SBT3I_ARATH
ID SBT3I_ARATH Reviewed; 779 AA.
AC Q9STQ2;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Subtilisin-like protease SBT3.18 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 18 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.18 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.18 {ECO:0000303|PubMed:16193095}; Synonyms=UNE17;
GN OrderedLocusNames=At4g26330 {ECO:0000312|Araport:AT4G26330};
GN ORFNames=T25K17.140 {ECO:0000312|EMBL:CAB38962.1};
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 -!- SEQUENCE CAUTION:
CC Sequence=AEE85186.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB38962.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79488.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049171; CAB38962.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161565; CAB79488.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85186.1; ALT_SEQ; Genomic_DNA.
DR PIR; T06017; T06017.
DR RefSeq; NP_567744.1; NM_118766.2.
DR AlphaFoldDB; Q9STQ2; -.
DR SMR; Q9STQ2; -.
DR STRING; 3702.AT4G26330.1; -.
DR MEROPS; S08.A40; -.
DR PaxDb; Q9STQ2; -.
DR PeptideAtlas; Q9STQ2; -.
DR PRIDE; Q9STQ2; -.
DR EnsemblPlants; AT4G26330.2; AT4G26330.2; AT4G26330.
DR GeneID; 828739; -.
DR Gramene; AT4G26330.2; AT4G26330.2; AT4G26330.
DR KEGG; ath:AT4G26330; -.
DR Araport; AT4G26330; -.
DR TAIR; locus:2136824; AT4G26330.
DR eggNOG; ENOG502QVIY; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; Q9STQ2; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:Q9STQ2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STQ2; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IMP:TAIR.
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; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PTHR10795; 1.
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..21
FT /evidence="ECO:0000255"
FT PROPEP 22..109
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435222"
FT CHAIN 110..?
FT /note="Subtilisin-like protease SBT3.18"
FT /id="PRO_0000435223"
FT PROPEP ?..779
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435224"
FT DOMAIN 30..109
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 113..621
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 553
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 779 AA; 85197 MW; EDF4FA9FF98EDA24 CRC64;
MYFWVMFFTL MIKVKLYITN GDIFQNRPTV YVVYLGANRL KNAALASSHH LHLLSKVFTS
KDDAEQSMLY SYNNGFLGFS AKLNSTQAAS LAKLNQVITV FKSKSLKLHT TRSWDFLGLA
VDNARRTPPP QLAYGSDIVV GIFDTGIWPE SESFRETPEA KPIPSSWNGK CVGGEDFDPS
VHCNRKLIGA RFYLRGFEET YGTIDFTRDP EYRSPRDYLG HGTHTASTAV GSVVRNVSGF
FGLGRGTARG GAPLARLAVF KTCWGKDLEG VCTEADILAA FDDAIHDGVH VISASFGYSP
PLSPFFESSA DIGAFHAAER GISVVFSTGN DGPDPGVVQN VAPWAVSVAA STVDRSFPTR
IVIDGSFTLT GQSLISQEIT GTLALATTYF NGGVCKWENW MKKLANETII LCFSTLGPVQ
FIEEAQAAAI RANALALIFA ASPTRQLAEE VDMIPTVRVD ILHGTRIRNY LARSPTVPMV
KIGPSKTVIG ETTAPSVAYF SSRGPSSLSP DILKPDITAP GIGILAAWPP RTPPTLLPGD
HRSIEWNFQS GTSMSCPHVA GVMALLQSAH PDWSPSAIRS AIMTTAYTRD TSYDLILSGG
SMKSTDPFDI GAGHINPLKA MDPGLVYNTR TDDYVLFMCN IGYTDQEIKS MVLHPEPSTT
CLPSHSYRTN ADFNYPSITI PSLRLTRTIK RTVSNVGPNK NTVYFVDIIR PVGVEVLIWP
RILVFSKCQQ EHSYYVTFKP TEIFSGRYVF GEIMWTNGLH RVRSPVVVFL SNAGFLASS
