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Q9M099 (SCP24_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine carboxypeptidase 24

EC=3.4.16.6
Alternative name(s):
Bri1 suppressor 1
Carboxypeptidase D
Serine carboxypeptidase II

Cleaved into the following 2 chains:

  1. Serine carboxypeptidase 24 chain A
    Alternative name(s):
    Serine carboxypeptidase II chain A
  2. Serine carboxypeptidase 24 chain B
    Alternative name(s):
    Serine carboxypeptidase II chain B
Gene names
Name:SCPL24
Synonyms:BRS1
Ordered Locus Names:At4g30610
ORF Names:F17I23.50
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Active serine carboxypeptidase with broad substrate preference, including basic and hydrophilic groups. Processes a protein involved in an early event in the brassinosteroid signaling pathway. Ref.4 Ref.5

Catalytic activity

Preferential release of a C-terminal arginine or lysine residue.

Enzyme regulation

Completely inhibited by phenylmethylsulfonyl fluoride (PMSF) and partially by leupeptin. Ref.5

Subunit structure

Heterodimer Potential.

Subcellular location

Secretedextracellular space Ref.5.

Tissue specificity

Expressed in shoots, leaves, cauline leaves, siliques and flowers. Expressed a low levels in roots and stems. Ref.5 Ref.6

Post-translational modification

N-glycosylated. Ref.5

Miscellaneous

Was isolated as a suppressor of bri1 mutant phenotype. The serine carboxypeptidase activity is necessary for suppression of bri1 mutant phenotype.

Sequence similarities

Belongs to the peptidase S10 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. Ref.5

Temperature dependence:

Optimum temperature is 50 degrees Celsius.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 286262Serine carboxypeptidase 24 chain A By similarity
PRO_0000004306
Propeptide287 – 31630Linker peptide By similarity
PRO_0000004307
Chain317 – 465149Serine carboxypeptidase 24 chain B By similarity
PRO_0000004308

Sites

Active site1811 By similarity
Active site3861 By similarity
Active site4381 By similarity

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation3381N-linked (GlcNAc...) Potential
Disulfide bond88 ↔ 349Interchain (between A and B chains) By similarity
Disulfide bond249 ↔ 260 By similarity
Disulfide bond285 ↔ 317Interchain (between A and B chains) By similarity

Experimental info

Mutagenesis1811S → F: Loss of activity. Ref.4
Mutagenesis4381H → A: Loss of activity. Decrease in A and B chains cleavage efficiency. Ref.4 Ref.5
Sequence conflict1071T → N in AAK44013. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9M099 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6403510C34110033

FASTA46552,845
        10         20         30         40         50         60 
MARTHFIFLL LVALLSTTFP SSSSSREQEK DRIKALPGQP KVAFSQYSGY VNVNQSHGRA 

        70         80         90        100        110        120 
LFYWLTESSS PSPHTKPLLL WLNGGPGCSS IAYGASEEIG PFRINKTGSN LYLNKFAWNK 

       130        140        150        160        170        180 
DANLLFLESP AGVGYSYTNT SSDLKDSGDE RTAQDNLIFL IKWLSRFPQY KYRDFYIAGE 

       190        200        210        220        230        240 
SYAGHYVPQL AKKINDYNKA FSKPIINLKG FLVGNAVTDN QYDSIGTVTY WWTHAIISDK 

       250        260        270        280        290        300 
SYKSILKYCN FTVERVSDDC DNAVNYAMNH EFGDIDQYSI YTPTCVAAQQ KKNTTGFFVR 

       310        320        330        340        350        360 
MKNTLLRRRL VSGYDPCTES YAEKYFNRPD VQRAMHANVT GIRYKWTACS DVLIKTWKDS 

       370        380        390        400        410        420 
DKTMLPIYKE LAASGLRIWI FSGDTDSVVP VTATRFSLSH LNLPVKTRWY PWYTDNQVGG 

       430        440        450        460 
WTEVYKGLTF ATVRGAGHEV PLFEPKRALI LFRSFLAGKE LPRSY 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"BRS1, a serine carboxypeptidase, regulates BRI1 signaling in Arabidopsis thaliana."
Li J., Lease K.A., Tax F.E., Walker J.C.
Proc. Natl. Acad. Sci. U.S.A. 98:5916-5921(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-181 AND HIS-438.
[5]"Arabidopsis BRS1 is a secreted and active serine carboxypeptidase."
Zhou A., Li J.
J. Biol. Chem. 280:35554-35561(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, MUTAGENESIS OF HIS-438.
[6]"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] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, TISSUE SPECIFICITY, NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL161577 Genomic DNA. Translation: CAB79779.1.
CP002687 Genomic DNA. Translation: AEE85786.1.
BT002334 mRNA. Translation: AAN86167.1.
AF370198 mRNA. Translation: AAK44013.1.
PIRB85358.
RefSeqNP_194790.1. NM_119207.3.
UniGeneAt.31819.
At.4582.

3D structure databases

ProteinModelPortalQ9M099.
SMRQ9M099. Positions 31-462.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.015.

Proteomic databases

PaxDbQ9M099.
PRIDEQ9M099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G30610.1; AT4G30610.1; AT4G30610.
GeneID829184.
KEGGath:AT4G30610.

Organism-specific databases

TAIRAT4G30610.

Phylogenomic databases

eggNOGCOG2939.
HOGENOMHOG000198295.
InParanoidQ9M099.
KOK16297.
OMANHEFGDI.
PhylomeDBQ9M099.
ProtClustDBCLSN2685632.

Enzyme and pathway databases

BioCycARA:AT4G30610-MONOMER.

Gene expression databases

GenevestigatorQ9M099.

Family and domain databases

InterProIPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
PROSITEPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSCP24_ARATH
AccessionPrimary (citable) accession number: Q9M099
Secondary accession number(s): Q94K84
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names