SBT3A_ARATH
ID SBT3A_ARATH Reviewed; 759 AA.
AC Q9ZSB1;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Subtilisin-like protease SBT3.10 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 10 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.10 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.10 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At4g10530 {ECO:0000312|Araport:AT4G10530};
GN ORFNames=F3H7.13 {ECO:0000312|EMBL:AAD03437.1},
GN F7L13.110 {ECO:0000312|EMBL:CAB40046.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=AAD03437.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AEE82894.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB40046.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB78176.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF118222; AAD03437.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL049524; CAB40046.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL161517; CAB78176.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP002687; AEE82894.1; ALT_FRAME; Genomic_DNA.
DR PIR; T04188; T04188.
DR RefSeq; NP_567360.1; NM_117121.1.
DR AlphaFoldDB; Q9ZSB1; -.
DR SMR; Q9ZSB1; -.
DR STRING; 3702.AT4G10530.1; -.
DR MEROPS; S08.A38; -.
DR PaxDb; Q9ZSB1; -.
DR PRIDE; Q9ZSB1; -.
DR GeneID; 826645; -.
DR KEGG; ath:AT4G10530; -.
DR Araport; AT4G10530; -.
DR TAIR; locus:2127656; AT4G10530.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR InParanoid; Q9ZSB1; -.
DR OrthoDB; 921536at2759; -.
DR PRO; PR:Q9ZSB1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZSB1; differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
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..108
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435204"
FT CHAIN 109..?
FT /note="Subtilisin-like protease SBT3.10"
FT /id="PRO_5004338915"
FT PROPEP ?..759
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435205"
FT DOMAIN 29..106
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 112..606
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 390..464
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 537
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 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 759 AA; 81167 MW; D837C93A53A58394 CRC64;
MSKTIILLAF FLSIVLNVQI SFVVAESKVY VVYLGEKEHD NPESVTESHH QMLWSLLGSK
EAVLDSIVYS YRHGFSGFAA KLTESQAQQI SELPEVVQVI PNTLYEMTTT RTWDYLGVSP
GNSDSLLQKA NMGYNVIVGV IDTGVWPESE MFNDKGYGPI PSRWKGGCES GELFNGSIHC
NRKLIGAKYF IDANNAQFGV LNKTENPDYL SPRDFNGHGT HVASTIGGSF LPNVSYLGLG
RGTARGGAPG VHIAVYKACW VQRGCSGADV LKAMDEAIHD GVDILSLSLQ TSVPLFPETD
ARELTSVGAF HAVAKGIPVV AAASNAGPTA QTLSNVAPWV LTVAATTQDR SFPTAITLGN
NITILGQAIF GGSELGFVGL TYPESPLSGD CEKLSANPKS AMEGKVVLCF AASTPSNAAI
TAVINAGGLG LIMARNPTHL LRPLRNFPYV SVDFELGTDI LFYIRSTRSP IVNIQASRTL
FGQSVSTKVA TFSSRGPNSV SPAILKPDIA APGVNILAAI SPNSINDGGF AMMSGTSMAT
PVVSGVVVLL KSLHPDWSPS AIKSAIVTTA WRTDPSGEPI FADGSSRKLA DPFDYGGGLI
NPEKAVKPGL IYDMTTDDYV MYMCSVDYSD ISISRVLGKI TVCPNPKPSV LDLNLPSITI
PNLRGEVTLT RTVTNVGPVN SVYKVVIDPP TGVNVAVTPT ELVFDSTTTK RSFTVRVSTT
HKVNTGYYFG SLTWTDTLHN VAIPVSVRTQ ILQRYYDEN
