ID   SCP24_ARATH             Reviewed;         465 AA.
AC   Q9M099; Q94K84;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 129.
DE   RecName: Full=Serine carboxypeptidase 24;
DE            EC=3.4.16.6;
DE   AltName: Full=Bri1 suppressor 1;
DE   AltName: Full=Carboxypeptidase D;
DE   AltName: Full=Serine carboxypeptidase II;
DE   Contains:
DE     RecName: Full=Serine carboxypeptidase 24 chain A;
DE     AltName: Full=Serine carboxypeptidase II chain A;
DE   Contains:
DE     RecName: Full=Serine carboxypeptidase 24 chain B;
DE     AltName: Full=Serine carboxypeptidase II chain B;
DE   Flags: Precursor;
GN   Name=SCPL24; Synonyms=BRS1; OrderedLocusNames=At4g30610;
GN   ORFNames=F17I23.50;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, AND MUTAGENESIS OF SER-181 AND HIS-438.
RX   PubMed=11320207; DOI=10.1073/pnas.091065998;
RA   Li J., Lease K.A., Tax F.E., Walker J.C.;
RT   "BRS1, a serine carboxypeptidase, regulates BRI1 signaling in Arabidopsis
RT   thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:5916-5921(2001).
RN   [5]
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND MUTAGENESIS OF HIS-438.
RX   PubMed=16123046; DOI=10.1074/jbc.m503299200;
RA   Zhou A., Li J.;
RT   "Arabidopsis BRS1 is a secreted and active serine carboxypeptidase.";
RL   J. Biol. Chem. 280:35554-35561(2005).
RN   [6]
RP   GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX   PubMed=15908604; DOI=10.1104/pp.104.057950;
RA   Fraser C.M., Rider L.W., Chapple C.;
RT   "An expression and bioinformatics analysis of the Arabidopsis serine
RT   carboxypeptidase-like gene family.";
RL   Plant Physiol. 138:1136-1148(2005).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
CC   -!- FUNCTION: Active serine carboxypeptidase with broad substrate
CC       preference, including basic and hydrophilic groups. Processes a protein
CC       involved in an early event in the brassinosteroid signaling pathway.
CC       {ECO:0000269|PubMed:11320207, ECO:0000269|PubMed:16123046}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential release of a C-terminal arginine or lysine
CC         residue.; EC=3.4.16.6;
CC   -!- ACTIVITY REGULATION: Completely inhibited by phenylmethylsulfonyl
CC       fluoride (PMSF) and partially by leupeptin.
CC       {ECO:0000269|PubMed:16123046}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:16123046};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:16123046};
CC   -!- SUBUNIT: Heterodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:16123046}.
CC   -!- TISSUE SPECIFICITY: Expressed in shoots, leaves, cauline leaves,
CC       siliques and flowers. Expressed a low levels in roots and stems.
CC       {ECO:0000269|PubMed:15908604, ECO:0000269|PubMed:16123046}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16123046}.
CC   -!- MISCELLANEOUS: Was isolated as a suppressor of bri1 mutant phenotype.
CC       The serine carboxypeptidase activity is necessary for suppression of
CC       bri1 mutant phenotype.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; AL161577; CAB79779.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85786.1; -; Genomic_DNA.
DR   EMBL; BT002334; AAN86167.1; -; mRNA.
DR   EMBL; AF370198; AAK44013.1; -; mRNA.
DR   PIR; B85358; B85358.
DR   RefSeq; NP_194790.1; NM_119207.3.
DR   AlphaFoldDB; Q9M099; -.
DR   SMR; Q9M099; -.
DR   BioGRID; 14471; 1.
DR   STRING; 3702.Q9M099; -.
DR   ESTHER; arath-AT4g30610; Carboxypeptidase_S10.
DR   MEROPS; S10.015; -.
DR   GlyCosmos; Q9M099; 6 sites, No reported glycans.
DR   PaxDb; 3702-AT4G30610-1; -.
DR   ProteomicsDB; 232703; -.
DR   EnsemblPlants; AT4G30610.1; AT4G30610.1; AT4G30610.
DR   GeneID; 829184; -.
DR   Gramene; AT4G30610.1; AT4G30610.1; AT4G30610.
DR   KEGG; ath:AT4G30610; -.
DR   Araport; AT4G30610; -.
DR   TAIR; AT4G30610; BRS1.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_0_1; -.
DR   InParanoid; Q9M099; -.
DR   OMA; CNFTVER; -.
DR   OrthoDB; 1647009at2759; -.
DR   PhylomeDB; Q9M099; -.
DR   PRO; PR:Q9M099; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9M099; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IDA:TAIR.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IDA:TAIR.
DR   GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IGI:TAIR.
DR   GO; GO:0006508; P:proteolysis; IDA:TAIR.
DR   Gene3D; 3.40.50.11320; -; 1.
DR   Gene3D; 6.10.250.940; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF25; SERINE CARBOXYPEPTIDASE 24; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
DR   Genevisible; Q9M099; AT.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..286
FT                   /note="Serine carboxypeptidase 24 chain A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004306"
FT   PROPEP          287..316
FT                   /note="Linker peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004307"
FT   CHAIN           317..465
FT                   /note="Serine carboxypeptidase 24 chain B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004308"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        386
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        88..349
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        249..260
FT                   /evidence="ECO:0000250"
FT   DISULFID        285..317
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         181
FT                   /note="S->F: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11320207"
FT   MUTAGEN         438
FT                   /note="H->A: Loss of activity. Decrease in A and B chains
FT                   cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:11320207,
FT                   ECO:0000269|PubMed:16123046"
FT   CONFLICT        107
FT                   /note="T -> N (in Ref. 3; AAK44013)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   465 AA;  52845 MW;  6403510C34110033 CRC64;
     MARTHFIFLL LVALLSTTFP SSSSSREQEK DRIKALPGQP KVAFSQYSGY VNVNQSHGRA
     LFYWLTESSS PSPHTKPLLL WLNGGPGCSS IAYGASEEIG PFRINKTGSN LYLNKFAWNK
     DANLLFLESP AGVGYSYTNT SSDLKDSGDE RTAQDNLIFL IKWLSRFPQY KYRDFYIAGE
     SYAGHYVPQL AKKINDYNKA FSKPIINLKG FLVGNAVTDN QYDSIGTVTY WWTHAIISDK
     SYKSILKYCN FTVERVSDDC DNAVNYAMNH EFGDIDQYSI YTPTCVAAQQ KKNTTGFFVR
     MKNTLLRRRL VSGYDPCTES YAEKYFNRPD VQRAMHANVT GIRYKWTACS DVLIKTWKDS
     DKTMLPIYKE LAASGLRIWI FSGDTDSVVP VTATRFSLSH LNLPVKTRWY PWYTDNQVGG
     WTEVYKGLTF ATVRGAGHEV PLFEPKRALI LFRSFLAGKE LPRSY
//