SCP12_ARATH
ID SCP12_ARATH Reviewed; 435 AA.
AC O81009; Q3EBW1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Serine carboxypeptidase-like 12;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL12; OrderedLocusNames=At2g22920; ORFNames=T20K9.13;
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 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=O81009-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O81009-2; Sequence=VSP_027465;
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:15908604}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AC004786; AAC32439.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07373.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07374.1; -; Genomic_DNA.
DR PIR; E84618; E84618.
DR RefSeq; NP_179876.1; NM_127857.5. [O81009-1]
DR RefSeq; NP_850033.1; NM_179702.1. [O81009-2]
DR AlphaFoldDB; O81009; -.
DR SMR; O81009; -.
DR STRING; 3702.AT2G22920.2; -.
DR ESTHER; arath-SCP12; Carboxypeptidase_S10.
DR MEROPS; S10.A09; -.
DR PaxDb; O81009; -.
DR PRIDE; O81009; -.
DR ProteomicsDB; 226603; -. [O81009-1]
DR EnsemblPlants; AT2G22920.1; AT2G22920.1; AT2G22920. [O81009-2]
DR EnsemblPlants; AT2G22920.2; AT2G22920.2; AT2G22920. [O81009-1]
DR GeneID; 816823; -.
DR Gramene; AT2G22920.1; AT2G22920.1; AT2G22920. [O81009-2]
DR Gramene; AT2G22920.2; AT2G22920.2; AT2G22920. [O81009-1]
DR KEGG; ath:AT2G22920; -.
DR Araport; AT2G22920; -.
DR TAIR; locus:2059175; AT2G22920.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; O81009; -.
DR OMA; FSMENAG; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; O81009; -.
DR BioCyc; ARA:AT2G22920-MON; -.
DR PRO; PR:O81009; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81009; baseline and differential.
DR Genevisible; O81009; 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..435
FT /note="Serine carboxypeptidase-like 12"
FT /id="PRO_0000274626"
FT ACT_SITE 176
FT /evidence="ECO:0000250"
FT ACT_SITE 360
FT /evidence="ECO:0000250"
FT ACT_SITE 413
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..323
FT /evidence="ECO:0000250"
FT DISULFID 244..258
FT /evidence="ECO:0000250"
FT DISULFID 282..289
FT /evidence="ECO:0000250"
FT VAR_SEQ 396..435
FT /note="TRTYSNKMTFATVKGSGHTAEYKPNETFIMFQRWISGHDL -> IIYFCVIH
FT ENLFQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_027465"
SQ SEQUENCE 435 AA; 49705 MW; C6F50A686AD2D617 CRC64;
MKSTPKLLLL LLFIINHHVD SGSIVKFLPG FEGPLPFELE TGYIGIGEEE DVQLFYYFIK
SERNPKEDPL LLWLSGGPGC SSITGLLFEN GPLALKSKVY NGSVPSLVST TYSWTKTANI
IFLDQPIGAG FSYSRIPLID TPSDTGEVKN IHEFLQKWLS KHPQFSSNPF YASGDSYSGM
IVPALVQEIS KGNYICCKPP INLQGYILGN PITYFEVDQN YRIPFSHGMA LISDELYESI
RRDCKGNYFN VDPRNTKCLK LVEEYHKCTD ELNEFNILSP DCDTTSPDCF LYPYYLLGYW
INDESVRDAL HVNKSSIGKW ERCTYQNRIP YNKDINNSIP YHMNNSISGY RSLIYSGDHD
LVVPFLATQA WIKSLNYSII HEWRPWMIKD QIAGYTRTYS NKMTFATVKG SGHTAEYKPN
ETFIMFQRWI SGHDL
