ID   SCP17_ARATH             Reviewed;         437 AA.
AC   Q9C7D6; Q9LHI6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Serine carboxypeptidase-like 17;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL17; OrderedLocusNames=At3g12203; ORFNames=F28J15.16;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA   Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA   Shinozaki K., Ecker J.R.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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 seedlings and siliques.
CC       {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB03129.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC069472; AAG51061.1; -; Genomic_DNA.
DR   EMBL; AP002047; BAB03129.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE75166.1; -; Genomic_DNA.
DR   EMBL; BT012565; AAS99709.1; -; mRNA.
DR   RefSeq; NP_187828.1; NM_112056.3.
DR   AlphaFoldDB; Q9C7D6; -.
DR   SMR; Q9C7D6; -.
DR   STRING; 3702.AT3G12203.1; -.
DR   ESTHER; arath-SCP17; Carboxypeptidase_S10.
DR   MEROPS; S10.A19; -.
DR   PaxDb; Q9C7D6; -.
DR   PRIDE; Q9C7D6; -.
DR   EnsemblPlants; AT3G12203.1; AT3G12203.1; AT3G12203.
DR   GeneID; 820399; -.
DR   Gramene; AT3G12203.1; AT3G12203.1; AT3G12203.
DR   KEGG; ath:AT3G12203; -.
DR   Araport; AT3G12203; -.
DR   TAIR; locus:2082249; AT3G12203.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_0_1_1; -.
DR   InParanoid; Q9C7D6; -.
DR   OrthoDB; 607679at2759; -.
DR   PhylomeDB; Q9C7D6; -.
DR   BioCyc; ARA:AT3G12203-MON; -.
DR   PRO; PR:Q9C7D6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9C7D6; baseline and differential.
DR   Genevisible; Q9C7D6; 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   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..437
FT                   /note="Serine carboxypeptidase-like 17"
FT                   /id="PRO_0000274631"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        415
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        85..327
FT                   /evidence="ECO:0000250"
FT   DISULFID        249..263
FT                   /evidence="ECO:0000250"
FT   DISULFID        287..293
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   437 AA;  49505 MW;  F53D7CD4B9C3C20E CRC64;
     MGKECYYLSW ILKFHLLLVL IQLVDSGSTI RFLPGFQGPL PFELETGYIG VGEAEKDQMF
     YYFIKSESNP EKDPLLLWLS GGPFCSSFTA LIYENGPIAF KAEEYNGSIP SLVSTTYAWT
     KVASILYLDQ PVGTGFSYSR NPLADIPSDT GVAKPVNEFL HKWLDKHPEF LSNPLYVAGN
     SYSGIVIPTI VQEISNGNHL DSKPQINLQG FVLGNPATDT DIDLNSRIPF AHGKALISDE
     HYESLKRSCQ GNYISVNPRN TKCLKLLEDF KKCVSGISEE YILKPDCMWL YSCMANLHSL
     SEYWANEKSV RKALLVNEGT VRKWIRCNTE IAYNKDIRSS VPYHKYISIE GYRSLVFSGD
     HDMLVPFLGT QAWIRSLNYS IVDDWRPWMV QNQVAGYTRT YANKMTFATV KGGGHTSEYK
     PVETYIMIKR WLSGQPL