Q8VZU3 (SCP19_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine carboxypeptidase-like 19
EC=3.4.16.-

Alternative name(s):
Protein SINAPOYLGLUCOSE ACCUMULATOR 2
Sinapoylglucose--choline O-sinapoyltransferase
Short name=SCT
EC=2.3.1.91

Cleaved into the following 2 chains:

1. Serine carboxypeptidase-like 19 chain A
2. Serine carboxypeptidase-like 19 chain B

Gene names

Name:	SCPL19
Synonyms:	SNG2
Ordered Locus Names:	At5g09640
ORF Names:	F17I14.170

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in plants secondary metabolism. Functions as acyltransferase to form the sinapate ester sinapoylcholine also known as sinapine. May rather catalyze a transesterification reaction rather than a hydrolysis. May also have carboxypeptidase activity. Ref.1 Ref.6
Catalytic activity	1-O-sinapoyl-beta-D-glucose + choline = D-glucose + sinapoylcholine.
Enzyme regulation	Slightly inhibited by phenylmethylsulphonylfluoride (PMSF). Ref.1
Subunit structure	Heterodimer Potential.
Subcellular location	Secreted Potential.
Tissue specificity	Expressed in roots and flowers, and at lower levels in young leaves and seedlings. Ref.1 Ref.7
Post-translational modification	N-glycosylated. Ref.6
Disruption phenotype	Plants accumulate sinapoylglucose and contain low levels of sinapoylcholine and increased levels of choline. Ref.1
Sequence similarities	Belongs to the peptidase S10 family.
Biophysicochemical properties	Kinetic parameters: Measured in vitro at pH 7.0 and 30 degrees Celsius. KM=0.16 mM for sinapoylglucose Ref.6 KM=0.41 mM for feruloylglucose KM=0.1 mM for caffeoylglucose KM=1.9 mM for p-coumaroylglucose KM=3.2 mM for choline KM=19 mM for N,N-dimethylethanolamine KM=245 mM for 2-methylaminoethanol KM=25 mM for neopentyl alcohol KM=105 mM for Tris Vmax=2.8 nmol/sec/mg enzyme with sinapoylglucose as substrate Vmax=1.8 nmol/sec/mg enzyme with feruloylglucose as substrate Vmax=0.75 nmol/sec/mg enzyme with caffeoylglucose as substrate Vmax=3.3 nmol/sec/mg enzyme with p-coumaroylglucose as substrate Vmax=2.5 nmol/sec/mg enzyme with choline as substrate Vmax=1.7 nmol/sec/mg enzyme with N,N-dimethylethanolamine as substrate Vmax=1.2 nmol/sec/mg enzyme with 2-methylaminoethanol as substrate Vmax=0.45 nmol/sec/mg enzyme with neopentyl alcohol as substrate Vmax=0.32 nmol/sec/mg enzyme with Tris as substrate
Sequence caution	The sequence BAB09519.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB89366.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Acyltransferase Carboxypeptidase Hydrolase Protease Transferase
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW secondary metabolic process Inferred from mutant phenotype Ref.1. Source: TAIR
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type carboxypeptidase activity Inferred from electronic annotation. Source: InterPro sinapoylglucose-choline O-sinapoyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 291	268	Serine carboxypeptidase-like 19 chain A By similarity		PRO_0000274633
	Propeptide	292 – 317	26	Linker peptide By similarity		PRO_0000274634
	Chain	318 – 465	148	Serine carboxypeptidase-like 19 chain B By similarity		PRO_0000274635
Sites
	Active site	178	1	By similarity
	Active site	389	1	By similarity
	Active site	443	1	By similarity
Amino acid modifications
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	310	1	N-linked (GlcNAc...) Potential
	Glycosylation	373	1	N-linked (GlcNAc...) Potential
	Glycosylation	405	1	N-linked (GlcNAc...) Potential
	Disulfide bond	82 ↔ 353		Interchain (between A and B chains) By similarity
	Disulfide bond	246 ↔ 260		By similarity
	Disulfide bond	284 ↔ 320		Interchain (between A and B chains) By similarity
Experimental info
	Sequence conflict	192	1	S → L in AAK52316. Ref.1
	Sequence conflict	346	1	Missing in AAK52316. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8VZU3 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: FE503DC4216753B1	FASTA	465	52,579
	10 20 30 40 50 60 MRNLSFIVLF LLTLFFIHHL VDASLLVKSL PGFEGPLPFE LETGYVSIGE SGDVELFYYF 70 80 90 100 110 120 VKSERNPEND PLMIWLTGGP GCSSICGLLF ANGPLAFKGD EYNGTVPPLE LTSFSWTKVA 130 140 150 160 170 180 NILYLEAPAG SGYSYAKTRR AFESSDTKQM HQIDQFLRSW FVKHPEFISN PFYVGGDSYS 190 200 210 220 230 240 GKIVPGAVQQ ISLGNEKGLT PLINIQGYVL GNPVTDKNIE TNYRVPFAHG MGLISDELFE 250 260 270 280 290 300 SLERSCGGKF FNVDPSNARC SNNLQAYDHC MSEIYSEHIL LRNCKVDYVL ADTPNIRTDR 310 320 330 340 350 360 RRVMKEFSVN DSSSLPPPSC FTYRYFLSAF WANDENVRRA LGVKKEVGKW NRCNSQNIPY 370 380 390 400 410 420 TFEIFNAVPY HVNNSLKGFR SLIYSGDHDS MVPFSSTQAW IRALNYSIVD DWRPWMMSSN 430 440 450 460 QVAGYTRTYA NKMTFATIKG GGHTAEYTPD QCSLMFRRWI DGEPL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sng2 mutant of Arabidopsis is defective in the gene encoding the serine carboxypeptidase-like protein sinapoylglucose:choline sinapoyltransferase." Shirley A.M., McMichael C.M., Chapple C. Plant J. 28:83-94(2001) [PubMed: 11696189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, ENZYME REGULATION, TISSUE SPECIFICITY. Strain: cv. Landsberg erecta.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S. DNA Res. 6:183-195(1999) [PubMed: 10470850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Biochemical characterization of sinapoylglucose:choline sinapoyltransferase, a serine carboxypeptidase-like protein that functions as an acyltransferase in plant secondary metabolism." Shirley A.M., Chapple C. J. Biol. Chem. 278:19870-19877(2003) [PubMed: 12657648] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION.
[7]	"An expression and bioinformatics analysis of the Arabidopsis serine carboxypeptidase-like gene family." Fraser C.M., Rider L.W., Chapple C. Plant Physiol. 138:1136-1148(2005) [PubMed: 15908604] [Abstract] Cited for: GENE FAMILY, TISSUE SPECIFICITY, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY033947 mRNA. Translation: AAK52316.1.
AB020752 Genomic DNA. Translation: BAB09519.1. Sequence problems.
AL353994 Genomic DNA. Translation: CAB89366.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED91420.1.
AY063833 mRNA. Translation: AAL36189.1.
AY091309 mRNA. Translation: AAM14248.1.

IPI

IPI00535326.

PIR

T49934.

RefSeq

NP_568215.2. NM_121001.2.

UniGene

At.1794.
At.21648.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DRG	model	-	A	24-284	[»]
			B	311-464	[»]

ProteinModelPortal

Q8VZU3.

SMR

Q8VZU3. Positions 21-465.

ModBase

Search...

Protein-protein interaction databases

STRING

Q8VZU3.

Protein family/group databases

MEROPS

S10.A18.

Proteomic databases

PRIDE

Q8VZU3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G09640.1; AT5G09640.1; AT5G09640.

GeneID

830823.

GenomeReviews

Gene locus AT5G09640 in contig BA000015_GR.

KEGG

ath:AT5G09640.

NMPDR

fig|3702.1.peg.23085.

Organism-specific databases

TAIR

At5g09640.

Phylogenomic databases

eggNOG

KOG1282.

GeneTree

EPGT00050000007670.

HOGENOM

HBG588032.

InParanoid

Q8VZU3.

OMA

FWANDEN.

PhylomeDB

Q8VZU3.

ProtClustDB

CLSN2918093.

Enzyme and pathway databases

BRENDA

2.3.1.91. 399.

Gene expression databases

ArrayExpress

Q8VZU3.

Genevestigator

Q8VZU3.

Family and domain databases

InterPro

IPR001563. Peptidase_S10.
[Graphical view]

KO

K09756.

PANTHER

PTHR11802. Peptidase_S10. 1 hit.

Pfam

PF00450. Peptidase_S10. 1 hit.
[Graphical view]

PRINTS

PR00724. CRBOXYPTASEC.

PROSITE

PS00560. CARBOXYPEPT_SER_HIS. False negative.
PS00131. CARBOXYPEPT_SER_SER. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SCP19_ARATH

Accession

Primary (citable) accession number: Q8VZU3
Secondary accession number(s): Q941P1, Q9FXX7, Q9LXC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 6, 2007
Last sequence update:	March 1, 2002
Last modified:	November 16, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program