SCP20_ARATH
ID SCP20_ARATH Reviewed; 497 AA.
AC Q8L7B2; Q9SV78;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Serine carboxypeptidase-like 20;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL20; OrderedLocusNames=At4g12910; ORFNames=F25G13.7;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
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: Ubiquitous. {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB53091.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB53091.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB78333.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78333.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL079349; CAB53091.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161535; CAB78333.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83202.1; -; Genomic_DNA.
DR EMBL; AY136365; AAM97031.1; -; mRNA.
DR EMBL; BT000181; AAN15500.1; -; mRNA.
DR PIR; A85139; A85139.
DR RefSeq; NP_193027.5; NM_117360.8.
DR AlphaFoldDB; Q8L7B2; -.
DR SMR; Q8L7B2; -.
DR STRING; 3702.AT4G12910.1; -.
DR ESTHER; arath-SCP20; Carboxypeptidase_S10.
DR MEROPS; S10.A11; -.
DR PaxDb; Q8L7B2; -.
DR PRIDE; Q8L7B2; -.
DR ProteomicsDB; 226627; -.
DR EnsemblPlants; AT4G12910.1; AT4G12910.1; AT4G12910.
DR GeneID; 826903; -.
DR Gramene; AT4G12910.1; AT4G12910.1; AT4G12910.
DR KEGG; ath:AT4G12910; -.
DR Araport; AT4G12910; -.
DR TAIR; locus:2123186; AT4G12910.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q8L7B2; -.
DR OMA; AIHAQPV; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q8L7B2; -.
DR PRO; PR:Q8L7B2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7B2; baseline and differential.
DR Genevisible; Q8L7B2; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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 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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..497
FT /note="Serine carboxypeptidase-like 20"
FT /id="PRO_0000274636"
FT MOTIF 495..497
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 186
FT /evidence="ECO:0000250"
FT ACT_SITE 421
FT /evidence="ECO:0000250"
FT ACT_SITE 474
FT /evidence="ECO:0000250"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..386
FT /evidence="ECO:0000250"
FT DISULFID 254..266
FT /evidence="ECO:0000250"
FT DISULFID 289..353
FT /evidence="ECO:0000250"
FT CONFLICT 221
FT /note="G -> V (in Ref. 3; AAM97031/AAN15500)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 55833 MW; 0258C97B8C6A9D8B CRC64;
MSIITMVWLM KVFVFVTLLS LVFVITESAP ESALITKLPG FEGTFPSKHY SGYVTIDKEH
GKNLWYYFIE SEKNPSKDPV VLWLNGGPGC SSMDGFVYEH GPFNFELPKK NNSLPLLHLN
PYSWSKVSNI IYLDSPVGVG FSYSNNKSDY ITGDIKTAVD SHAFLLKWFQ MFPEFQSNPF
FISGESYAGV YVPTLASEVV IGNKNGVKPA LNFKGYLVGN GVADPKFDGN AFVPFAHGMG
LISDELFENV TKACKGNFYE IEGLECEEQY TKVNDDTNQL NIYNILEPCY HGTSLSAFDI
RSLPSSLLQL GKTEKRLPIR KRMFGRAWPV RAPVHPGIVP SWSQLLADVT VPCIDDRVAT
AWLNDPEIRK AIHTKEESEI GRWELCSGKL SFYHDAGSMI DFHRNLTLSG YRALIYSGDH
DMCVPFTGSE AWTKSLGYKV IDEWRAWISN DQVAGYTQGY ANNLTFLTIK GAGHTVPEYK
PREALDFYSR FLEGSKI
