ID   SCP11_ARATH             Reviewed;         433 AA.
AC   Q2V465; O64807;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Serine carboxypeptidase-like 11;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL11; OrderedLocusNames=At2g22970; ORFNames=F21P24.3, T20K9.19;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q2V465-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2V465-2; Sequence=VSP_022845, VSP_022846;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {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; AC004401; AAC17814.1; -; Genomic_DNA.
DR   EMBL; AC004786; AAM15007.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07382.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07383.1; -; Genomic_DNA.
DR   EMBL; AY039596; AAK62651.1; -; mRNA.
DR   EMBL; AY113074; AAM47382.1; -; mRNA.
DR   EMBL; BT000747; AAN31888.1; -; mRNA.
DR   PIR; A84619; A84619.
DR   RefSeq; NP_001031401.1; NM_001036324.1. [Q2V465-2]
DR   RefSeq; NP_179880.1; NM_127862.4. [Q2V465-1]
DR   AlphaFoldDB; Q2V465; -.
DR   SMR; Q2V465; -.
DR   STRING; 3702.AT2G22970.3; -.
DR   ESTHER; arath-SCP11; Carboxypeptidase_S10.
DR   MEROPS; S10.A08; -.
DR   PaxDb; Q2V465; -.
DR   PRIDE; Q2V465; -.
DR   ProteomicsDB; 232916; -. [Q2V465-1]
DR   EnsemblPlants; AT2G22970.1; AT2G22970.1; AT2G22970. [Q2V465-1]
DR   EnsemblPlants; AT2G22970.2; AT2G22970.2; AT2G22970. [Q2V465-2]
DR   GeneID; 816828; -.
DR   Gramene; AT2G22970.1; AT2G22970.1; AT2G22970. [Q2V465-1]
DR   Gramene; AT2G22970.2; AT2G22970.2; AT2G22970. [Q2V465-2]
DR   KEGG; ath:AT2G22970; -.
DR   Araport; AT2G22970; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_0_1_1; -.
DR   InParanoid; Q2V465; -.
DR   OMA; NEFLRQW; -.
DR   PhylomeDB; Q2V465; -.
DR   BioCyc; ARA:AT2G22970-MON; -.
DR   PRO; PR:Q2V465; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q2V465; baseline and differential.
DR   Genevisible; Q2V465; 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   Alternative splicing; Carboxypeptidase; Disulfide bond; Glycoprotein;
KW   Hydrolase; Protease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..433
FT                   /note="Serine carboxypeptidase-like 11"
FT                   /id="PRO_0000274625"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        411
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        80..322
FT                   /evidence="ECO:0000250"
FT   DISULFID        243..257
FT                   /evidence="ECO:0000250"
FT   DISULFID        281..288
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         314..320
FT                   /note="RSIGKWE -> VYAINNV (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_022845"
FT   VAR_SEQ         321..433
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_022846"
SQ   SEQUENCE   433 AA;  49233 MW;  729A21EEC080D6D4 CRC64;
     MELTLKLLVL LLFILNHHVG SGSIVKFLPG FEGPLPFELE TGYIGIGEEE EVQLFYYFIK
     SERNPKEDPL LLWLSGGPGC SSITGLLFQN GPLALKSEVY NGSVPSLVST TYSWTKTANI
     IFLDQPVGAG FSYSRAPLID TPTDTGEVKR IHEFLQKWLS KHPQFSSNHF YAGGDSYSGM
     IVPALVQEIS KGNYICCNPP INLKGYVLGN PITHEDDPNY RIPFSHGMAL ISDELYESIR
     EACKGNYFNV DPRNTKCLKL VEEFHKCTDK LNEFHILSPD CDTASPDCYL YPFYLISFWA
     NDESVRDALH VNKRSIGKWE RCNYLSKPYN KDIKSSVPYH MNNSVSGYRS LIYSGDHDLV
     VPFLATQAWI KSLNYSIIDE WRPWMIRDQI TGYTRTYSNK MTFATVKGSG HTAENKPQES
     FIMFRRWING QPL