SCP10_ARATH
ID SCP10_ARATH Reviewed; 437 AA.
AC O64810;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine carboxypeptidase-like 10;
DE AltName: Full=Sinapoylglucose--anthocyanin acyltransferase;
DE AltName: Full=Sinapoylglucose--anthocyanin sinapoyltransferase;
DE Short=SAT;
DE EC=2.3.1.-;
DE Flags: Precursor;
GN Name=SCPL10; Synonyms=SAT; OrderedLocusNames=At2g23000; ORFNames=F21P24.6;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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).
RN [6]
RP FUNCTION.
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).
RN [7]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
CC -!- FUNCTION: Involved in the biosynthesis of sinapoylated anthocyanins.
CC {ECO:0000269|PubMed:17600138, ECO:0000269|PubMed:19969522}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in senescent leaves.
CC {ECO:0000269|PubMed:15908604}.
CC -!- DISRUPTION PHENOTYPE: Lack of sinapoylated anthocyanins.
CC {ECO:0000269|PubMed:17600138}.
CC -!- MISCELLANEOUS: In cv. Pna-10, this protein SCP10 and the adjacent SCP8
CC are not present due to a natural 13-kb deletion (PubMed:19969522).
CC {ECO:0000305|PubMed:19969522}.
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=AY089099; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC004401; AAC17817.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07395.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62468.1; -; Genomic_DNA.
DR EMBL; AY089099; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D84619; D84619.
DR RefSeq; NP_001324624.1; NM_001335834.1.
DR RefSeq; NP_179883.1; NM_127865.3.
DR AlphaFoldDB; O64810; -.
DR SMR; O64810; -.
DR STRING; 3702.AT2G23000.1; -.
DR ESTHER; arath-SCP10; Carboxypeptidase_S10.
DR MEROPS; S10.A13; -.
DR PaxDb; O64810; -.
DR PRIDE; O64810; -.
DR ProteomicsDB; 232701; -.
DR EnsemblPlants; AT2G23000.1; AT2G23000.1; AT2G23000.
DR EnsemblPlants; AT2G23000.2; AT2G23000.2; AT2G23000.
DR GeneID; 816831; -.
DR Gramene; AT2G23000.1; AT2G23000.1; AT2G23000.
DR Gramene; AT2G23000.2; AT2G23000.2; AT2G23000.
DR KEGG; ath:AT2G23000; -.
DR Araport; AT2G23000; -.
DR TAIR; locus:2045384; AT2G23000.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; O64810; -.
DR OMA; RTYANRM; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; O64810; -.
DR BioCyc; ARA:AT2G23000-MON; -.
DR BioCyc; MetaCyc:AT2G23000-MON; -.
DR PRO; PR:O64810; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64810; baseline and differential.
DR Genevisible; O64810; 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: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; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal; Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..437
FT /note="Serine carboxypeptidase-like 10"
FT /id="PRO_0000274624"
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 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..327
FT /evidence="ECO:0000250"
FT DISULFID 243..257
FT /evidence="ECO:0000250"
FT DISULFID 281..293
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 49785 MW; A290AF519B350943 CRC64;
MGSTLKHLLL LLLVLIRHVD SAAIVKSLPG LEGRLPFELE TGYIGIGEEE DIQLFYYFIK
SENNPKEDPL LLWLDGGPGC SSLGGLLFEN GPVALKSAVY NGSNPSLFST TYSWTKMANI
IYLDQPVGSG FSYSRTPIGK SSDTSEVKRI HEFLQKWLSK HPQFFSNPFY VTGDSYSGMI
VPALVQEISK GNYICCKHLI NLQGYVLGNP ITYAEHEKNY RIPFSHGMSL ISDELYESLK
RNCKGNYENV DPRNTKCVRL VEEYHKCTDK INTQHILIPD CDKKGHGITS PDCYYYLYFL
IECWANNERV REALHVTKGT KGQWQRCNWT IPYDNNIISS VPYHMDNSIN GYRSLIYSGD
HDITMPFQAT QAWIKSLNYS IVDDWRPWMI NDQIAGYTRT YSNKMTFATV KGGGHTAEYL
PNESSIMFQR WISGQPL
