SBT48_ARATH
ID SBT48_ARATH Reviewed; 710 AA.
AC Q9FIM6; F4KGD5;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Subtilisin-like protease SBT4.8 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 4 member 8 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT4.8 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT4.8 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g58830 {ECO:0000312|Araport:AT5G58830};
GN ORFNames=K19M22.3 {ECO:0000312|EMBL:BAB09628.1};
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}.
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DR EMBL; AB016885; BAB09628.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97108.2; -; Genomic_DNA.
DR RefSeq; NP_001318833.1; NM_001345324.1.
DR AlphaFoldDB; Q9FIM6; -.
DR SMR; Q9FIM6; -.
DR STRING; 3702.AT5G58830.1; -.
DR MEROPS; S08.A12; -.
DR PaxDb; Q9FIM6; -.
DR PRIDE; Q9FIM6; -.
DR ProteomicsDB; 232688; -.
DR EnsemblPlants; AT5G58830.1; AT5G58830.1; AT5G58830.
DR GeneID; 836000; -.
DR Gramene; AT5G58830.1; AT5G58830.1; AT5G58830.
DR KEGG; ath:AT5G58830; -.
DR Araport; AT5G58830; -.
DR TAIR; locus:2154513; AT5G58830.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR OMA; MRASSFC; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9FIM6; -.
DR PRO; PR:Q9FIM6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIM6; 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; 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 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..111
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435240"
FT CHAIN 112..?
FT /note="Subtilisin-like protease SBT4.8"
FT /evidence="ECO:0000255"
FT /id="PRO_5004329286"
FT PROPEP ?..710
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435241"
FT DOMAIN 33..110
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 115..559
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 354..414
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 498
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 710 AA; 76221 MW; ED6451B36538D601 CRC64;
MVKRASFCLL SCLIILFLSS VSAIIYDPQD KQVYVVYMGS LPSQPNYTPM SNHINILQEV
TGESSIEGRL VRSYKRSFNG FSALLTESER EGVAEMEGVV SVFRSKNYKL QTTASWDFMG
MKEGKNTKRN FAVESDTIIG FIDSGIWPES ESFSDKGFGP PPKKWKGVCK GGKNFTCNNK
LIGARDYTSE GTRDLQGHGT HTTSTAAGNA VADTSFFGIG NGTARGGVPA SRVAAYKVCT
ITGCSDDNVL SAFDDAIADG VDLISVSLGG DYPSLYAEDT IAIGAFHAMA KGILTVHSAG
NAGPNPTTVV SVAPWMLTVA ATTTNRRFLT KVVLGNGKTL VGKSVNAFDL KGKKYPLEYG
DYLNESLVKG KILVSRYLSG SEVAVSFITT DNKDYASISS RPLSVLSQDD FDSLVSYINS
TRSPQGSVLK TEAIFNQLSP KVASFSSRGP NTIAVDILKP DISAPGVEIL AAYSPLSLPS
EDRRDKRRVK YSVLSGTSMA CPHVTGVAAY IKTFHPDWSP SVIQSAIMTT AWQMNATGTG
AESTEFAYGA GHVDPIAAIN PGLVYELNKT DHISFLCGMN YTSKTLKLIS GDAVICSGKT
LQRNLNYPSM SAKLSESNSS FTVTFKRTVT NLGTANSTYK SKIVLNHGSK LNVKVSPSVL
SMKSLKEKQS FTVTVSGSNI DPKLPSSANL IWSDGTHNVR SPIVVYIDGY
