP13_ARATH Reviewed; 430 AA.
AC Q8H780; O64808; Q94EH0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Serine carboxypeptidase-like 13;
DE AltName: Full=Sinapoylglucose--sinapoylglucose O-sinapoyltransferase;
DE EC=2.3.1.103;
DE AltName: Full=Sinapoylglucose--sinapoylglucose acyltransferase;
DE Flags: Precursor;
GN Name=SCPL13; OrderedLocusNames=At2g22980; ORFNames=F21P24.4, T20K9.20;
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 MRNA] (ISOFORM 2).
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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] OF 78-430 (ISOFORM 1).
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 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 [6]
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).
CC -!- FUNCTION: Catalyzes the formation of 1,2-bis-O-sinapoyl beta-D-
CC glucoside. {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=2;
CC Name=1;
CC IsoId=Q8H780-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H780-2; Sequence=VSP_022847, VSP_022848;
CC -!- TISSUE SPECIFICITY: Expression not detected.
CC {ECO:0000269|PubMed:15908604}.
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=AAK95312.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAN18098.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF083796; AAN60354.1; -; mRNA.
DR EMBL; AC004401; AAC17815.1; -; Genomic_DNA.
DR EMBL; AC004786; AAM15008.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07385.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07386.1; -; Genomic_DNA.
DR EMBL; AF410326; AAK95312.1; ALT_FRAME; mRNA.
DR EMBL; BT000529; AAN18098.1; ALT_INIT; mRNA.
DR PIR; B84619; B84619.
DR RefSeq; NP_001031402.1; NM_001036325.3. [Q8H780-2]
DR RefSeq; NP_179881.3; NM_127863.5. [Q8H780-1]
DR AlphaFoldDB; Q8H780; -.
DR SMR; Q8H780; -.
DR STRING; 3702.AT2G22980.4; -.
DR ESTHER; arath-SCP13; Carboxypeptidase_S10.
DR MEROPS; S10.004; -.
DR PaxDb; Q8H780; -.
DR PRIDE; Q8H780; -.
DR ProteomicsDB; 232702; -. [Q8H780-1]
DR EnsemblPlants; AT2G22980.1; AT2G22980.1; AT2G22980. [Q8H780-1]
DR EnsemblPlants; AT2G22980.2; AT2G22980.2; AT2G22980. [Q8H780-2]
DR GeneID; 816829; -.
DR Gramene; AT2G22980.1; AT2G22980.1; AT2G22980. [Q8H780-1]
DR Gramene; AT2G22980.2; AT2G22980.2; AT2G22980. [Q8H780-2]
DR KEGG; ath:AT2G22980; -.
DR Araport; AT2G22980; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q8H780; -.
DR OMA; RTNVIFL; -.
DR PhylomeDB; Q8H780; -.
DR BioCyc; ARA:AT2G22980-MON; -.
DR BioCyc; MetaCyc:AT2G22980-MON; -.
DR PRO; PR:Q8H780; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8H780; baseline and differential.
DR Genevisible; Q8H780; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..430
FT /note="Serine carboxypeptidase-like 13"
FT /id="PRO_0000274627"
FT ACT_SITE 177
FT /evidence="ECO:0000250"
FT ACT_SITE 355
FT /evidence="ECO:0000250"
FT ACT_SITE 408
FT /evidence="ECO:0000250"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..319
FT /evidence="ECO:0000250"
FT DISULFID 240..254
FT /evidence="ECO:0000250"
FT DISULFID 278..285
FT /evidence="ECO:0000250"
FT VAR_SEQ 405..411
FT /note="GSGHTAE -> ASLLVST (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_022847"
FT VAR_SEQ 412..430
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_022848"
FT CONFLICT 15
FT /note="I -> F (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="P -> S (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> A (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="S -> A (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="I -> T (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="G -> A (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="K -> N (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="I -> L (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="I -> M (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="K -> E (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="K -> R (in Ref. 1; AAN60354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 49150 MW; D527D52879E8F11B CRC64;
MSLTLEFLLL LIVLILSHHA HSGSIVKFLP GFEGPLPFEL ETGYIGIGEE EEVQLFYYFI
KSEKNPEEDP LLLWLSGGPG CSSLTGLLFE NGPVALKFEV YNGSVPSLVS TTYSWTKMAN
IIFLDQPVGS GFSYSRTPLV DKISDTGEVK RIYEFLQKWL SKHQQFFSNP FYVGGDSYSG
MIVPPLVQEI GKGNYQINLQ GYILGNPITD TESEQNYQIP YAHGMALISD ELYKSMERIC
KGNYVKVDSL NTKCYKLIKD YQKCIHKLNK YHILLPDCDI TSPDCFLYRY TLITFWANNK
SVREALQVNK GSIGKWVQCN YKNISYNYDI KSSVAYHMKN SIDGYRSLIY NGDHDMMVPF
LATQAWIRSL NYSITDDWKP WMINDQIAGY TRSYSNKMTF ATIKGSGHTA EYKPKETSIM
FKRWISAQPL
