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Protein

Serine carboxypeptidase 24

Gene

SCPL24

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

Completely inhibited by phenylmethylsulfonyl fluoride (PMSF) and partially by leupeptin.1 Publication

pH dependencei

Optimum pH is 5.5.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei181 – 1811By similarity
Active sitei386 – 3861By similarity
Active sitei438 – 4381By similarity

GO - Molecular functioni

  1. serine-type carboxypeptidase activity Source: TAIR

GO - Biological processi

  1. brassinosteroid mediated signaling pathway Source: TAIR
  2. proteolysis Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Enzyme and pathway databases

BioCyciARA:AT4G30610-MONOMER.

Protein family/group databases

MEROPSiS10.015.

Names & Taxonomyi

Protein namesi
Recommended 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:
Alternative name(s):
Serine carboxypeptidase II chain A
Alternative name(s):
Serine carboxypeptidase II chain B
Gene namesi
Name:SCPL24
Synonyms:BRS1
Ordered Locus Names:At4g30610
ORF Names:F17I23.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G30610.

Subcellular locationi

Secretedextracellular space 1 Publication

GO - Cellular componenti

  1. extracellular space Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi181 – 1811S → F: Loss of activity. 1 Publication
Mutagenesisi438 – 4381H → A: Loss of activity. Decrease in A and B chains cleavage efficiency. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 286262Serine carboxypeptidase 24 chain ABy similarityPRO_0000004306Add
BLAST
Propeptidei287 – 31630Linker peptideBy similarityPRO_0000004307Add
BLAST
Chaini317 – 465149Serine carboxypeptidase 24 chain BBy similarityPRO_0000004308Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi88 ↔ 349Interchain (between A and B chains)By similarity
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi249 ↔ 260By similarity
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi285 ↔ 317Interchain (between A and B chains)By similarity
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9M099.
PRIDEiQ9M099.

Expressioni

Tissue specificityi

Expressed in shoots, leaves, cauline leaves, siliques and flowers. Expressed a low levels in roots and stems.2 Publications

Gene expression databases

GenevestigatoriQ9M099.

Interactioni

Subunit structurei

Heterodimer.Curated

Structurei

3D structure databases

ProteinModelPortaliQ9M099.
SMRiQ9M099. Positions 25-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2939.
HOGENOMiHOG000198295.
InParanoidiQ9M099.
KOiK16297.
OMAiDNQVGGW.
PhylomeDBiQ9M099.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9M099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTHFIFLL LVALLSTTFP SSSSSREQEK DRIKALPGQP KVAFSQYSGY
60 70 80 90 100
VNVNQSHGRA LFYWLTESSS PSPHTKPLLL WLNGGPGCSS IAYGASEEIG
110 120 130 140 150
PFRINKTGSN LYLNKFAWNK DANLLFLESP AGVGYSYTNT SSDLKDSGDE
160 170 180 190 200
RTAQDNLIFL IKWLSRFPQY KYRDFYIAGE SYAGHYVPQL AKKINDYNKA
210 220 230 240 250
FSKPIINLKG FLVGNAVTDN QYDSIGTVTY WWTHAIISDK SYKSILKYCN
260 270 280 290 300
FTVERVSDDC DNAVNYAMNH EFGDIDQYSI YTPTCVAAQQ KKNTTGFFVR
310 320 330 340 350
MKNTLLRRRL VSGYDPCTES YAEKYFNRPD VQRAMHANVT GIRYKWTACS
360 370 380 390 400
DVLIKTWKDS DKTMLPIYKE LAASGLRIWI FSGDTDSVVP VTATRFSLSH
410 420 430 440 450
LNLPVKTRWY PWYTDNQVGG WTEVYKGLTF ATVRGAGHEV PLFEPKRALI
460
LFRSFLAGKE LPRSY
Length:465
Mass (Da):52,845
Last modified:September 30, 2000 - v1
Checksum:i6403510C34110033
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071T → N in AAK44013 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161577 Genomic DNA. Translation: CAB79779.1.
CP002687 Genomic DNA. Translation: AEE85786.1.
BT002334 mRNA. Translation: AAN86167.1.
AF370198 mRNA. Translation: AAK44013.1.
PIRiB85358.
RefSeqiNP_194790.1. NM_119207.3.
UniGeneiAt.31819.
At.4582.

Genome annotation databases

EnsemblPlantsiAT4G30610.1; AT4G30610.1; AT4G30610.
GeneIDi829184.
KEGGiath:AT4G30610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161577 Genomic DNA. Translation: CAB79779.1.
CP002687 Genomic DNA. Translation: AEE85786.1.
BT002334 mRNA. Translation: AAN86167.1.
AF370198 mRNA. Translation: AAK44013.1.
PIRiB85358.
RefSeqiNP_194790.1. NM_119207.3.
UniGeneiAt.31819.
At.4582.

3D structure databases

ProteinModelPortaliQ9M099.
SMRiQ9M099. Positions 25-462.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS10.015.

Proteomic databases

PaxDbiQ9M099.
PRIDEiQ9M099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G30610.1; AT4G30610.1; AT4G30610.
GeneIDi829184.
KEGGiath:AT4G30610.

Organism-specific databases

TAIRiAT4G30610.

Phylogenomic databases

eggNOGiCOG2939.
HOGENOMiHOG000198295.
InParanoidiQ9M099.
KOiK16297.
OMAiDNQVGGW.
PhylomeDBiQ9M099.

Enzyme and pathway databases

BioCyciARA:AT4G30610-MONOMER.

Gene expression databases

GenevestigatoriQ9M099.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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.
    , 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(2002) [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(2000) [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(2004) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, TISSUE SPECIFICITY, NOMENCLATURE.

Entry informationi

Entry nameiSCP24_ARATH
AccessioniPrimary (citable) accession number: Q9M099
Secondary accession number(s): Q94K84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 3, 2005
Last sequence update: September 30, 2000
Last modified: January 6, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.