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Subtilisin-like protease SBT1.7 (EC 3.4.21.-) (Cucumisin-like serine protease) (Subtilase subfamily 1 member 7) (AtSBT1.7) (Subtilisin-like serine protease 1) (At-SLP1)

 SBT17_ARATH             Reviewed;         757 AA.
O65351; P80854; Q39007; Q8RWQ7;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
25-OCT-2017, entry version 128.
RecName: Full=Subtilisin-like protease SBT1.7 {ECO:0000303|PubMed:16193095};
EC=3.4.21.- {ECO:0000305};
AltName: Full=Cucumisin-like serine protease;
AltName: Full=Subtilase subfamily 1 member 7 {ECO:0000303|PubMed:16193095};
Short=AtSBT1.7 {ECO:0000303|PubMed:16193095};
AltName: Full=Subtilisin-like serine protease 1 {ECO:0000303|PubMed:12702015};
Short=At-SLP1 {ECO:0000303|PubMed:12702015};
Flags: Precursor;
Name=SBT1.7 {ECO:0000303|PubMed:16193095};
Synonyms=ARA12, ASP48 {ECO:0000303|PubMed:11055401},
SLP1 {ECO:0000303|PubMed:12702015}; OrderedLocusNames=At5g67360;
ORFNames=K8K14.8;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=11055401; DOI=10.1271/bbb.64.1947;
Yamagata H., Uesugi M., Saka K., Iwasaki T., Aizono Y.;
"Molecular cloning and characterization of a cDNA and a gene for
subtilisin-like serine proteases from rice (Oryza sativa L.) and
Arabidopsis thaliana.";
Biosci. Biotechnol. Biochem. 64:1947-1957(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9501997; DOI=10.1093/dnares/4.6.401;
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. III.
Sequence features of the regions of 1,191,918 bp covered by seventeen
physically assigned P1 clones.";
DNA Res. 4:401-414(1997).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-757, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia;
PubMed=7647567; DOI=10.1105/tpc.7.6.785;
Ribeiro A., Akkermans A.D.L., van Kammen A., Bisseling T.,
Pawlowski K.;
"A nodule-specific gene encoding a subtilisin-like protease is
expressed in early stages of actinorhizal nodule development.";
Plant Cell 7:785-794(1995).
[6]
PROTEIN SEQUENCE OF 107-126, AND SUBCELLULAR LOCATION.
STRAIN=cv. Landsberg erecta;
PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
Slabas A.R.;
"Differential extraction and protein sequencing reveals major
differences in patterns of primary cell wall proteins from plants.";
J. Biol. Chem. 272:15841-15848(1997).
[7]
PROTEIN SEQUENCE OF 107-116, FUNCTION, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MASS SPECTROMETRY.
PubMed=12413398; DOI=10.1042/BJ20021125;
Hamilton J.M.U., Simpson D.J., Hyman S.C., Ndimba B.K., Slabas A.R.;
"Ara12 subtilisin-like protease from Arabidopsis thaliana:
purification, substrate specificity and tissue localization.";
Biochem. J. 370:57-67(2003).
[8]
INDUCTION BY METHYL JASMONATE.
PubMed=12702015; DOI=10.1034/j.1399-3054.2003.00087.x;
Golldack D., Vera P., Dietz K.J.;
"Expression of subtilisin-like serine proteases in Arabidopsis
thaliana is cell-specific and responds to jasmonic acid and heavy
metals with developmental differences.";
Physiol. Plantarum 118:64-73(2003).
[9]
GENE FAMILY, AND NOMENCLATURE.
PubMed=16193095; DOI=10.1371/journal.pcbi.0010040;
Rautengarten C., Steinhauser D., Bussis D., Stintzi A., Schaller A.,
Kopka J., Altmann T.;
"Inferring hypotheses on functional relationships of genes: Analysis
of the Arabidopsis thaliana subtilase gene family.";
PLoS Comput. Biol. 1:E40-E40(2005).
[10]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=18266922; DOI=10.1111/j.1365-313X.2008.03437.x;
Rautengarten C., Usadel B., Neumetzler L., Hartmann J., Bussis D.,
Altmann T.;
"A subtilisin-like serine protease essential for mucilage release from
Arabidopsis seed coats.";
Plant J. 54:466-480(2008).
-!- FUNCTION: Serine protease. Has a substrate preference for the
hydrophobic residues Phe and Ala and the basic residue Asp in the
P1 position, and for Asp, Leu or Ala in the P1' position
(PubMed:12413398). Essential for mucilage release from seed coats.
Triggers the accumulation and/or activation of cell wall modifying
enzymes necessary either for the loosening of the outer primary
cell wall, or to facilitate swelling of the mucilage
(PubMed:18266922). {ECO:0000269|PubMed:12413398,
ECO:0000269|PubMed:18266922}.
-!- ENZYME REGULATION: Activated by calcium. Inhibited by the serine
protease inhibitors 4-(2-aminoethyl)benzenesulphonyl fluoride
(AEBSF), PMSF, di-isopropyl phosphofluoridate (DFP) and soybean
trypsin inhibitor (SBTI). Not inhibited by benzamidine or
iodoacetamide. Leupeptin and pepstatin A have a minor inhibitory
action. {ECO:0000269|PubMed:12413398}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.0. {ECO:0000269|PubMed:12413398};
Temperature dependence:
Optimum temperature is 80 degrees Celsius. Thermostable.
{ECO:0000269|PubMed:12413398};
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:12413398, ECO:0000269|PubMed:9188482}.
Note=Intracellular spaces and cell wall.
-!- TISSUE SPECIFICITY: Expressed in immature siliques and at lower
levels in stems and flowers (PubMed:11055401, PubMed:7647567,
PubMed:12413398). Widely expressed at low levels
(PubMed:18266922). {ECO:0000269|PubMed:11055401,
ECO:0000269|PubMed:12413398, ECO:0000269|PubMed:18266922,
ECO:0000269|PubMed:7647567}.
-!- DEVELOPMENTAL STAGE: Highest levels of expression detected during
silique development (PubMed:7647567). Hihghly expressed in the
seed coat during seed development (PubMed:18266922).
{ECO:0000269|PubMed:18266922, ECO:0000269|PubMed:7647567}.
-!- INDUCTION: By methyl jasmonate. {ECO:0000269|PubMed:12702015}.
-!- MASS SPECTROMETRY: Mass=76102.8; Method=MALDI; Range=107-757;
Evidence={ECO:0000269|PubMed:12413398};
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but mutant seeds are defective in mucilage extrusion.
{ECO:0000269|PubMed:18266922}.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF065639; AAC18851.1; -; Genomic_DNA.
EMBL; AB007645; BAB09021.1; -; Genomic_DNA.
EMBL; CP002688; AED98332.1; -; Genomic_DNA.
EMBL; AF360285; AAK25995.1; -; mRNA.
EMBL; AY091773; AAM10321.1; -; mRNA.
EMBL; AY142612; AAN13181.1; -; mRNA.
EMBL; BT001082; AAN46863.1; -; mRNA.
EMBL; X85974; CAA59963.1; -; mRNA.
PIR; JC7519; JC7519.
PIR; S52770; S52770.
RefSeq; NP_569048.1; NM_126136.3.
UniGene; At.23238; -.
UniGene; At.67722; -.
UniGene; At.71531; -.
ProteinModelPortal; O65351; -.
SMR; O65351; -.
BioGrid; 22113; 2.
STRING; 3702.AT5G67360.1; -.
MEROPS; S08.112; -.
PaxDb; O65351; -.
PRIDE; O65351; -.
EnsemblPlants; AT5G67360.1; AT5G67360.1; AT5G67360.
GeneID; 836871; -.
Gramene; AT5G67360.1; AT5G67360.1; AT5G67360.
KEGG; ath:AT5G67360; -.
Araport; AT5G67360; -.
TAIR; locus:2158187; AT5G67360.
eggNOG; ENOG410IEMN; Eukaryota.
eggNOG; COG1404; LUCA.
HOGENOM; HOG000238262; -.
InParanoid; O65351; -.
OMA; PTLHGTH; -.
OrthoDB; EOG093603BF; -.
PhylomeDB; O65351; -.
BioCyc; ARA:AT5G67360-MONOMER; -.
PRO; PR:O65351; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; O65351; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005576; C:extracellular region; IDA:TAIR.
GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:TAIR.
GO; GO:0080001; P:mucilage extrusion from seed coat; IMP:TAIR.
GO; GO:0048359; P:mucilage metabolic process involved in seed coat development; IMP:TAIR.
GO; GO:0010214; P:seed coat development; IMP:TAIR.
CDD; cd04852; Peptidases_S8_3; 1.
Gene3D; 3.30.70.80; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR034197; Peptidases_S8_3.
InterPro; IPR010259; S8pro/Inhibitor_I9.
InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
Pfam; PF05922; Inhibitor_I9; 1.
Pfam; PF02225; PA; 1.
Pfam; PF00082; Peptidase_S8; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF52743; SSF52743; 2.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
Calcium; Cell wall; Complete proteome; Direct protein sequencing;
Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
Serine protease; Signal; Zymogen.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 106 {ECO:0000255,
ECO:0000269|PubMed:12413398,
ECO:0000269|PubMed:9188482}.
/FTId=PRO_0000042846.
CHAIN 107 757 Subtilisin-like protease SBT1.7.
{ECO:0000269|PubMed:12413398}.
/FTId=PRO_0000042847.
DOMAIN 131 579 Peptidase S8.
ACT_SITE 139 139 Charge relay system.
{ECO:0000250|UniProtKB:P00782,
ECO:0000255|PROSITE-ProRule:PRU10082}.
ACT_SITE 212 212 Charge relay system.
{ECO:0000250|UniProtKB:P00782,
ECO:0000255|PROSITE-ProRule:PRU10082}.
ACT_SITE 542 542 Charge relay system.
{ECO:0000250|UniProtKB:P00782,
ECO:0000255|PROSITE-ProRule:PRU10082}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 376 376 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 631 631 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 644 644 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 41 41 M -> T (in Ref. 5; CAA59963).
{ECO:0000305}.
CONFLICT 242 247 APRARV -> LHAL (in Ref. 5; CAA59963).
{ECO:0000305}.
CONFLICT 562 562 W -> C (in Ref. 4; AAM10321/AAN46863).
{ECO:0000305}.
CONFLICT 670 670 V -> A (in Ref. 5; CAA59963).
{ECO:0000305}.
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


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