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Serine carboxypeptidase 24 (EC 3.4.16.6) (Bri1 suppressor 1) (Carboxypeptidase D) (Serine carboxypeptidase II) [Cleaved into: Serine carboxypeptidase 24 chain A (Serine carboxypeptidase II chain A); Serine carboxypeptidase 24 chain B (Serine carboxypeptidase II chain B)]

 SCP24_ARATH             Reviewed;         465 AA.
Q9M099; Q94K84;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
10-MAY-2017, entry version 104.
RecName: Full=Serine carboxypeptidase 24;
EC=3.4.16.6;
AltName: Full=Bri1 suppressor 1;
AltName: Full=Carboxypeptidase D;
AltName: Full=Serine carboxypeptidase II;
Contains:
RecName: Full=Serine carboxypeptidase 24 chain A;
AltName: Full=Serine carboxypeptidase II chain A;
Contains:
RecName: Full=Serine carboxypeptidase 24 chain B;
AltName: Full=Serine carboxypeptidase II chain B;
Flags: Precursor;
Name=SCPL24; Synonyms=BRS1; OrderedLocusNames=At4g30610;
ORFNames=F17I23.50;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
FUNCTION, AND MUTAGENESIS OF SER-181 AND HIS-438.
PubMed=11320207; DOI=10.1073/pnas.091065998;
Li J., Lease K.A., Tax F.E., Walker J.C.;
"BRS1, a serine carboxypeptidase, regulates BRI1 signaling in
Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 98:5916-5921(2001).
[5]
FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND
MUTAGENESIS OF HIS-438.
PubMed=16123046; DOI=10.1074/jbc.M503299200;
Zhou A., Li J.;
"Arabidopsis BRS1 is a secreted and active serine carboxypeptidase.";
J. Biol. Chem. 280:35554-35561(2005).
[6]
GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
PubMed=15908604; DOI=10.1104/pp.104.057950;
Fraser C.M., Rider L.W., Chapple C.;
"An expression and bioinformatics analysis of the Arabidopsis serine
carboxypeptidase-like gene family.";
Plant Physiol. 138:1136-1148(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
-!- 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. {ECO:0000269|PubMed:11320207,
ECO:0000269|PubMed:16123046}.
-!- CATALYTIC ACTIVITY: Preferential release of a C-terminal arginine
or lysine residue.
-!- ENZYME REGULATION: Completely inhibited by phenylmethylsulfonyl
fluoride (PMSF) and partially by leupeptin.
{ECO:0000269|PubMed:16123046}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.5. {ECO:0000269|PubMed:16123046};
Temperature dependence:
Optimum temperature is 50 degrees Celsius.
{ECO:0000269|PubMed:16123046};
-!- SUBUNIT: Heterodimer. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space
{ECO:0000269|PubMed:16123046}.
-!- TISSUE SPECIFICITY: Expressed in shoots, leaves, cauline leaves,
siliques and flowers. Expressed a low levels in roots and stems.
{ECO:0000269|PubMed:15908604, ECO:0000269|PubMed:16123046}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:16123046}.
-!- MISCELLANEOUS: Was isolated as a suppressor of bri1 mutant
phenotype. The serine carboxypeptidase activity is necessary for
suppression of bri1 mutant phenotype.
-!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL161577; CAB79779.1; -; Genomic_DNA.
EMBL; CP002687; AEE85786.1; -; Genomic_DNA.
EMBL; BT002334; AAN86167.1; -; mRNA.
EMBL; AF370198; AAK44013.1; -; mRNA.
PIR; B85358; B85358.
RefSeq; NP_194790.1; NM_119207.3.
UniGene; At.31819; -.
UniGene; At.4582; -.
ProteinModelPortal; Q9M099; -.
SMR; Q9M099; -.
STRING; 3702.AT4G30610.1; -.
ESTHER; arath-AT4g30610; Carboxypeptidase_S10.
MEROPS; S10.015; -.
PaxDb; Q9M099; -.
PRIDE; Q9M099; -.
EnsemblPlants; AT4G30610.1; AT4G30610.1; AT4G30610.
GeneID; 829184; -.
Gramene; AT4G30610.1; AT4G30610.1; AT4G30610.
KEGG; ath:AT4G30610; -.
Araport; AT4G30610; -.
TAIR; locus:2118706; AT4G30610.
eggNOG; KOG1282; Eukaryota.
eggNOG; COG2939; LUCA.
HOGENOM; HOG000198295; -.
InParanoid; Q9M099; -.
KO; K16297; -.
OMA; CNFTVER; -.
OrthoDB; EOG09360880; -.
PhylomeDB; Q9M099; -.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q9M099; -.
Proteomes; UP000006548; Chromosome 4.
Genevisible; Q9M099; AT.
GO; GO:0005615; C:extracellular space; IDA:TAIR.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IDA:TAIR.
GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IGI:TAIR.
GO; GO:0006508; P:proteolysis; IDA:TAIR.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR001563; Peptidase_S10.
InterPro; IPR033124; Ser_caboxypep_his_AS.
InterPro; IPR018202; Ser_caboxypep_ser_AS.
PANTHER; PTHR11802; PTHR11802; 1.
Pfam; PF00450; Peptidase_S10; 1.
PRINTS; PR00724; CRBOXYPTASEC.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
1: Evidence at protein level;
Carboxypeptidase; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Protease; Reference proteome; Secreted; Signal; Zymogen.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 286 Serine carboxypeptidase 24 chain A.
{ECO:0000250}.
/FTId=PRO_0000004306.
PROPEP 287 316 Linker peptide. {ECO:0000250}.
/FTId=PRO_0000004307.
CHAIN 317 465 Serine carboxypeptidase 24 chain B.
{ECO:0000250}.
/FTId=PRO_0000004308.
ACT_SITE 181 181 {ECO:0000250}.
ACT_SITE 386 386 {ECO:0000250}.
ACT_SITE 438 438 {ECO:0000250}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 88 349 Interchain (between A and B chains).
{ECO:0000250}.
DISULFID 249 260 {ECO:0000250}.
DISULFID 285 317 Interchain (between A and B chains).
{ECO:0000250}.
MUTAGEN 181 181 S->F: Loss of activity.
{ECO:0000269|PubMed:11320207}.
MUTAGEN 438 438 H->A: Loss of activity. Decrease in A and
B chains cleavage efficiency.
{ECO:0000269|PubMed:11320207,
ECO:0000269|PubMed:16123046}.
CONFLICT 107 107 T -> N (in Ref. 3; AAK44013).
{ECO:0000305}.
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


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