ID   SBT56_ARATH             Reviewed;         791 AA.
AC   Q9FK76;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Subtilisin-like protease SBT5.6 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 5 member 6 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT5.6 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT5.6 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At5g45650 {ECO:0000312|Araport:AT5G45650};
GN   ORFNames=MRA19.5 {ECO:0000312|EMBL:BAB09208.1};
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=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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   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   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AB012245; BAB09208.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95280.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70243.1; -; Genomic_DNA.
DR   EMBL; AK118053; BAC42684.1; -; mRNA.
DR   EMBL; BT005679; AAO64099.1; -; mRNA.
DR   RefSeq; NP_001318744.1; NM_001344636.1.
DR   RefSeq; NP_199378.1; NM_123933.3.
DR   AlphaFoldDB; Q9FK76; -.
DR   SMR; Q9FK76; -.
DR   STRING; 3702.AT5G45650.1; -.
DR   MEROPS; S08.082; -.
DR   PaxDb; Q9FK76; -.
DR   PRIDE; Q9FK76; -.
DR   ProteomicsDB; 232930; -.
DR   EnsemblPlants; AT5G45650.1; AT5G45650.1; AT5G45650.
DR   EnsemblPlants; AT5G45650.2; AT5G45650.2; AT5G45650.
DR   GeneID; 834605; -.
DR   Gramene; AT5G45650.1; AT5G45650.1; AT5G45650.
DR   Gramene; AT5G45650.2; AT5G45650.2; AT5G45650.
DR   KEGG; ath:AT5G45650; -.
DR   Araport; AT5G45650; -.
DR   TAIR; locus:2171938; AT5G45650.
DR   eggNOG; ENOG502QRC5; Eukaryota.
DR   HOGENOM; CLU_000625_4_6_1; -.
DR   InParanoid; Q9FK76; -.
DR   OMA; EEHHHSY; -.
DR   OrthoDB; 337164at2759; -.
DR   PhylomeDB; Q9FK76; -.
DR   PRO; PR:Q9FK76; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FK76; 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; -; 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   Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..108
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435259"
FT   CHAIN           109..?
FT                   /note="Subtilisin-like protease SBT5.6"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004325448"
FT   PROPEP          ?..791
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435260"
FT   DOMAIN          26..104
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          134..645
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          400..494
FT                   /note="PA"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        160
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        235
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        578
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        666
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        713
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        761
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   791 AA;  85146 MW;  E3A11A3ECD036D41 CRC64;
     MKKLTSLFPL LFLIPLLASC AEEKQVYIVY FGEHKGDKAF HEIEEHHHSY LQSVKESEED
     ARASLLYSYK HSINGFAAEL TPDQASKLEK LAEVVSVFKS HPRKYEAHTT RSWEFVGLEE
     EETDSDVPRR KNDADDRFRV GRNFLKKAKH GDGIIVGVLD SGVWPESKSF NDKGMGPVPK
     SWKGICQTGV AFNSSHCNRK IIGARYYVKG YERYYGAFNA TANKDFLSPR DPDGHGSHTA
     STAVGRRVLG ASALGGFAKG SASGGAPLAR LAIYKACWAK PNAEKVEGNI CLEEDMLAAI
     DDAIADGVHV ISISIGTTEP FPFTQDGIAM GALHAVKRNI VVAASAGNSG PKPGTLSNLA
     PWIITVGAST LDRAFVGGLV LGNGYTIKTD SITAFKMDKF APLVYASNVV VPGIALNETS
     QCLPNSLKPE LVSGKVVLCL RGAGSRIGKG MEVKRAGGAG MILGNIAANG NEVPSDSHFV
     PTAGVTPTVV DKILEYIKTD KNPKAFIKPG KTVYKYQAAP SMTGFSSRGP NVVDPNILKP
     DITAPGLYIL AAWSGADSPS KMSVDQRVAG YNIYSGTSMS CPHVAGAIAL LKAIHPKWSS
     AAIRSALMTT AWMTNDKKKP IQDTTGLPAN PFALGSGHFR PTKAADPGLV YDASYRAYLL
     YGCSVNITNI DPTFKCPSKI PPGYNHNYPS IAVPNLKKTV TVKRTVTNVG TGNSTSTYLF
     SVKPPSGISV KAIPNILSFN RIGQKQRFKI VIKPLKNQVM NATEKGQYQF GWFSWTDKVH
     VVRSPIAVSL A