ID   SCP36_ARATH             Reviewed;         482 AA.
AC   Q9SV04;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Serine carboxypeptidase-like 36;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL36; OrderedLocusNames=At3g52000; ORFNames=F4F15.110;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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, flowers and siliques.
CC       {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; AL049711; CAB41320.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78873.1; -; Genomic_DNA.
DR   EMBL; DQ056620; AAY78768.1; -; mRNA.
DR   PIR; T49079; T49079.
DR   RefSeq; NP_190768.1; NM_115059.3.
DR   AlphaFoldDB; Q9SV04; -.
DR   SMR; Q9SV04; -.
DR   ESTHER; arath-SCP36; Carboxypeptidase_S10.
DR   MEROPS; S10.A37; -.
DR   PaxDb; Q9SV04; -.
DR   PRIDE; Q9SV04; -.
DR   ProteomicsDB; 232940; -.
DR   EnsemblPlants; AT3G52000.1; AT3G52000.1; AT3G52000.
DR   GeneID; 824363; -.
DR   Gramene; AT3G52000.1; AT3G52000.1; AT3G52000.
DR   KEGG; ath:AT3G52000; -.
DR   Araport; AT3G52000; -.
DR   TAIR; locus:2083695; AT3G52000.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_2_1; -.
DR   InParanoid; Q9SV04; -.
DR   OMA; RRNKHSW; -.
DR   OrthoDB; 607679at2759; -.
DR   PhylomeDB; Q9SV04; -.
DR   PRO; PR:Q9SV04; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SV04; baseline and differential.
DR   Genevisible; Q9SV04; 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   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.
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..482
FT                   /note="Serine carboxypeptidase-like 36"
FT                   /id="PRO_0000274651"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        402
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        455
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        119..363
FT                   /evidence="ECO:0000250"
FT   DISULFID        275..286
FT                   /evidence="ECO:0000250"
FT   DISULFID        310..331
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   482 AA;  54359 MW;  071F4291B5078D2E CRC64;
     MGKRQDWSVT ACIFLFLSLA SQIHCRSHIP FPSPKRGVSS SGDTSHFNVI QRESVPSPKD
     KDLIQQLPGQ PSDVTFKQYG GYVAVNKPAG RFLYYYFVET IKPGNTTPLV IWFNGGPGCS
     SLGGAFKELG PFRVHSDGKT LFRNPYSWNN EANVLFLETP VGTGFSYSNS PINGKQGDKA
     TAEDNYMFLV NWLERFPEYK GRDIYIAGQS YAGHYVPQLA QIILHRNNQT LINLRGILIG
     NPSLNREIQD DFGYKFMFSH GLISQQQMDN YNKFCTDSDL YDWDKCHLAS QKIEAQKTHL
     DIYNIYAPLC LNSTLSSEPK KCTTIMKADP CSGNYLKAYL NIKEVQEAIH ANTTKIPYEW
     TSCNTKLLWE WNEKDRYVSL TPILQELMGK GVRVMLYNGD VDLVIPFTST LAVVKTMNLT
     VVKEWRPWFT GGHVGGFTED YKGNLTFVTV KGAGHSVPTD QPIHALNIFT SFIRNTPLPQ
     TA