(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 140.
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};
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   SMR; Q9STQ2; -.
DR   STRING; 3702.AT4G26330.1; -.
DR   MEROPS; S08.A40; -.
DR   PaxDb; 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; ENOG410IJ6M; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   HOGENOM; HOG000238262; -.
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   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;
DR   PRODOM; Q9STQ2.
DR   SWISS-2DPAGE; Q9STQ2.
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
//

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