SBT12_ARATH
ID SBT12_ARATH Reviewed; 775 AA.
AC O64495;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Subtilisin-like protease SBT1.2 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Cucumisin-like serine protease SDD1;
DE AltName: Full=Protein STOMATAL DENSITY AND DISTRIBUTION 1;
DE AltName: Full=Subtilase subfamily 1 member 2 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT1.2 {ECO:0000303|PubMed:16193095};
DE AltName: Full=Subtilisin-like protease SDD1 {ECO:0000303|PubMed:10809670};
DE Flags: Precursor;
GN Name=SBT1.2 {ECO:0000303|PubMed:16193095};
GN Synonyms=SDD1 {ECO:0000303|PubMed:10809670};
GN OrderedLocusNames=At1g04110 {ECO:0000312|Araport:AT1G04110};
GN ORFNames=F20D22.12 {ECO:0000303|PubMed:11130712};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=10809670; DOI=10.1101/gad.14.9.1119;
RA Berger D., Altmann T.;
RT "A subtilisin-like serine protease involved in the regulation of stomatal
RT density and distribution in Arabidopsis thaliana.";
RL Genes Dev. 14:1119-1131(2000).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND PROBABLE SUBCELLULAR LOCATION.
RC STRAIN=cv. C24;
RX PubMed=12119372; DOI=10.1105/tpc.001016;
RA Von Groll U., Berger D., Altmann T.;
RT "The subtilisin-like serine protease SDD1 mediates cell-to-cell signaling
RT during Arabidopsis stomatal development.";
RL Plant Cell 14:1527-1539(2002).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=12554730; DOI=10.1093/jxb/erg087;
RA Schlueter U., Muschak M., Berger D., Altmann T.;
RT "Photosynthetic performance of an Arabidopsis mutant with elevated stomatal
RT density (sdd1-1) under different light regimes.";
RL J. Exp. Bot. 54:867-874(2003).
RN [6]
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 [7]
RP REVIEW.
RX PubMed=18266617; DOI=10.1111/j.1469-8137.2007.02351.x;
RA Casson S., Gray J.E.;
RT "Influence of environmental factors on stomatal development.";
RL New Phytol. 178:9-23(2008).
RN [8]
RP REVIEW.
RX PubMed=19565615; DOI=10.1002/bies.200800231;
RA Serna L.;
RT "Cell fate transitions during stomatal development.";
RL Bioessays 31:865-873(2009).
RN [9]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=20056678; DOI=10.1242/dev.040931;
RA Abrash E.B., Bergmann D.C.;
RT "Regional specification of stomatal production by the putative ligand
RT CHALLAH.";
RL Development 137:447-455(2010).
RN [10]
RP FUNCTION, AND INDUCTION BY GTL1.
RC STRAIN=cv. Columbia;
RX PubMed=21169508; DOI=10.1105/tpc.110.078691;
RA Yoo C.Y., Pence H.E., Jin J.B., Miura K., Gosney M.J., Hasegawa P.M.,
RA Mickelbart M.V.;
RT "The Arabidopsis GTL1 transcription factor regulates water use efficiency
RT and drought tolerance by modulating stomatal density via transrepression of
RT SDD1.";
RL Plant Cell 22:4128-4141(2010).
CC -!- FUNCTION: Serine protease involved in the negative regulation of
CC stomatal density and distribution. Not active on EPFL6 (AC Q1PEY6)
CC (PubMed:20056678). Positive regulator of water use efficiency (WUE).
CC {ECO:0000269|PubMed:10809670, ECO:0000269|PubMed:12119372,
CC ECO:0000269|PubMed:20056678, ECO:0000269|PubMed:21169508}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000305}. Cell membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and cotyledons
CC (especially in epidermal cells), and, to a lower extent, in floral
CC buds, stems, and siliques. Strongly expressed in stomatal precursor
CC cells (meristemoids and guard mother cells).
CC {ECO:0000269|PubMed:10809670, ECO:0000269|PubMed:12119372}.
CC -!- INDUCTION: Negatively feedback controlled by components of an SDD1-
CC dependent signaling pathway. Repressed by GTL1.
CC {ECO:0000269|PubMed:12119372, ECO:0000269|PubMed:21169508}.
CC -!- DISRUPTION PHENOTYPE: Increased stomatal density and formation of
CC clustered stomata by enhanced stomatal development initiation and
CC extension of stomatal cell lineages. No major impact on photosynthesis,
CC except 30% higher CO2 assimilation rates in low-light-adapted plants
CC exposed to high light intensities. {ECO:0000269|PubMed:10809670,
CC ECO:0000269|PubMed:12554730}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AC002411; AAC16749.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27657.1; -; Genomic_DNA.
DR PIR; T00962; T00962.
DR RefSeq; NP_563701.1; NM_100292.2.
DR AlphaFoldDB; O64495; -.
DR SMR; O64495; -.
DR STRING; 3702.AT1G04110.1; -.
DR MEROPS; S08.084; -.
DR PaxDb; O64495; -.
DR PRIDE; O64495; -.
DR ProteomicsDB; 226651; -.
DR EnsemblPlants; AT1G04110.1; AT1G04110.1; AT1G04110.
DR GeneID; 839287; -.
DR Gramene; AT1G04110.1; AT1G04110.1; AT1G04110.
DR KEGG; ath:AT1G04110; -.
DR Araport; AT1G04110; -.
DR TAIR; locus:2020245; AT1G04110.
DR eggNOG; ENOG502QV3N; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; O64495; -.
DR OMA; VQLHPQG; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; O64495; -.
DR PRO; PR:O64495; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64495; baseline and differential.
DR Genevisible; O64495; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:TAIR.
DR GO; GO:0010103; P:stomatal complex morphogenesis; 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; IPR003137; PA_domain.
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; PF02225; PA; 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 Apoplast; Cell membrane; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..775
FT /note="Subtilisin-like protease SBT1.2"
FT /id="PRO_0000405797"
FT DOMAIN 27..111
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 116..618
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 388..470
FT /note="PA"
FT ACT_SITE 146
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 552
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 775 AA; 83776 MW; 7740B20397C7C211 CRC64;
MEPKPFFLCI IFLLFCSSSS EILQKQTYIV QLHPNSETAK TFASKFDWHL SFLQEAVLGV
EEEEEEPSSR LLYSYGSAIE GFAAQLTESE AEILRYSPEV VAVRPDHVLQ VQTTYSYKFL
GLDGFGNSGV WSKSRFGQGT IIGVLDTGVW PESPSFDDTG MPSIPRKWKG ICQEGESFSS
SSCNRKLIGA RFFIRGHRVA NSPEESPNMP REYISARDST GHGTHTASTV GGSSVSMANV
LGNGAGVARG MAPGAHIAVY KVCWFNGCYS SDILAAIDVA IQDKVDVLSL SLGGFPIPLY
DDTIAIGTFR AMERGISVIC AAGNNGPIES SVANTAPWVS TIGAGTLDRR FPAVVRLANG
KLLYGESLYP GKGIKNAGRE VEVIYVTGGD KGSEFCLRGS LPREEIRGKM VICDRGVNGR
SEKGEAVKEA GGVAMILANT EINQEEDSID VHLLPATLIG YTESVLLKAY VNATVKPKAR
IIFGGTVIGR SRAPEVAQFS ARGPSLANPS ILKPDMIAPG VNIIAAWPQN LGPTGLPYDS
RRVNFTVMSG TSMSCPHVSG ITALIRSAYP NWSPAAIKSA LMTTADLYDR QGKAIKDGNK
PAGVFAIGAG HVNPQKAINP GLVYNIQPVD YITYLCTLGF TRSDILAITH KNVSCNGILR
KNPGFSLNYP SIAVIFKRGK TTEMITRRVT NVGSPNSIYS VNVKAPEGIK VIVNPKRLVF
KHVDQTLSYR VWFVLKKKNR GGKVASFAQG QLTWVNSHNL MQRVRSPISV TLKTN
