SCP21_ARATH
ID SCP21_ARATH Reviewed; 494 AA.
AC Q9LSV8; F4J901;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serine carboxypeptidase-like 21;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL21; OrderedLocusNames=At3g25420; ORFNames=MWL2.3;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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, 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).
CC -!- FUNCTION: Probable carboxypeptidase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and siliques.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01313.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025639; BAB01313.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77009.2; -; Genomic_DNA.
DR RefSeq; NP_001319641.1; NM_001338744.1.
DR AlphaFoldDB; Q9LSV8; -.
DR SMR; Q9LSV8; -.
DR STRING; 3702.AT3G25420.1; -.
DR ESTHER; arath-SCP21; Carboxypeptidase_S10.
DR MEROPS; S10.A10; -.
DR PaxDb; Q9LSV8; -.
DR PRIDE; Q9LSV8; -.
DR ProteomicsDB; 226628; -.
DR EnsemblPlants; AT3G25420.1; AT3G25420.1; AT3G25420.
DR GeneID; 822126; -.
DR Gramene; AT3G25420.1; AT3G25420.1; AT3G25420.
DR KEGG; ath:AT3G25420; -.
DR Araport; AT3G25420; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q9LSV8; -.
DR OMA; MIPYHKT; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q9LSV8; -.
DR PRO; PR:Q9LSV8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSV8; baseline and differential.
DR Genevisible; Q9LSV8; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019748; P:secondary metabolic process; IBA:GO_Central.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..494
FT /note="Serine carboxypeptidase-like 21"
FT /id="PRO_0000274637"
FT ACT_SITE 179
FT /evidence="ECO:0000250"
FT ACT_SITE 418
FT /evidence="ECO:0000250"
FT ACT_SITE 471
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..383
FT /evidence="ECO:0000250"
FT DISULFID 247..263
FT /evidence="ECO:0000250"
FT DISULFID 286..350
FT /evidence="ECO:0000250"
SQ SEQUENCE 494 AA; 54885 MW; D93690347B5CFB8C CRC64;
MGRLVEAIIA SILLSLCFTI TKSAPKSALI TNLPGFNGTF PSKHYAGYVA IDKHRNKNLW
YYFVESERNA SVDPVVLWLN GGPGCSSMDG FVYEHGPFNF EPKKKNSHLL HLNPYSWSKV
SNIIYLDSPV GVGFSYSNDN ADYTTDDTKT ASDTHTFLLE WFKMFPEFQS NPFFISGESY
AGIYVPTLAA EVVKGHKNVT KPVINFKGYL VGNGVTDEVF DGNALVPFTH GMGLISDELY
EETKLVCNGT YYTGGQSGVS KECAGKLKTV SDTVNLLNLY NILEPCYHGT SLSALDIEFL
PKSLLTLGKT EKPMAVRKRM FGRAWPLGAV VRPGIVPSWS QLLAGFGVPC IDDTVATKWL
NDPAVRKAVH AKEEKAIGNW ELCSSNLEYR HDTGSMIEYH RNLTLSGFRA LIFSGDHDMC
VPYTGSEAWT KAMGYKVVDE WRPWMSNNQV AGFTQGYANN LTFLTIKGAG HTVPEYKPRE
SLDFYSRFLA GEKI
