Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine carboxypeptidase-like 8

Gene

SCPL8

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in plants secondary metabolism. Functions as acyltransferase to form the sinapate ester sinapoylmalate. Also capable of catalyzing the formation of 1,2-bis-O-sinapoyl beta-D-glucoside.5 Publications

Miscellaneous

In cv. Pna-10, this protein SCP8 and the adjacent SCP10 are not present due to a natural 13-kb deletion (PubMed:19969522).1 Publication

Caution

Was classified as a serine carboxypeptidase-like (SCPL) protein solely on the basis of the overall sequence similarity (PubMed:15908604) but it has been shown that it belongs to a class of enzymes that catalyze acyltransferase reactions (PubMed:17600138).2 Publications

Catalytic activityi

1-O-sinapoyl-beta-D-glucose + (S)-malate = D-glucose + sinapoyl-(S)-malate.
2 1-O-sinapoyl beta-D-glucoside = D-glucose + 1,2-bis-O-sinapoyl beta-D-glucoside.

Enzyme regulationi

95% inhibition by diisopropyl fluorophosphate (DFP) and 30% by phenylmethylsulfonyl fluoride (PMSF).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei173By similarity1
Active sitei358By similarity1
Active sitei411By similarity1

GO - Molecular functioni

GO - Biological processi

  • phenylpropanoid metabolic process Source: TAIR
  • proteolysis Source: InterPro

Keywordsi

Molecular functionAcyltransferase, Transferase

Enzyme and pathway databases

BioCyciARA:AT2G22990-MONOMER
BRENDAi2.3.1.92 399
ReactomeiR-ATH-2132295 MHC class II antigen presentation
R-ATH-6798695 Neutrophil degranulation

Protein family/group databases

ESTHERiarath-SCP8 Carboxypeptidase_S10
MEROPSiS10.A14

Names & Taxonomyi

Protein namesi
Recommended name:
Serine carboxypeptidase-like 8
Alternative name(s):
Protein SINAPOYLGLUCOSE ACCUMULATOR 1
Sinapoylglucose--malate O-sinapoyltransferase (EC:2.3.1.92)
Short name:
SMT
Sinapoylglucose--sinapoylglucose O-sinapoyltransferase (EC:2.3.1.103)
Gene namesi
Name:SCPL8
Synonyms:SMT, SNG1
Ordered Locus Names:At2g22990
ORF Names:F21P24.5, T20K9.18
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

AraportiAT2G22990
TAIRilocus:2045374 AT2G22990

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Disruption phenotypei

Plants do not contain sinapoylmalate and accumulate its biosynthetic precursor, sinapoylglucose.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi73N → A: 87% reduction of activity. 1 Publication1
Mutagenesisi172 – 175DSYS → ESYA: 85% reduction of activity. 1 Publication4
Mutagenesisi173S → A: Total loss of activity. 1 Publication1
Mutagenesisi268K → E: 25% reduction of activity. 1 Publication1
Mutagenesisi272H → D: 78% reduction of activity. 1 Publication1
Mutagenesisi322R → E: 99% reduction of activity. 1 Publication1
Mutagenesisi358D → A: 80% reduction of activity. 1 Publication1
Mutagenesisi411H → A: Total loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 192 PublicationsAdd BLAST19
ChainiPRO_000027462220 – 433Serine carboxypeptidase-like 8Add BLAST414

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi78 ↔ 323By similarity
Glycosylationi99N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi241 ↔ 255By similarity
Disulfide bondi279 ↔ 289By similarity
Glycosylationi283N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi324N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi342N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi418N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8RUW5

Expressioni

Tissue specificityi

Highly expressed in seedlings. Expressed in leaves, stems, flowers and siliques, and at low levels in roots.3 Publications

Gene expression databases

ExpressionAtlasiQ8RUW5 baseline and differential
GenevisibleiQ8RUW5 AT

Interactioni

Protein-protein interaction databases

STRINGi3702.AT2G22990.3

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DRFmodel-B20-433[»]
ProteinModelPortaliQ8RUW5
SMRiQ8RUW5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1282 Eukaryota
COG2939 LUCA
HOGENOMiHOG000198297
InParanoidiQ8RUW5
KOiK09757
OMAiECWANDE
PhylomeDBiQ8RUW5

Family and domain databases

Gene3Di3.40.50.18201 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR001563 Peptidase_S10
PANTHERiPTHR11802 PTHR11802, 1 hit
PfamiView protein in Pfam
PF00450 Peptidase_S10, 1 hit
PRINTSiPR00724 CRBOXYPTASEC
SUPFAMiSSF53474 SSF53474, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8RUW5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSLKIKFLLL LVLYHHVDSA SIVKFLPGFE GPLPFELETG YIGIGEDENV
60 70 80 90 100
QFFYYFIKSE NNPKEDPLLI WLNGGPGCSC LGGIIFENGP VGLKFEVFNG
110 120 130 140 150
SAPSLFSTTY SWTKMANIIF LDQPVGSGFS YSKTPIDKTG DISEVKRTHE
160 170 180 190 200
FLQKWLSRHP QYFSNPLYVV GDSYSGMIVP ALVQEISQGN YICCEPPINL
210 220 230 240 250
QGYMLGNPVT YMDFEQNFRI PYAYGMGLIS DEIYEPMKRI CNGNYYNVDP
260 270 280 290 300
SNTQCLKLTE EYHKCTAKIN IHHILTPDCD VTNVTSPDCY YYPYHLIECW
310 320 330 340 350
ANDESVREAL HIEKGSKGKW ARCNRTIPYN HDIVSSIPYH MNNSISGYRS
360 370 380 390 400
LIYSGDHDIA VPFLATQAWI RSLNYSPIHN WRPWMINNQI AGYTRAYSNK
410 420 430
MTFATIKGGG HTAEYRPNET FIMFQRWISG QPL
Length:433
Mass (Da):49,439
Last modified:February 6, 2007 - v2
Checksum:i67234085A5FBAF0C
GO
Isoform 2 (identifier: Q8RUW5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     408-433: GGGHTAEYRPNETFIMFQRWISGQPL → ASVDTRQSID...NIHVKRSCLC

Note: Derived from EST data. May be due to a competing donor splice site. No experimental confirmation available.
Show »
Length:458
Mass (Da):52,122
Checksum:iDC1C8BB0FF1E94E8
GO

Sequence cautioni

The sequence AAC17816 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAK32769 differs from that shown. Reason: Frameshift at position 260.Curated
The sequence AAM15006 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAN28819 differs from that shown. Reason: Erroneous termination at position 260. Translated as Glu.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_027464408 – 433GGGHT…SGQPL → ASVDTRQSIDQTRPLSCSKG GSVANPCNKRLMTFTYNYLP TNIHVKRSCLC in isoform 2. CuratedAdd BLAST26

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF275313 mRNA Translation: AAF78760.1
AC004401 Genomic DNA Translation: AAC17816.2 Sequence problems.
AC004786 Genomic DNA Translation: AAM15006.1 Sequence problems.
CP002685 Genomic DNA Translation: AEC07390.1
CP002685 Genomic DNA Translation: AEC07393.1
AF361601 mRNA Translation: AAK32769.1 Frameshift.
AY035052 mRNA Translation: AAK59557.1
AY051060 mRNA Translation: AAK93737.1
AY143880 mRNA Translation: AAN28819.1 Sequence problems.
PIRiC84619
RefSeqiNP_850034.1, NM_179703.2 [Q8RUW5-1]
NP_850035.1, NM_179704.1 [Q8RUW5-2]
UniGeneiAt.24365

Genome annotation databases

EnsemblPlantsiAT2G22990.1; AT2G22990.1; AT2G22990 [Q8RUW5-1]
AT2G22990.3; AT2G22990.3; AT2G22990 [Q8RUW5-2]
GeneIDi816830
GrameneiAT2G22990.1; AT2G22990.1; AT2G22990 [Q8RUW5-1]
AT2G22990.3; AT2G22990.3; AT2G22990 [Q8RUW5-2]
KEGGiath:AT2G22990

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSCP8_ARATH
AccessioniPrimary (citable) accession number: Q8RUW5
Secondary accession number(s): O64809, Q3EBV9, Q9ASY4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: April 25, 2018
This is version 105 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome