SBT26_ARATH
ID SBT26_ARATH Reviewed; 816 AA.
AC Q9SZV5;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Subtilisin-like protease SBT2.6 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 2 member 6 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT2.6 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT2.6 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At4g30020 {ECO:0000312|Araport:AT4G30020};
GN ORFNames=F6G3.50 {ECO:0000312|EMBL:CAB43837.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
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 -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AL078464; CAB43837.1; -; Genomic_DNA.
DR EMBL; AL161576; CAB80995.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85709.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66536.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66537.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66538.1; -; Genomic_DNA.
DR EMBL; AY139780; AAM98098.1; -; mRNA.
DR EMBL; BT005822; AAO64757.1; -; mRNA.
DR EMBL; AK226227; BAE98391.1; -; mRNA.
DR PIR; T08978; T08978.
DR RefSeq; NP_001328423.1; NM_001341988.1.
DR RefSeq; NP_001328424.1; NM_001341989.1.
DR RefSeq; NP_001328425.1; NM_001341990.1.
DR RefSeq; NP_567839.1; NM_119148.4.
DR AlphaFoldDB; Q9SZV5; -.
DR SMR; Q9SZV5; -.
DR STRING; 3702.AT4G30020.1; -.
DR MEROPS; S08.A02; -.
DR PaxDb; Q9SZV5; -.
DR PRIDE; Q9SZV5; -.
DR ProteomicsDB; 232904; -.
DR EnsemblPlants; AT4G30020.1; AT4G30020.1; AT4G30020.
DR EnsemblPlants; AT4G30020.2; AT4G30020.2; AT4G30020.
DR EnsemblPlants; AT4G30020.3; AT4G30020.3; AT4G30020.
DR EnsemblPlants; AT4G30020.4; AT4G30020.4; AT4G30020.
DR GeneID; 829125; -.
DR Gramene; AT4G30020.1; AT4G30020.1; AT4G30020.
DR Gramene; AT4G30020.2; AT4G30020.2; AT4G30020.
DR Gramene; AT4G30020.3; AT4G30020.3; AT4G30020.
DR Gramene; AT4G30020.4; AT4G30020.4; AT4G30020.
DR KEGG; ath:AT4G30020; -.
DR Araport; AT4G30020; -.
DR TAIR; locus:2126485; AT4G30020.
DR eggNOG; ENOG502QS8I; Eukaryota.
DR HOGENOM; CLU_000625_3_1_1; -.
DR InParanoid; Q9SZV5; -.
DR OMA; QPCDLNI; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9SZV5; -.
DR PRO; PR:Q9SZV5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZV5; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; IPR010435; Fn3_5.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
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 PANTHER; PTHR10795; PTHR10795; 1.
DR Pfam; PF06280; fn3_5; 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; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..126
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q9MAP7"
FT /id="PRO_0000435186"
FT CHAIN 127..?
FT /note="Subtilisin-like protease SBT2.6"
FT /id="PRO_5004337366"
FT PROPEP ?..816
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435187"
FT DOMAIN 22..124
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 120..672
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 418..492
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 597
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 816 AA; 87505 MW; 6C77ECBC1F5D9B30 CRC64;
MDIGCKVLVF FTCFLTVTAE IYIVTMEGEP IISYKGGDNG FEATAVESDE KIDTTSELVT
SYARHLERKH DMLLGMLFVE GSYKKLYSYK HLINGFAAHV SPDQAEMLRR APGVKSVDRD
WKVRKLTTHT PQFLGLPTDV WPTGGGYDRA GEDIVIGFID SGIFPHHPSF ASHHTTVPYG
PHPSYKGKCE EDPHTKISFC NGKIIGAQHF AEAAKAAGAF NPDIDFASPM DGDGHGSHTA
AIAAGNNGIP VRMHGYEFGK ASGMAPRARI AVYKALYRLF GGFVADVVAA IDQAVHDGVD
ILSLSVGPNS PPATTKTTFL NPFDATLLGA VKAGVFVAQA AGNGGPFPKT LVSYSPWITT
VAAAIDDRRY KNHLTLGNGK MLAGIGLSPS TRPHRSYKMV SANDVLLGSS GMKYNPSDCQ
KPEVLNKKLV EGNILLCGYS FNFVAGSASI KKVAETAKHL GAAGFVLVVE NVSPGTKFDP
VPSCIPGILI TDVSKSMDLI DYYNVTTSRD WMGRVKDFKA EGSIGDGLEP ILHKSAPEVA
LFSARGPNTK DFSFQDADLL KPDILAPGSL IWSAWSANGT DEANYIGEGF ALISGTSMAA
PHIAGIAALV KQKHPQWSPA AIKSALMTTS TVIDRAGRPL QAQQYSETET VTLVKATPFD
YGSGHVNPSA ALDPGLIFDA GYEDYIGFLC TTPGIDAHEI KNFTNTPCNF KMVHPSNFNT
PSIAISHLVR TQTVTRRVTN VAEEEETYTI TSRMEPAIAI EVSPPAMTVR AGASRTFSVT
LTVRSVTGAY SFGQVTLKGS RGHKVTLPVV AMGQRR
