SBT17_ARATH
ID SBT17_ARATH Reviewed; 757 AA.
AC O65351; P80854; Q39007; Q8RWQ7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Subtilisin-like protease SBT1.7 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Cucumisin-like serine protease;
DE AltName: Full=Subtilase subfamily 1 member 7 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT1.7 {ECO:0000303|PubMed:16193095};
DE AltName: Full=Subtilisin-like serine protease 1 {ECO:0000303|PubMed:12702015};
DE Short=At-SLP1 {ECO:0000303|PubMed:12702015};
DE Flags: Precursor;
GN Name=SBT1.7 {ECO:0000303|PubMed:16193095};
GN Synonyms=ARA12, ASP48 {ECO:0000303|PubMed:11055401},
GN SLP1 {ECO:0000303|PubMed:12702015}; OrderedLocusNames=At5g67360;
GN ORFNames=K8K14.8;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11055401; DOI=10.1271/bbb.64.1947;
RA Yamagata H., Uesugi M., Saka K., Iwasaki T., Aizono Y.;
RT "Molecular cloning and characterization of a cDNA and a gene for
RT subtilisin-like serine proteases from rice (Oryza sativa L.) and
RT Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 64:1947-1957(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-757, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=7647567; DOI=10.2307/3870179;
RA Ribeiro A., Akkermans A.D.L., van Kammen A., Bisseling T., Pawlowski K.;
RT "A nodule-specific gene encoding a subtilisin-like protease is expressed in
RT early stages of actinorhizal nodule development.";
RL Plant Cell 7:785-794(1995).
RN [6]
RP PROTEIN SEQUENCE OF 107-126, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
RA Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
RA Slabas A.R.;
RT "Differential extraction and protein sequencing reveals major differences
RT in patterns of primary cell wall proteins from plants.";
RL J. Biol. Chem. 272:15841-15848(1997).
RN [7]
RP PROTEIN SEQUENCE OF 107-116, FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MASS SPECTROMETRY.
RX PubMed=12413398; DOI=10.1042/bj20021125;
RA Hamilton J.M.U., Simpson D.J., Hyman S.C., Ndimba B.K., Slabas A.R.;
RT "Ara12 subtilisin-like protease from Arabidopsis thaliana: purification,
RT substrate specificity and tissue localization.";
RL Biochem. J. 370:57-67(2003).
RN [8]
RP INDUCTION BY METHYL JASMONATE.
RX PubMed=12702015; DOI=10.1034/j.1399-3054.2003.00087.x;
RA Golldack D., Vera P., Dietz K.J.;
RT "Expression of subtilisin-like serine proteases in Arabidopsis thaliana is
RT cell-specific and responds to jasmonic acid and heavy metals with
RT developmental differences.";
RL Physiol. Plantarum 118:64-73(2003).
RN [9]
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 [10]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18266922; DOI=10.1111/j.1365-313x.2008.03437.x;
RA Rautengarten C., Usadel B., Neumetzler L., Hartmann J., Bussis D.,
RA Altmann T.;
RT "A subtilisin-like serine protease essential for mucilage release from
RT Arabidopsis seed coats.";
RL Plant J. 54:466-480(2008).
CC -!- FUNCTION: Serine protease. Has a substrate preference for the
CC hydrophobic residues Phe and Ala and the basic residue Asp in the P1
CC position, and for Asp, Leu or Ala in the P1' position
CC (PubMed:12413398). Essential for mucilage release from seed coats.
CC Triggers the accumulation and/or activation of cell wall modifying
CC enzymes necessary either for the loosening of the outer primary cell
CC wall, or to facilitate swelling of the mucilage (PubMed:18266922).
CC {ECO:0000269|PubMed:12413398, ECO:0000269|PubMed:18266922}.
CC -!- ACTIVITY REGULATION: Activated by calcium. Inhibited by the serine
CC protease inhibitors 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF),
CC PMSF, di-isopropyl phosphofluoridate (DFP) and soybean trypsin
CC inhibitor (SBTI). Not inhibited by benzamidine or iodoacetamide.
CC Leupeptin and pepstatin A have a minor inhibitory action.
CC {ECO:0000269|PubMed:12413398}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:12413398};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius. Thermostable.
CC {ECO:0000269|PubMed:12413398};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:12413398,
CC ECO:0000269|PubMed:9188482}. Note=Intracellular spaces and cell wall.
CC -!- TISSUE SPECIFICITY: Expressed in immature siliques and at lower levels
CC in stems and flowers (PubMed:11055401, PubMed:7647567,
CC PubMed:12413398). Widely expressed at low levels (PubMed:18266922).
CC {ECO:0000269|PubMed:11055401, ECO:0000269|PubMed:12413398,
CC ECO:0000269|PubMed:18266922, ECO:0000269|PubMed:7647567}.
CC -!- DEVELOPMENTAL STAGE: Highest levels of expression detected during
CC silique development (PubMed:7647567). Hihghly expressed in the seed
CC coat during seed development (PubMed:18266922).
CC {ECO:0000269|PubMed:18266922, ECO:0000269|PubMed:7647567}.
CC -!- INDUCTION: By methyl jasmonate. {ECO:0000269|PubMed:12702015}.
CC -!- MASS SPECTROMETRY: Mass=76102.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12413398};
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seeds are defective in mucilage extrusion.
CC {ECO:0000269|PubMed:18266922}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AF065639; AAC18851.1; -; Genomic_DNA.
DR EMBL; AB007645; BAB09021.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98332.1; -; Genomic_DNA.
DR EMBL; AF360285; AAK25995.1; -; mRNA.
DR EMBL; AY091773; AAM10321.1; -; mRNA.
DR EMBL; AY142612; AAN13181.1; -; mRNA.
DR EMBL; BT001082; AAN46863.1; -; mRNA.
DR EMBL; X85974; CAA59963.1; -; mRNA.
DR PIR; JC7519; JC7519.
DR PIR; S52770; S52770.
DR RefSeq; NP_569048.1; NM_126136.3.
DR AlphaFoldDB; O65351; -.
DR SMR; O65351; -.
DR BioGRID; 22113; 2.
DR STRING; 3702.AT5G67360.1; -.
DR MEROPS; S08.112; -.
DR PaxDb; O65351; -.
DR PRIDE; O65351; -.
DR ProteomicsDB; 232882; -.
DR EnsemblPlants; AT5G67360.1; AT5G67360.1; AT5G67360.
DR GeneID; 836871; -.
DR Gramene; AT5G67360.1; AT5G67360.1; AT5G67360.
DR KEGG; ath:AT5G67360; -.
DR Araport; AT5G67360; -.
DR TAIR; locus:2158187; AT5G67360.
DR eggNOG; ENOG502QUSV; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; O65351; -.
DR OMA; YACAENK; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; O65351; -.
DR PRO; PR:O65351; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65351; baseline and differential.
DR Genevisible; O65351; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0080001; P:mucilage extrusion from seed coat; IMP:TAIR.
DR GO; GO:0048359; P:mucilage metabolic process involved in seed coat development; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0010214; P:seed coat development; 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 1: Evidence at protein level;
KW Calcium; Cell wall; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..106
FT /evidence="ECO:0000255, ECO:0000269|PubMed:12413398,
FT ECO:0000269|PubMed:9188482"
FT /id="PRO_0000042846"
FT CHAIN 107..757
FT /note="Subtilisin-like protease SBT1.7"
FT /evidence="ECO:0000269|PubMed:12413398"
FT /id="PRO_0000042847"
FT DOMAIN 31..106
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 102..610
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 196..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /note="Charge relay system"
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 542
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 41
FT /note="M -> T (in Ref. 5; CAA59963)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..247
FT /note="APRARV -> LHAL (in Ref. 5; CAA59963)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="W -> C (in Ref. 4; AAM10321/AAN46863)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="V -> A (in Ref. 5; CAA59963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 79415 MW; E7F68FCAD16700AB CRC64;
MSSSFLSSTA FFLLLCLGFC HVSSSSSDQG TYIVHMAKSQ MPSSFDLHSN WYDSSLRSIS
DSAELLYTYE NAIHGFSTRL TQEEADSLMT QPGVISVLPE HRYELHTTRT PLFLGLDEHT
ADLFPEAGSY SDVVVGVLDT GVWPESKSYS DEGFGPIPSS WKGGCEAGTN FTASLCNRKL
IGARFFARGY ESTMGPIDES KESRSPRDDD GHGTHTSSTA AGSVVEGASL LGYASGTARG
MAPRARVAVY KVCWLGGCFS SDILAAIDKA IADNVNVLSM SLGGGMSDYY RDGVAIGAFA
AMERGILVSC SAGNAGPSSS SLSNVAPWIT TVGAGTLDRD FPALAILGNG KNFTGVSLFK
GEALPDKLLP FIYAGNASNA TNGNLCMTGT LIPEKVKGKI VMCDRGINAR VQKGDVVKAA
GGVGMILANT AANGEELVAD AHLLPATTVG EKAGDIIRHY VTTDPNPTAS ISILGTVVGV
KPSPVVAAFS SRGPNSITPN ILKPDLIAPG VNILAAWTGA AGPTGLASDS RRVEFNIISG
TSMSCPHVSG LAALLKSVHP EWSPAAIRSA LMTTAYKTYK DGKPLLDIAT GKPSTPFDHG
AGHVSPTTAT NPGLIYDLTT EDYLGFLCAL NYTSPQIRSV SRRNYTCDPS KSYSVADLNY
PSFAVNVDGV GAYKYTRTVT SVGGAGTYSV KVTSETTGVK ISVEPAVLNF KEANEKKSYT
VTFTVDSSKP SGSNSFGSIE WSDGKHVVGS PVAISWT
