ID   SCP16_ARATH             Reviewed;         435 AA.
AC   Q9C7D4; Q9LHI4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Serine carboxypeptidase-like 16;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL16; OrderedLocusNames=At3g12220; ORFNames=F28J15.109, F28J15.15;
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   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, roots and leaves.
CC       {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB03131.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC069472; AAG51080.1; -; Genomic_DNA.
DR   EMBL; AP002047; BAB03131.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE75169.1; -; Genomic_DNA.
DR   RefSeq; NP_566414.3; NM_112058.4.
DR   AlphaFoldDB; Q9C7D4; -.
DR   SMR; Q9C7D4; -.
DR   STRING; 3702.AT3G12220.1; -.
DR   ESTHER; arath-SCP16; Carboxypeptidase_S10.
DR   MEROPS; S10.A17; -.
DR   iPTMnet; Q9C7D4; -.
DR   PaxDb; Q9C7D4; -.
DR   PRIDE; Q9C7D4; -.
DR   EnsemblPlants; AT3G12220.1; AT3G12220.1; AT3G12220.
DR   GeneID; 820402; -.
DR   Gramene; AT3G12220.1; AT3G12220.1; AT3G12220.
DR   KEGG; ath:AT3G12220; -.
DR   Araport; AT3G12220; -.
DR   TAIR; locus:2082239; AT3G12220.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_0_1_1; -.
DR   InParanoid; Q9C7D4; -.
DR   OMA; MIHDQVA; -.
DR   OrthoDB; 607679at2759; -.
DR   PhylomeDB; Q9C7D4; -.
DR   BioCyc; ARA:AT3G12220-MON; -.
DR   PRO; PR:Q9C7D4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9C7D4; baseline and differential.
DR   Genevisible; Q9C7D4; 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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..435
FT                   /note="Serine carboxypeptidase-like 16"
FT                   /id="PRO_0000274630"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        360
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        413
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..325
FT                   /evidence="ECO:0000250"
FT   DISULFID        246..260
FT                   /evidence="ECO:0000250"
FT   DISULFID        284..291
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   435 AA;  49237 MW;  FEB6A1BFB7F5D11A CRC64;
     MGSWIPKLLL LQLVLLLTKH ADSSSIIKYL PGFEGPLPFE LETGYIGVGE EDEDQMFYYF
     IKSESNPKTD PLLLWLSGGP GCSSFTGLIY ENGPLGFKVE AYNGSIPTLV STTYSWTKVA
     NIIYLDQPVG TGFSYSRNPL ADIPSDTGSA KRVDEFLRKW LTKHPEYFSN PFYAGGNSYS
     GKMVPVIVQE ISNGNCIYGK PQIRLQGYVL GSPVTDYDLD RNSRIQFAHG MALISNELYE
     SMKRTCGGNY IFVDPLNTEC LELIKDYDNC VSGIYENLIL VPKCDLTSPD CHSYRSMLSD
     YWANNESVRR ALKVVEGTTG RWERCKWTLQ NNKDIKSSIP YHKKNSIQGY RSLIFSGDHD
     MLTPYVGTQD WIRSLNYSII DKWRPWMILD QVAGYTTTYA NKMTFATVKG GGHTLDYKPD
     ENSILFKRWI SGQLL