SBT43_ARATH
ID SBT43_ARATH Reviewed; 729 AA.
AC Q9FIF8; F4KHT7;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Subtilisin-like protease SBT4.3 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 4 member 3 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT4.3 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT4.3 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g59190 {ECO:0000312|Araport:AT5G59190};
GN ORFNames=MNC17.10 {ECO:0000312|EMBL:BAB09764.1};
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 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 -!- PTM: The C-terminal propeptide is autocleaved.
CC {ECO:0000250|UniProtKB:Q39547}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED97155.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016890; BAB09764.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97155.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_568901.1; NM_125309.1.
DR AlphaFoldDB; Q9FIF8; -.
DR SMR; Q9FIF8; -.
DR STRING; 3702.AT5G59190.1; -.
DR MEROPS; S08.A09; -.
DR PaxDb; Q9FIF8; -.
DR PRIDE; Q9FIF8; -.
DR ProteomicsDB; 232687; -.
DR EnsemblPlants; AT5G59190.1; AT5G59190.1; AT5G59190.
DR GeneID; 836037; -.
DR Gramene; AT5G59190.1; AT5G59190.1; AT5G59190.
DR KEGG; ath:AT5G59190; -.
DR Araport; AT5G59190; -.
DR TAIR; locus:2168524; AT5G59190.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9FIF8; -.
DR PRO; PR:Q9FIF8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIF8; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046686; P:response to cadmium ion; IEP: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 3: Inferred from homology;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..109
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435230"
FT CHAIN 110..?
FT /note="Subtilisin-like protease SBT4.3"
FT /evidence="ECO:0000255"
FT /id="PRO_5004325495"
FT PROPEP ?..729
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435231"
FT DOMAIN 32..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 113..580
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 350..436
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 521
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 729 AA; 78489 MW; 97689F606D379FBF CRC64;
MAKLSTPLYL ICLAFIFTRD VSANDYRQAS SVYIVYMGTL PEIKYSPPSH HLSILQKLVG
TIAASHLLVR SYKRSFNGFA ANLSQAESQK LQNMKEVVSV FPSKSHELTT TRSWDFVGFG
EKARRESVKE SDVIVGVIDS GIWPESESFD DEGFGPPPKK WKGSCKGGLK FACNNKLIGA
RFYNKFADSA RDEEGHGTHT ASTAAGNAVQ AASFYGLAQG TARGGVPSAR IAAYKVCFNR
CNDVDILAAF DDAIADGVDV ISISISADYV SNLLNASVAI GSFHAMMRGI ITAGSAGNNG
PDQGSVANVS PWMITVAASG TDRQFIDRVV LGNGKALTGI SVNTFNLNGT KFPIVYGQNV
SRNCSQAQAG YCSSGCVDSE LVKGKIVLCD DFLGYREAYL AGAIGVIVQN TLLPDSAFVV
PFPASSLGFE DYKSIKSYIE SAEPPQAEIL RTEEIVDREA PYVPSFSSRG PSFVIQNLLK
PDVSAPGLEI LAAFSPVASP SSFLNPEDKR SVRYSVMSGT SMACPHVAGV AAYVKSFHPD
WSPSAIKSAI MTTATPMNLK KNPEQEFAYG SGQINPTKAS DPGLVYEVET EDYLKMLCAE
GFDSTTLTTT SGQNVTCSER TEVKDLNYPT MTTFVSSLDP FNVTFKRTVT NVGFPNSTYK
ASVVPLQPEL QISIEPEILR FGFLEEKKSF VVTISGKELK DGSFVSSSVV WSDGSHSVRS
PIVAYSIQP
