SBT13_ARATH
ID SBT13_ARATH Reviewed; 780 AA.
AC Q9FLI4;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Subtilisin-like protease SBT1.3 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 1 member 3 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT1.3 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT1.3 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g51750 {ECO:0000312|Araport:AT5G51750};
GN ORFNames=MIO24.12 {ECO:0000312|EMBL:BAB11244.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(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=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 [4]
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; AB010074; BAB11244.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96122.1; -; Genomic_DNA.
DR EMBL; AY080831; AAL87307.1; -; mRNA.
DR RefSeq; NP_568765.1; NM_124554.3.
DR AlphaFoldDB; Q9FLI4; -.
DR SMR; Q9FLI4; -.
DR STRING; 3702.AT5G51750.1; -.
DR MEROPS; S08.A25; -.
DR PaxDb; Q9FLI4; -.
DR PRIDE; Q9FLI4; -.
DR ProteomicsDB; 232764; -.
DR EnsemblPlants; AT5G51750.1; AT5G51750.1; AT5G51750.
DR GeneID; 835249; -.
DR Gramene; AT5G51750.1; AT5G51750.1; AT5G51750.
DR KEGG; ath:AT5G51750; -.
DR Araport; AT5G51750; -.
DR TAIR; locus:2165366; AT5G51750.
DR eggNOG; ENOG502R0K0; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; Q9FLI4; -.
DR OMA; ISNYHVV; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9FLI4; -.
DR PRO; PR:Q9FLI4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLI4; 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..25
FT /evidence="ECO:0000255"
FT PROPEP 26..120
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q9MAP7"
FT /id="PRO_0000435170"
FT CHAIN 121..?
FT /note="Subtilisin-like protease SBT1.3"
FT /id="PRO_5004326092"
FT PROPEP ?..780
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435171"
FT DOMAIN 36..120
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 116..628
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 384..477
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 227
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 560
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 731
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 780 AA; 84950 MW; BE22D41550C8CBCF CRC64;
MANKNPLQKP FLFIILSINL IFLQAETTTQ ISTKKTYVIH MDKSAMPLPY TNHLQWYSSK
INSVTQHKSQ EEEGNNNRIL YTYQTAFHGL AAQLTQEEAE RLEEEDGVVA VIPETRYELH
TTRSPTFLGL ERQESERVWA ERVTDHDVVV GVLDTGIWPE SESFNDTGMS PVPATWRGAC
ETGKRFLKRN CNRKIVGARV FYRGYEAATG KIDEELEYKS PRDRDGHGTH TAATVAGSPV
KGANLFGFAY GTARGMAQKA RVAAYKVCWV GGCFSSDILS AVDQAVADGV QVLSISLGGG
VSTYSRDSLS IATFGAMEMG VFVSCSAGNG GPDPISLTNV SPWITTVGAS TMDRDFPATV
KIGTMRTFKG VSLYKGRTVL PKNKQYPLVY LGRNASSPDP TSFCLDGALD RRHVAGKIVI
CDRGVTPRVQ KGQVVKRAGG IGMVLTNTAT NGEELVADSH MLPAVAVGEK EGKLIKQYAM
TSKKATASLE ILGTRIGIKP SPVVAAFSSR GPNFLSLEIL KPDLLAPGVN ILAAWTGDMA
PSSLSSDPRR VKFNILSGTS MSCPHVSGVA ALIKSRHPDW SPAAIKSALM TTAYVHDNMF
KPLTDASGAA PSSPYDHGAG HIDPLRATDP GLVYDIGPQE YFEFLCTQDL SPSQLKVFTK
HSNRTCKHTL AKNPGNLNYP AISALFPENT HVKAMTLRRT VTNVGPHISS YKVSVSPFKG
ASVTVQPKTL NFTSKHQKLS YTVTFRTRFR MKRPEFGGLV WKSTTHKVRS PVIITWLPPL
