SBT61_ARATH
ID SBT61_ARATH Reviewed; 1038 AA.
AC Q0WUG6; Q8L7B7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Subtilisin-like protease SBT6.1 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Site-1 protease {ECO:0000303|PubMed:17662035};
DE Short=AtS1P {ECO:0000303|PubMed:17662035};
DE AltName: Full=Subtilase subfamily 6 member 1 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT6.1 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT6.1 {ECO:0000303|PubMed:16193095}; Synonyms=S1P {ECO:0000305};
GN OrderedLocusNames=At5g19660 {ECO:0000312|Araport:AT5G19660};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17662035; DOI=10.1111/j.1365-313x.2007.03195.x;
RA Liu J.X., Srivastava R., Che P., Howell S.H.;
RT "Salt stress responses in Arabidopsis utilize a signal transduction pathway
RT related to endoplasmic reticulum stress signaling.";
RL Plant J. 51:897-909(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH PME1 AND PME5.
RX PubMed=19144003; DOI=10.1111/j.1365-313x.2009.03784.x;
RA Wolf S., Rausch T., Greiner S.;
RT "The N-terminal pro region mediates retention of unprocessed type-I PME in
RT the Golgi apparatus.";
RL Plant J. 58:361-375(2009).
RN [8]
RP FUNCTION.
RX PubMed=19473327; DOI=10.1111/j.1365-313x.2009.03926.x;
RA Srivastava R., Liu J.-X., Guo H., Yin Y., Howell S.H.;
RT "Regulation and processing of a plant peptide hormone, AtRALF23, in
RT Arabidopsis.";
RL Plant J. 59:930-939(2009).
RN [9]
RP SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20876872; DOI=10.1126/scisignal.2001140;
RA Che P., Bussell J.D., Zhou W., Estavillo G.M., Pogson B.J., Smith S.M.;
RT "Signaling from the endoplasmic reticulum activates brassinosteroid
RT signaling and promotes acclimation to stress in Arabidopsis.";
RL Sci. Signal. 3:RA69-RA69(2010).
CC -!- FUNCTION: Serine protease that catalyzes the first step (site-1
CC cleavage) in the proteolytic activation of various factors, prior to
CC site-2 cleavage. Part of a regulated intramembrane proteolysis (RIP)
CC cascade. Cleaves BZIP17 and BZIP28 after the Arg-Arg-Ile-Leu (RRIL)
CC motif. May cleave BZIP49 after the RRIL motif. Targets the membrane-
CC associated BZIP17 factor, which functions as a stress sensor and
CC transducer in a signaling pathway that resembles an ER stress response.
CC Following salt stress, BZIP17 is cleaved by SBT6.1 (S1P) and S2P at the
CC C-terminus and the N-terminal bZIP component is translocated to the
CC nucleus, where it activates the expression of salt stress response
CC genes (PubMed:17662035). Cleaves the pectinesterases PME1 after the
CC Arg-Arg-Leu-Met (RRLM) and Arg-Arg-Leu-Leu (RRLL) motifs, and PME5
CC after the Arg-Arg-Leu-Leu (RRLL) and Arg-Lys-Leu-Met (RKLM) motifs.
CC This processing and C-terminus release occurs in the Golgi apparatus
CC and is required for cell wall targeting of pectinesterases. Thus,
CC SBT6.1 mediates the regulated release of mature pectinesterases from
CC the Golgi (PubMed:19144003). Cleaves the peptide growth factor RALF23
CC after the Arg-Arg-Ile-Leu (RRIL) motif. This processing is required for
CC RALF23 function in the negative regulation of brassinolide (BL)-
CC mediated signaling pathway (e.g. BL-induced hypocotyl elongation and
CC branching limitation) (PubMed:19473327). {ECO:0000269|PubMed:17662035,
CC ECO:0000269|PubMed:19144003, ECO:0000269|PubMed:19473327}.
CC -!- SUBUNIT: Interacts with PME1 and PME5. {ECO:0000269|PubMed:19144003}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:17662035, ECO:0000305|PubMed:20876872}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature of roots, cotyledons
CC and leaves. {ECO:0000269|PubMed:17662035, ECO:0000269|PubMed:20876872}.
CC -!- DISRUPTION PHENOTYPE: Short root (PubMed:20876872). Mutant plants have
CC increased sensitivity to salt-induced osmotic stress (PubMed:17662035).
CC {ECO:0000269|PubMed:17662035, ECO:0000269|PubMed:20876872}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AF296838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92735.1; -; Genomic_DNA.
DR EMBL; AY136354; AAM97020.1; -; mRNA.
DR EMBL; AK227193; BAE99232.1; -; mRNA.
DR RefSeq; NP_197467.1; NM_121971.3.
DR AlphaFoldDB; Q0WUG6; -.
DR SMR; Q0WUG6; -.
DR STRING; 3702.AT5G19660.1; -.
DR MEROPS; S08.063; -.
DR PaxDb; Q0WUG6; -.
DR PRIDE; Q0WUG6; -.
DR ProteomicsDB; 232794; -.
DR EnsemblPlants; AT5G19660.1; AT5G19660.1; AT5G19660.
DR GeneID; 832086; -.
DR Gramene; AT5G19660.1; AT5G19660.1; AT5G19660.
DR KEGG; ath:AT5G19660; -.
DR Araport; AT5G19660; -.
DR TAIR; locus:2183224; AT5G19660.
DR eggNOG; KOG4266; Eukaryota.
DR HOGENOM; CLU_004504_2_0_1; -.
DR InParanoid; Q0WUG6; -.
DR OMA; MKFANIW; -.
DR OrthoDB; 340650at2759; -.
DR PhylomeDB; Q0WUG6; -.
DR PRO; PR:Q0WUG6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WUG6; baseline and differential.
DR Genevisible; Q0WUG6; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004175; F:endopeptidase activity; IDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IMP:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IDA:TAIR.
DR CDD; cd07479; Peptidases_S8_SKI-1_like; 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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034185; Site-1_peptidase_cat_dom.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..181
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:17662035"
FT /id="PRO_0000431968"
FT CHAIN 182..1038
FT /note="Subtilisin-like protease SBT6.1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431969"
FT TOPO_DOM 182..1000
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:20876872"
FT TRANSMEM 1001..1021
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1022..1038
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20876872"
FT DOMAIN 175..473
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 409
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 902
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 429
FT /note="A -> S (in Ref. 3; AAM97020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1038 AA; 116151 MW; 1446BDD8E36366D4 CRC64;
MKVLGEASSY PYRSCIIVVF LSVSLFWLRP STYHPQQQNL NPENVTRLES ENETKTNYII
RFKQYKPAKD HRIYLESKVR SGGWGWIERI NPATKYPTDF GVLWIEESGK EAVVGEIERL
EMVKDVNVEF KYQRVLLGGS FPDGKKRPGK IFTSMSFEEG TESSPMADTS NTTLNWSRHL
LAQKTQVTSM FGADHLWKKG YTGAKVKMAI FDTGIRADHP HFRKIKERTN WTNEDTLNDN
LGHGTFVAGV IAGRNPECLG FASDTEIYAF RVFTDAQVSY TSWFLDAFNY AIATDMDVLN
LSIGGPDYLD LPFVEKVWEI TASNIIMVSA IGNDGPLYGT LNNPADQSDV IGVGGIDNDD
HIASFSSRGM STWELPHGYG RVKPDVVAYG RDIMGSKIST GCKSLSGTSV ASPVVAGIVC
LLVSVIPEAR RKDLLNPASM KQALVEGAAK LSGPNMYEQG AGRVDLLESY EILKSYHPRA
SIFPSILDYN DCPYSWPFCR QPLYAGAMPI IFNTTILNGM GVIGYIESPP TWHPANEEGN
LLSIHFKYPD VIWPWTGYLA LHMQIKEEGA QFTGEIEGNV TVKVYSPPAS GESGPRRSTC
SLQLKLKVIP TPPRAKRILW DQFHSIKYPP GYIPRDSLDV RNDILDWHGD HLHTNFHIMY
NMLRDAGYYI ETLGSPLTCF DAQQYGTLLM VDLEDDYFPE EIEKLRDDVI NTGLGLVVFA
EWYNVDTMVK MRFFDDNTRS WWTPVTGGAN IPALNNLLAS FGIAFGDKIL NGDFSIDGEQ
SRYASGTNIV RFPAGGFLHT FPLLDSSESG ATQNLLLTEA SKEDPAVLGL LEIGEGRVGV
YGDSNCLDSS HMVTNCYWLL KKMLDFSSSN IKDPVLFSKF AKRYSPVIID EKQLPSRRTD
VNFSTYSSVI GKELICESDS RFEVWGTKGY NLHVRGRNRR LPGYHGIDLG RGLNFTVESK
RPTRWRSAKE GGELSSSRSK SLGGLFNRDE IDMPFLVPTR WIVLAGVVAS GVLVLLSIWR
IRQKRGRRRR ASGSNRLA
