SBT45_ARATH
ID SBT45_ARATH Reviewed; 738 AA.
AC F4JA91; Q9STF6;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Subtilisin-like protease SBT4.5 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 4 member 5 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT4.5 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT4.5 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At3g46840 {ECO:0000312|Araport:AT3G46840};
GN ORFNames=T6H20.130 {ECO:0000312|EMBL:CAB51181.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 -!- PTM: The C-terminal propeptide is autocleaved.
CC {ECO:0000250|UniProtKB:Q39547}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL096859; CAB51181.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78210.1; -; Genomic_DNA.
DR PIR; T12964; T12964.
DR RefSeq; NP_566887.2; NM_114551.2.
DR AlphaFoldDB; F4JA91; -.
DR SMR; F4JA91; -.
DR STRING; 3702.AT3G46840.1; -.
DR MEROPS; S08.A18; -.
DR iPTMnet; F4JA91; -.
DR PaxDb; F4JA91; -.
DR PRIDE; F4JA91; -.
DR ProteomicsDB; 226648; -.
DR EnsemblPlants; AT3G46840.1; AT3G46840.1; AT3G46840.
DR GeneID; 823837; -.
DR Gramene; AT3G46840.1; AT3G46840.1; AT3G46840.
DR KEGG; ath:AT3G46840; -.
DR Araport; AT3G46840; -.
DR TAIR; locus:2102792; AT3G46840.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR HOGENOM; CLU_000625_4_3_1; -.
DR InParanoid; F4JA91; -.
DR OMA; CGLKYTG; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:F4JA91; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JA91; 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 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..112
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435234"
FT CHAIN 113..738
FT /note="Subtilisin-like protease SBT4.5"
FT /evidence="ECO:0000255"
FT /id="PRO_5003309744"
FT PROPEP ?..738
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435235"
FT DOMAIN 35..111
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 116..589
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 362..433
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 527
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 348
FT /note="T -> TV (in Ref. 1; CAB51181)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 738 AA; 79061 MW; 7DE1BD9C136146AC CRC64;
MTKPAVSYCL LSCIFALLVV SFASADKDDQ DKQEYIVYMG ALPARVDYMP MSHHTSILQD
VTGESSIEDR LVRNYKRSFN GFAARLTKSE REILASMDEV VSVFPNKKLK LQTTTSWNFM
GLKESKRTKR NTIIESDTII GVIDSGIYPE SDSFSGKGFG PPPKKWKGVC KGGKNFTWNN
KLIGARYYTP KLEGFPESAR DYMGHGSHTA STAAGNAVKH VSFYGLGNGT ARGGVPAARI
AVYKVCDPGV DGCTTDGILA AFDDAIADKV DIITISIGGD NSSPFEEDPI AIGAFHAMAK
GILIVNSAGN SGPEPSTVAS IAPWMFTVAA SNTNRAFVTK VVLGNGKTVG RSVNSFDLNG
KKYPLVYGKS ASSSCGAASA GFCSPGCLDS KRVKGKIVLC DSPQNPDEAQ AMGAIASIVR
SHRTDVASIF SFPVSVLLED DYNTVLSYMN STKNPKAAVL KSETIFNQRA PVVASYFSRG
PNTIIPDILK PDITAPGSEI VAAYSPDAPP SISDTRRVKY SVDTGTSMSC PHVAGVAAYL
KSFHPRWSPS MIQSAIMTTA WPMNASTSPF NELAEFAYGA GHVDPITAIH PGLVYEANKS
DHIAFLCGLN YTAKNLRLIS GDSSSCTKEQ TKSLPRNLNY PSMTAQVSAA KPFKVIFRRT
VTNVGRPNAT YKAKVVGSKL KVKVVPAVLS LKSLYEKKSF TVTASGAGPK AENLVSAQLI
WSDGVHFVRS PIVVYATN