SBT3E_ARATH
ID SBT3E_ARATH Reviewed; 759 AA.
AC Q9SVT4;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Subtilisin-like protease SBT3.14 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 14 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.14 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.14 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At4g21630 {ECO:0000312|Araport:AT4G21630};
GN ORFNames=F17L22.90 {ECO:0000312|EMBL:CAB36807.1};
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16193095; DOI=10.1371/journal.pcbi.0010040;
RA Rautengarten C., Steinhauser D., Bussis D., Stintzi A., Schaller A.,
RA Kopka J., Altmann T.;
RT "Inferring hypotheses on functional relationships of genes: Analysis of the
RT Arabidopsis thaliana subtilase gene family.";
RL PLoS Comput. Biol. 1:E40-E40(2005).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
CC -!- SIMILARITY: Belongs to the peptidase S8 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; AL035527; CAB36807.1; -; Genomic_DNA.
DR EMBL; AL161555; CAB81270.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84483.2; -; Genomic_DNA.
DR PIR; T05838; T05838.
DR RefSeq; NP_001320025.1; NM_001341507.1.
DR AlphaFoldDB; Q9SVT4; -.
DR SMR; Q9SVT4; -.
DR STRING; 3702.AT4G21630.1; -.
DR MEROPS; S08.A47; -.
DR PaxDb; Q9SVT4; -.
DR PRIDE; Q9SVT4; -.
DR ProteomicsDB; 232906; -.
DR EnsemblPlants; AT4G21630.1; AT4G21630.1; AT4G21630.
DR GeneID; 828250; -.
DR Gramene; AT4G21630.1; AT4G21630.1; AT4G21630.
DR KEGG; ath:AT4G21630; -.
DR Araport; AT4G21630; -.
DR TAIR; locus:2119008; AT4G21630.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR InParanoid; Q9SVT4; -.
DR OMA; VEHAGGC; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:Q9SVT4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVT4; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..118
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435212"
FT CHAIN 119..?
FT /note="Subtilisin-like protease SBT3.14"
FT /id="PRO_5004337321"
FT PROPEP ?..759
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435213"
FT DOMAIN 39..117
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 122..611
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 542
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 759 AA; 81222 MW; EC4C75FB0D94A512 CRC64;
MENCLSTLVF LLSIALVLFP KTGVSFLAAE GASDSDSKVY IVYLGEREHD DPELFTASHH
QMLESLLQSK DDAHNSLIYS YQYGFSGFAA LLTSSQAKKI SEHPEVIHVI PNRILKLKTT
RTWDHLGLSP NPTSFSSSSS AKGLLHETNM GSEAIIGVVD TGIWPESKVF NDHGLGPIPQ
RWRGKCESGE QFNAKIHCNN KLIGAKYYLS GLLAETGGKF NRTIIQDFKS NRDAIGHGTH
TATIAGGSFV PNVSFYGLAR GTVRGGAPRA RIASYKVCWN VVGYDGICTV ADMWKAFDDA
IHDQVDVLSV SIGAGIPENS EVDSVDFIAA FHAVAKGITV VAAGGNDGPG AQNITNAAPW
LLTVAATTLD RSFPTKITLG NNQTLFAESL FTGPEISTSL AFLDSDHNVD VKGKTILEFD
STHPSSIAGR GVVAVILAKK PDDLLARYNS IPYIFTDYEI GTHILQYIRT TRSPTVRISA
ATTLNGQPAM TKVAEFSSRG PNSVSPAILK PDIAAPGVSI LAAVSPLDPD AFNGFGLYSG
TSMSTPVVSG IIALLKSLHP NWSPAAMRSA LVTTAWRTSP SGEPIFAQGS NKKLADPFDY
GGGLVNPDKA AQPGLVYDMG IKDYINYMCS AGYIDSSISR VLGKKTKCTI PKPSILDINL
PSITIPNLEK EVTLTRTVTN VGPIKSVYKA VIESPLGITL TVNPTTLVFN SAAKRVLTFS
VKAKTSHKVN SGYFFGSLTW TDGVHDVIIP VSVKTTISM
