SBT51_ARATH
ID SBT51_ARATH Reviewed; 780 AA.
AC F4HSQ2; Q9LNU0;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Subtilisin-like protease SBT5.1 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 5 member 1 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT5.1 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT5.1 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At1g20150 {ECO:0000312|Araport:AT1G20150};
GN ORFNames=T20H2.7 {ECO:0000312|EMBL:AAF79898.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79898.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC022472; AAF79898.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE29944.1; -; Genomic_DNA.
DR PIR; C86335; C86335.
DR RefSeq; NP_564106.1; NM_101869.2.
DR AlphaFoldDB; F4HSQ2; -.
DR SMR; F4HSQ2; -.
DR STRING; 3702.AT1G20150.1; -.
DR MEROPS; S08.A23; -.
DR iPTMnet; F4HSQ2; -.
DR PaxDb; F4HSQ2; -.
DR PRIDE; F4HSQ2; -.
DR EnsemblPlants; AT1G20150.1; AT1G20150.1; AT1G20150.
DR GeneID; 838605; -.
DR Gramene; AT1G20150.1; AT1G20150.1; AT1G20150.
DR KEGG; ath:AT1G20150; -.
DR Araport; AT1G20150; -.
DR TAIR; locus:2198606; AT1G20150.
DR eggNOG; ENOG502QUSK; Eukaryota.
DR HOGENOM; CLU_000625_4_4_1; -.
DR InParanoid; F4HSQ2; -.
DR OMA; ARNCAPD; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:F4HSQ2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HSQ2; 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; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
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; PS00137; SUBTILASE_HIS; 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..25
FT /evidence="ECO:0000255"
FT PROPEP 26..106
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435255"
FT CHAIN 107..?
FT /note="Subtilisin-like protease SBT5.1"
FT /evidence="ECO:0000255"
FT /id="PRO_5003315062"
FT PROPEP ?..780
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435256"
FT DOMAIN 33..106
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 110..617
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 385..469
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 550
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 780 AA; 85722 MW; 1AA630A956D5BFA6 CRC64;
MMRCLTITIM FFMFFFLSVI QKCKSETSKS GDYIIYMGAA SSDGSTDNDH VELLSSLLQR
SGKTPMHRYK HGFSGFAAHL SEDEAHLIAK QPGVLSVFPD QMLQLHTTRS WDFLVQESYQ
RDTYFTEMNY EQESEMHEGD TIIGFLDSGI WPEAQSFNDR HMGPVPEKWK GTCMRGKKTQ
PDSFRCNRKL IGARYYNSSF FLDPDYETPR DFLGHGTHVA SIAAGQIIAN ASYYGLASGI
MRGGSPSSRI AMYRACSLLG CRGSSILAAF DDAIADGVDV ISISMGLWPD NLLEDPLSIG
SFHAVERGIT VVCSVGNSGP SSQSVFNAAP WMITVAASTI DRGFESNILL GGDENRLIEG
FGINIANIDK TQAYPLIHAR SAKKIDANEE AARNCAPDTL DQTIVKGKIV VCDSDLDNQV
IQWKSDEVKR LGGIGMVLVD DESMDLSFID PSFLVTIIKP EDGIQIMSYI NSTREPIATI
MPTRSRTGHM LAPSIPSFSS RGPYLLTRSI LKPDIAAPGV NILASWLVGD RNAAPEGKPP
PLFNIESGTS MSCPHVSGIA ARLKSRYPSW SPAAIRSAIM TTAVQMTNTG SHITTETGEK
ATPYDFGAGQ VTIFGPSSPG LIYETNHMDY LNFLGYYGFT SDQIKKISNR IPQGFACPEQ
SNRGDISNIN YPSISISNFN GKESRRVSRT VTNVASRLIG DEDTVYTVSI DAPEGLLVRV
IPRRLHFRKI GDKLSYQVIF SSTTTILKDD AFGSITWSNG MYNVRSPFVV TSKDDNDSER
