SBT3F_ARATH
ID SBT3F_ARATH Reviewed; 761 AA.
AC F4JJL8; Q1PE61; Q9SVT3;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Subtilisin-like protease SBT3.15 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 15 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.15 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.15 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At4g21640 {ECO:0000312|Araport:AT4G21640};
GN ORFNames=F17L22.100 {ECO:0000312|EMBL:CAB81271.1};
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 {ECO:0000312|Proteomes:UP000006548};
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JJL8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JJL8-2; Sequence=VSP_058030, VSP_058031;
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE84484.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB36808.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81271.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035527; CAB36808.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161555; CAB81271.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84484.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ446857; ABE66081.1; -; mRNA.
DR PIR; T05839; T05839.
DR RefSeq; NP_193895.2; NM_118284.2.
DR AlphaFoldDB; F4JJL8; -.
DR SMR; F4JJL8; -.
DR STRING; 3702.AT4G21640.1; -.
DR MEROPS; S08.A42; -.
DR PaxDb; F4JJL8; -.
DR PRIDE; F4JJL8; -.
DR ProteomicsDB; 232869; -. [F4JJL8-1]
DR GeneID; 828251; -.
DR KEGG; ath:AT4G21640; -.
DR Araport; AT4G21640; -.
DR TAIR; locus:2119018; AT4G21640.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR InParanoid; F4JJL8; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:F4JJL8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JJL8; baseline.
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 2: Evidence at transcript level;
KW Alternative splicing; Autocatalytic cleavage; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..120
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435214"
FT CHAIN 121..?
FT /note="Subtilisin-like protease SBT3.15"
FT /id="PRO_5003316476"
FT PROPEP ?..761
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435215"
FT DOMAIN 41..119
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 134..613
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 164
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 544
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 299..301
FT /note="KAY -> NGL (in isoform 2)"
FT /id="VSP_058030"
FT VAR_SEQ 302..761
FT /note="Missing (in isoform 2)"
FT /id="VSP_058031"
SQ SEQUENCE 761 AA; 81479 MW; D3641E91F976ABC7 CRC64;
MENSFLSSKL VFLLAIALVL FLNTELSFLT AEGASDSNSK VYIVYLGQRE HDDPELLTAS
HHQMLESLLQ SKEDAHNSMI YSYQHGFSGF AALLTSSQAK KISEHPEVIH VIPNRILKLK
TTRIWDHLGL SPIPTSFSSS SSAKAKGLLH NTSMGSEAII GVVDSGIWPE SKVFNDQGLG
PIPKRWRGKC RSGEKFNATM HCNKKLIGAK YYQSGLLAMN GGKFNRIIIR DFKSNRDATG
HGTHTATIAG GSFVPNASFY GLARGTVRGG APRARIASYK ACWNVVGWGG ICSSADMWKA
YDDAIHDQVD VLSVSIGASI PEDSERVDFI AAFHAVAKGI TVVAAAGNDG SGAQTICNVA
PWLLTVAATT LDRSFPTKIT LGNNQTFFVS NLAESLFTGP EISTGLAFLD DDVDVKGKTI
LEFDSTHPSS IAGRGVVAVI LAKKPDDRPA PDNSYIFTDY EIGTHILQYI RTTRSPTVRI
SAATTLTGQP ATPKVAAFSS RGPNSVSPAI LKPDIAAPGV SILAAVSPLD PGAFNGFKLH
SGTSMSTPVV SGIIVLLKSL HPKWSPAAMR SALVTTAWRT SPSGEPIFAQ GSNKKLADPF
DYGGGLVNPE KAAKPGLVYD MGIKDYINYM CSAGYNDSSI SRVLGKKTKC PIPKPSMLDI
NLPSITIPNL EKEVTLTRTV TNVGPIKSVY RAVIESPLGI TLTVNPTILV FKSAAKRVLT
FSVKAKTSHK VNSGYFFGSL TWTDGVHDVT IPVSVKTTIS M
