SCP42_ARATH
ID SCP42_ARATH Reviewed; 473 AA.
AC Q9FH05;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Serine carboxypeptidase-like 42;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL42; OrderedLocusNames=At5g42240; ORFNames=K5J14.4;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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;
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 -!- TISSUE SPECIFICITY: Expression not detected.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AB023032; BAB10197.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94786.1; -; Genomic_DNA.
DR EMBL; AF361604; AAK32772.1; -; mRNA.
DR EMBL; AY143899; AAN28838.1; -; mRNA.
DR RefSeq; NP_199039.1; NM_123589.4.
DR AlphaFoldDB; Q9FH05; -.
DR SMR; Q9FH05; -.
DR BioGRID; 19479; 1.
DR IntAct; Q9FH05; 1.
DR STRING; 3702.AT5G42240.1; -.
DR ESTHER; arath-SCP42; Carboxypeptidase_S10.
DR MEROPS; S10.A21; -.
DR PaxDb; Q9FH05; -.
DR PRIDE; Q9FH05; -.
DR ProteomicsDB; 226610; -.
DR EnsemblPlants; AT5G42240.1; AT5G42240.1; AT5G42240.
DR GeneID; 834229; -.
DR Gramene; AT5G42240.1; AT5G42240.1; AT5G42240.
DR KEGG; ath:AT5G42240; -.
DR Araport; AT5G42240; -.
DR TAIR; locus:2157622; AT5G42240.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_1_1; -.
DR InParanoid; Q9FH05; -.
DR OMA; YSSWFRR; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; Q9FH05; -.
DR PRO; PR:Q9FH05; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH05; baseline and differential.
DR Genevisible; Q9FH05; 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; 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; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..473
FT /note="Serine carboxypeptidase-like 42"
FT /id="PRO_0000274657"
FT ACT_SITE 179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..346
FT /evidence="ECO:0000250"
FT DISULFID 247..264
FT /evidence="ECO:0000250"
FT DISULFID 289..314
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 52874 MW; 714E0F29BC251590 CRC64;
MASVSWRAVA VAMVVVLLSL QWFAKGYPEE DLVVRLPGQP TVGFKQYAGY VDVDVKAGRS
LFYYYVEAVK QPDSKPLTLW LNGGPGCSSI GGGAFTELGP FYPTGDGRGL RVNSMSWNKA
SHLLFVESPA GVGWSYSNKS SDYNTGDKST ANDMLVFLLR WFEKFPKLKS RDLFLTGESY
AGHYIPQLAD AILSYNSHSS GFKFNIKGVA IGNPLLKLDR DSPATYEFFW SHGMISDELK
LTITSQCDFD DYTFASPHNV STACNEAISE TENIITEYVN NYDVLLDVCY PSIVQQELRL
KKMATKMSMG VDVCMTYERR FYFNLPEVQK ALHANRTHLP YSWSMCSGVL NYSDIDGNID
MLPILKRIIL NKTPIWIFSG DQDSVVPFGG SRTLVRELAQ DLNFKTTVPY GAWFHKSQVG
GWAIEYGKLL TFATVRGAAH MVPYAQPSRA LHLFSSFVSG RRLPNNTHSS TDE
