SBT36_ARATH
ID SBT36_ARATH Reviewed; 778 AA.
AC Q8L7I2; A8MS13; F4JMC8; Q0WVJ9; Q9T0B5; Q9ZSB3;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Subtilisin-like protease SBT3.6 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 6 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.6 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.6 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At4g10550 {ECO:0000312|Araport:AT4G10550};
GN ORFNames=F3H7.3 {ECO:0000312|EMBL:AAD03431.1},
GN T4F9.10 {ECO:0000312|EMBL:CAB40021.1};
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|EMBL:AAM91616.1};
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 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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=3;
CC Name=1;
CC IsoId=Q8L7I2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L7I2-2; Sequence=VSP_058028;
CC Name=3;
CC IsoId=Q8L7I2-3; Sequence=VSP_058029;
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD03431.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB40021.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78178.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF118222; AAD03431.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL049523; CAB40021.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161517; CAB78178.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82896.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82897.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82898.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66371.1; -; Genomic_DNA.
DR EMBL; AY133682; AAM91616.1; -; mRNA.
DR EMBL; AK226748; BAE98849.1; -; mRNA.
DR PIR; T04190; T04190.
DR RefSeq; NP_001078370.1; NM_001084901.3. [Q8L7I2-2]
DR RefSeq; NP_001190697.1; NM_001203768.1. [Q8L7I2-3]
DR RefSeq; NP_001328268.1; NM_001340675.1. [Q8L7I2-2]
DR RefSeq; NP_567362.1; NM_117123.3. [Q8L7I2-1]
DR AlphaFoldDB; Q8L7I2; -.
DR SMR; Q8L7I2; -.
DR STRING; 3702.AT4G10550.3; -.
DR MEROPS; S08.A43; -.
DR PaxDb; Q8L7I2; -.
DR PRIDE; Q8L7I2; -.
DR ProteomicsDB; 232846; -. [Q8L7I2-1]
DR EnsemblPlants; AT4G10550.1; AT4G10550.1; AT4G10550. [Q8L7I2-1]
DR EnsemblPlants; AT4G10550.2; AT4G10550.2; AT4G10550. [Q8L7I2-2]
DR EnsemblPlants; AT4G10550.3; AT4G10550.3; AT4G10550. [Q8L7I2-3]
DR EnsemblPlants; AT4G10550.4; AT4G10550.4; AT4G10550. [Q8L7I2-2]
DR GeneID; 826647; -.
DR Gramene; AT4G10550.1; AT4G10550.1; AT4G10550. [Q8L7I2-1]
DR Gramene; AT4G10550.2; AT4G10550.2; AT4G10550. [Q8L7I2-2]
DR Gramene; AT4G10550.3; AT4G10550.3; AT4G10550. [Q8L7I2-3]
DR Gramene; AT4G10550.4; AT4G10550.4; AT4G10550. [Q8L7I2-2]
DR KEGG; ath:AT4G10550; -.
DR Araport; AT4G10550; -.
DR TAIR; locus:2139182; AT4G10550.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q8L7I2; -.
DR PRO; PR:Q8L7I2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7I2; 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; 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 2: Evidence at transcript level;
KW Alternative splicing; Autocatalytic cleavage; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..113
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435195"
FT CHAIN 114..?
FT /note="Subtilisin-like protease SBT3.6"
FT /id="PRO_5004309532"
FT PROPEP ?..778
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435196"
FT DOMAIN 34..113
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 117..625
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 388..483
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 556
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 2)"
FT /id="VSP_058028"
FT VAR_SEQ 1..21
FT /note="MMNYRTSIYVVLSLVIFLNVQ -> MKLRLQNPISPALKFTGHLPPSKALKS
FT SKETIFLTKE (in isoform 3)"
FT /id="VSP_058029"
FT CONFLICT 108
FT /note="S -> G (in Ref. 4; BAE98849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 83654 MW; A142BE537FA6D644 CRC64;
MMNYRTSIYV VLSLVIFLNV QRSFVAESSA KRKVHIVYLG EKQHDDPEFV TESHHRMLWS
LLGSKEDAND SMVYSYRHGF SGFAAKLTES QAKKIADLPD VVHVIPDSFY KLATTRTWDY
LGLSAANPKS LLHETNMGEQ IIIGVIDTGV WPESEVFNDS GFGPVPSHWK GGCETGENFN
SSNCNKKLIG AKYFINGFLA ENESFNSTNS LDFISPRDLD GHGTHVSTIA GGSFVPNISY
KGLAGGTVRG GAPRAHIAMY KACWYLDDDD TTTCSSADIL KAMDEAMHDG VDVLSISLGS
SVPLYGETDI RDGITTGAFH AVLKGITVVC SGGNSGPDSL TVTNTAPWII TVAATTLDRS
FATPLTLGNN KVILGQAMYT GPGLGFTSLV YPENPGNSNE SFSGTCEELL FNSNRTMEGK
VVLCFTTSPY GGAVLSAARY VKRAGGLGVI IARHPGYAIQ PCLDDFPCVA VDWELGTDIL
LYTRSSGSPV VKIQPSKTLV GQPVGTKVAT FSSRGPNSIA PAILKPDIAA PGVSILAATT
NTTFSDQGFI MLSGTSMAAP AISGVAALLK ALHRDWSPAA IRSAIVTTAW KTDPFGEQIF
AEGSPPKLAD PFDYGGGLVN PEKSANPGLV YDMGLEDYVL YMCSVGYNET SISQLIGKTT
VCSNPKPSVL DFNLPSITIP NLKDEVTITR TVTNVGPLNS VYRVTVEPPL GFQVTVTPET
LVFNSTTKKV YFKVKVSTTH KTNTGYYFGS LTWSDSLHNV TIPLSVRTQI LQNYYDEN
