SCP23_ARATH
ID SCP23_ARATH Reviewed; 454 AA.
AC O82229; F4INP1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative serine carboxypeptidase-like 23;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL23; OrderedLocusNames=At2g24010; ORFNames=T29E15.21;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 GENE FAMILY, 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).
CC -!- FUNCTION: Probable carboxypeptidase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expression not detected.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC63669.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005170; AAC63669.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC07517.2; -; Genomic_DNA.
DR PIR; E84631; E84631.
DR RefSeq; NP_001318279.1; NM_001335912.1.
DR AlphaFoldDB; O82229; -.
DR SMR; O82229; -.
DR STRING; 3702.AT2G24010.1; -.
DR ESTHER; arath-SCP23; Carboxypeptidase_S10.
DR MEROPS; S10.A30; -.
DR PaxDb; O82229; -.
DR ProteomicsDB; 226630; -.
DR EnsemblPlants; AT2G24010.1; AT2G24010.1; AT2G24010.
DR GeneID; 816935; -.
DR Gramene; AT2G24010.1; AT2G24010.1; AT2G24010.
DR KEGG; ath:AT2G24010; -.
DR Araport; AT2G24010; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_0_1; -.
DR InParanoid; O82229; -.
DR PhylomeDB; O82229; -.
DR PRO; PR:O82229; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82229; baseline and differential.
DR Genevisible; O82229; AT.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..454
FT /note="Putative serine carboxypeptidase-like 23"
FT /id="PRO_0000274639"
FT ACT_SITE 178
FT /evidence="ECO:0000250"
FT ACT_SITE 375
FT /evidence="ECO:0000250"
FT ACT_SITE 427
FT /evidence="ECO:0000250"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..338
FT /evidence="ECO:0000250"
FT DISULFID 247..258
FT /evidence="ECO:0000250"
FT DISULFID 282..306
FT /evidence="ECO:0000250"
SQ SEQUENCE 454 AA; 51528 MW; F15930B2E16B5F4C CRC64;
MARIHLIIIL LVISSTSSSS SSLREQEEDM IKALPGQPQV GFSQFSGYVT VNESHGRSLF
YWLTESPSSS HTKPLLLWLN GGPGCSSIGY GASEEIGPFR INKTGSNLYL NKFTWNTEAN
ILFLESPAGV GFSYTNTSSD LKDSGDERTA QENLIFLIKW MSRFPQYQYR DFYIVGESYA
GHYVPQLAKK IHLYNKAFNN TPIINLKGFM VGNGDMDKHY DRLGAAMYAW SHAMISDKTY
KSILKHCSFT ADKTSDKCNW ALYFAYREFG KVNGYSIYSP SCVHQTNQTK FLHGRLLVEE
YEYDPCTESY AEIYYNRPDV QRAMHANLTS IPYKWTLCNM VVNNNWKDSE FSMLPIYKEL
TAAGLRIWVF SGDTDAVVPV TGTRLALSKL NLPVKTPWYP WYSEKQVGGW TEVYEGLTFA
TIRGAGHEVP VLQPERALTL LRSFLAGKEL PRSY
