ID   SCP33_ARATH             Reviewed;         478 AA.
AC   Q9LSM9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Serine carboxypeptidase-like 33;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL33; OrderedLocusNames=At3g17180; ORFNames=K14A17.30;
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 senescent leaves and flowers.
CC       {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA94996.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB026636; BAA94996.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002686; AEE75915.1; -; Genomic_DNA.
DR   RefSeq; NP_188343.1; NM_112594.2.
DR   AlphaFoldDB; Q9LSM9; -.
DR   SMR; Q9LSM9; -.
DR   STRING; 3702.AT3G17180.1; -.
DR   ESTHER; arath-SCP33; Carboxypeptidase_S10.
DR   MEROPS; S10.A20; -.
DR   PaxDb; Q9LSM9; -.
DR   PRIDE; Q9LSM9; -.
DR   ProteomicsDB; 232824; -.
DR   EnsemblPlants; AT3G17180.1; AT3G17180.1; AT3G17180.
DR   GeneID; 820975; -.
DR   Gramene; AT3G17180.1; AT3G17180.1; AT3G17180.
DR   KEGG; ath:AT3G17180; -.
DR   Araport; AT3G17180; -.
DR   TAIR; locus:2086137; AT3G17180.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_0_1; -.
DR   InParanoid; Q9LSM9; -.
DR   OMA; DQVYERI; -.
DR   OrthoDB; 607679at2759; -.
DR   PRO; PR:Q9LSM9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LSM9; baseline and differential.
DR   Genevisible; Q9LSM9; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; 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..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..478
FT                   /note="Serine carboxypeptidase-like 33"
FT                   /id="PRO_0000274648"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        398
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        451
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..361
FT                   /evidence="ECO:0000250"
FT   DISULFID        257..268
FT                   /evidence="ECO:0000250"
FT   DISULFID        292..330
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  54145 MW;  0C3FEA72217D6276 CRC64;
     MNLTLPMKKQ KFLLIISLLI LLSLLHQDYH IEAQNSDKVV NLPEQPLNPK ISHFSGYVNV
     NQENTRSLFF WFFEALSESP STRPLVLWLN GGPGCSSIGY GAASELGPFR VVENGTSLSF
     NQYSWVQEAN MLFLESPVGV GFSYTNSSSD LENLNDAFVA EDAYNFMVAW FARYPQYKSR
     DFFIAGESYA GHYSPQLAEL IYDRNKVQPK DSFINLKGFI VGNPLTDDEY DNKGILEYAW
     SHAVISDHLY DSAKHNCDFK SSNWSEPCNV AMNTVFTKYK EIDIYNIYAP KCISNSSSGA
     SYLGFGVNDK SPAVKDWFKR VRWFEGYDPC YSNYAEEYFN RVDVRLSLHA TTRNVARWKV
     CNDSILQTYH FTVSSMLPTY SKLIKAGLKI WVYSGDADGR VPVIGSRYCV EALGISVKSE
     WRSWFHNHQV GGRITEYEGG LTFVTVRGAG HLVPLNKPEE ALALFRSFLN GQELPSSP