ID   SCP39_ARATH             Reviewed;         501 AA.
AC   Q9SV02;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Serine carboxypeptidase-like 39;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL39; OrderedLocusNames=At3g52020; ORFNames=F4F15.130;
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   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 seedlings, roots, leaves, flowers and
CC       siliques. {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL049711; CAB41322.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78875.1; -; Genomic_DNA.
DR   PIR; T49081; T49081.
DR   RefSeq; NP_190770.1; NM_115061.2.
DR   AlphaFoldDB; Q9SV02; -.
DR   SMR; Q9SV02; -.
DR   ESTHER; arath-SCP39; Carboxypeptidase_S10.
DR   MEROPS; S10.A38; -.
DR   PaxDb; Q9SV02; -.
DR   PRIDE; Q9SV02; -.
DR   ProteomicsDB; 232941; -.
DR   EnsemblPlants; AT3G52020.1; AT3G52020.1; AT3G52020.
DR   GeneID; 824365; -.
DR   Gramene; AT3G52020.1; AT3G52020.1; AT3G52020.
DR   KEGG; ath:AT3G52020; -.
DR   Araport; AT3G52020; -.
DR   TAIR; locus:2083720; AT3G52020.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_2_1; -.
DR   InParanoid; Q9SV02; -.
DR   OMA; MMNLTAV; -.
DR   OrthoDB; 607679at2759; -.
DR   PhylomeDB; Q9SV02; -.
DR   PRO; PR:Q9SV02; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SV02; baseline and differential.
DR   Genevisible; Q9SV02; 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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..501
FT                   /note="Serine carboxypeptidase-like 39"
FT                   /id="PRO_0000274654"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        421
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        474
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        134..381
FT                   /evidence="ECO:0000250"
FT   DISULFID        292..303
FT                   /evidence="ECO:0000250"
FT   DISULFID        327..351
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   501 AA;  56553 MW;  8B8D7E1F6F9C76CA CRC64;
     MGELQDWSVT TCLLLLLFQA SQIHCTSQTH VLNRLLYRSK RGFGSSVDTN HLNAIRHLSV
     SSPQNTSGVN QQEQKERDLI ENLPGQPSVS FRQYGGYVTV NESAGRSLYY YFVEATKTKK
     SLPLVLWLNG GPGCSSLYGA FQELGPFRIY GDGKTLYTNP YSWNNVANIL FLESPVGTGF
     SYTNTESDLE NPGDMKAAAD KYIFLVKWLE RFPEYKGREF YIAGESYAGH YVPQLAQTIL
     VHNKNQNFIN LRGILIGNPT LNDIVETTGS FDYLVSHALL SQDSLLSYKE NCATDTPKME
     VDCIALSMKI DDDIKKMNLY NILTPTCINA TLTPLTNQSK ECTTVLQYEP CGMQYIAAYL
     NREDVQRSMH VTKLPHTWML CNEATGFNWN QTDYSASMLP ILKELMKHDQ LRVWVYTGDT
     DTVIPLTVTM HALKMMNLTA VTDWLPWFSE GQVGGFTEEY KGNFRYATVI GAGHEVPLYK
     PKAALTLFKH FIRNSPLPLT P