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SBT4A_ARATH
ID   SBT4A_ARATH             Reviewed;         693 AA.
AC   Q9FIM8;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Subtilisin-like protease SBT4.10 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 4 member 10 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT4.10 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT4.10 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At5g58810 {ECO:0000312|Araport:AT5G58810};
GN   ORFNames=K19M22.1 {ECO:0000312|EMBL:BAB09626.1};
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   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR   EMBL; AB016885; BAB09626.1; -; Genomic_DNA.
DR   EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q9FIM8; -.
DR   SMR; Q9FIM8; -.
DR   MEROPS; S08.A10; -.
DR   PeptideAtlas; Q9FIM8; -.
DR   PRIDE; Q9FIM8; -.
DR   Araport; AT5G58810; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIM8; 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   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 2.
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; 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   5: Uncertain;
KW   Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..113
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435244"
FT   CHAIN           114..?
FT                   /note="Subtilisin-like protease SBT4.10"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004325497"
FT   PROPEP          ?..693
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435245"
FT   DOMAIN          35..113
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          117..536
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          354..396
FT                   /note="PA"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        145
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        200
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        475
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        467
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        559
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        603
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        613
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   693 AA;  74246 MW;  C792103DA6BA7F4B CRC64;
     MAKLREASFC ALACVLVLFL SFVSADTYNR QDKQVYVVYM GSLPSQPDYK PTSDHISILQ
     QVTGESSMEG RLVRSYKKSF NGFSARLTES ERKRVAEMEG VVSVFPSKKY KLHTTASWDF
     MGLKEGKNTK RNLAVESDTI VGVFDTGISP ESESFSGKGF GPPPKKWKGV CKGGKNFTCN
     NKLIGARDYT NEGTRDIEGH GTHTASTAAG NVVENTSFYG IGNGTARGGV PDSRIAAYKV
     CSGAGCSSEY ILSAFDDAIA DGVDVISASL GGDTAYMYEK DPIAIGAFHA MAKGILTVQS
     AGNNGPNPTV SVAPWILTVA ASTTNRRIVT KVVLGNGKTL VGQSVNAFDL KGKQYPLVYE
     TSVEKCNNES LTTLALSFLT LTPQSNEQII SMFHTLIMWS PKATILKSEA IFNQTDPKVA
     GFSSRGPNTI AVDILKPDIT APGVEILAAY SPLVSPSATT LDNRRVNYTI TSGTSMACPH
     VSGVAAYIKT FHPEWYPSMI QSAIMTTAWP MNPSGTDAVS TEFAYGSGHI DPIAAINPGL
     VYELGKSDHI AFLCGLNYNA TTLKLIAGEA VTCTGKTLPR NLNYPSMSAK LSKSKSSFTV
     TFNRTVTNVG TSNSTYKSKV VINHGSKLKV KVSPSVLSMK SVNEKQSFTV SVSGNDLNPK
     LPSSANLIWS DGTHNVRSPI VVYTDYASSV DIF
 
 
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