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Q9M099

- SCP24_ARATH

UniProt

Q9M099 - SCP24_ARATH

Protein

Serine carboxypeptidase 24

Gene

SCPL24

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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

    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: Chromosome 4

    Organism-specific databases

    TAIRiAT4G30610.

    Subcellular locationi

    Secretedextracellular space 1 Publication

    GO - Cellular componenti

    1. extracellular space Source: TAIR

    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.
    OMAiTYWWTHA.
    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

    MARTHFIFLL LVALLSTTFP SSSSSREQEK DRIKALPGQP KVAFSQYSGY    50
    VNVNQSHGRA LFYWLTESSS PSPHTKPLLL WLNGGPGCSS IAYGASEEIG 100
    PFRINKTGSN LYLNKFAWNK DANLLFLESP AGVGYSYTNT SSDLKDSGDE 150
    RTAQDNLIFL IKWLSRFPQY KYRDFYIAGE SYAGHYVPQL AKKINDYNKA 200
    FSKPIINLKG FLVGNAVTDN QYDSIGTVTY WWTHAIISDK SYKSILKYCN 250
    FTVERVSDDC DNAVNYAMNH EFGDIDQYSI YTPTCVAAQQ KKNTTGFFVR 300
    MKNTLLRRRL VSGYDPCTES YAEKYFNRPD VQRAMHANVT GIRYKWTACS 350
    DVLIKTWKDS DKTMLPIYKE LAASGLRIWI FSGDTDSVVP VTATRFSLSH 400
    LNLPVKTRWY PWYTDNQVGG WTEVYKGLTF ATVRGAGHEV PLFEPKRALI 450
    LFRSFLAGKE LPRSY 465
    Length:465
    Mass (Da):52,845
    Last modified:October 1, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL161577 Genomic DNA. Translation: CAB79779.1 .
    CP002687 Genomic DNA. Translation: AEE85786.1 .
    BT002334 mRNA. Translation: AAN86167.1 .
    AF370198 mRNA. Translation: AAK44013.1 .
    PIRi B85358.
    RefSeqi NP_194790.1. NM_119207.3.
    UniGenei At.31819.
    At.4582.

    3D structure databases

    ProteinModelPortali Q9M099.
    SMRi Q9M099. Positions 25-462.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S10.015.

    Proteomic databases

    PaxDbi Q9M099.
    PRIDEi Q9M099.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G30610.1 ; AT4G30610.1 ; AT4G30610 .
    GeneIDi 829184.
    KEGGi ath:AT4G30610.

    Organism-specific databases

    TAIRi AT4G30610.

    Phylogenomic databases

    eggNOGi COG2939.
    HOGENOMi HOG000198295.
    InParanoidi Q9M099.
    KOi K16297.
    OMAi TYWWTHA.
    PhylomeDBi Q9M099.

    Enzyme and pathway databases

    BioCyci ARA:AT4G30610-MONOMER.

    Gene expression databases

    Genevestigatori Q9M099.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    [Graphical view ]
    PANTHERi PTHR11802. PTHR11802. 1 hit.
    Pfami PF00450. Peptidase_S10. 1 hit.
    [Graphical view ]
    PRINTSi PR00724. CRBOXYPTASEC.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00560. CARBOXYPEPT_SER_HIS. 1 hit.
    PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(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.
      , 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.

    Entry informationi

    Entry nameiSCP24_ARATH
    AccessioniPrimary (citable) accession number: Q9M099
    Secondary accession number(s): Q94K84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 89 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