SCP24_ARATH
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 25-MAY-2022, entry version 124.
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.AT4G30610.1; -.
DR ESTHER; arath-AT4g30610; Carboxypeptidase_S10.
DR MEROPS; S10.015; -.
DR PaxDb; Q9M099; -.
DR PRIDE; Q9M099; -.
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; locus:2118706; AT4G30610.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_0_1; -.
DR InParanoid; Q9M099; -.
DR OMA; CNFTVER; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; Q9M099; -.
DR PRO; PR:Q9M099; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M099; baseline and differential.
DR Genevisible; Q9M099; AT.
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; 3.40.50.1820; -; 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; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
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
