SBT33_ARATH
ID SBT33_ARATH Reviewed; 777 AA.
AC Q9MAP5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Subtilisin-like protease SBT3.3 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Subtilase subfamily 3 member 3 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.3 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.3 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At1g32960 {ECO:0000312|Araport:AT1G32960};
GN ORFNames=F9L11.13 {ECO:0000312|EMBL:AAF31276.1};
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=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 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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23818851; DOI=10.1371/journal.ppat.1003445;
RA Ramirez V., Lopez A., Mauch-Mani B., Gil M.J., Vera P.;
RT "An extracellular subtilase switch for immune priming in Arabidopsis.";
RL PLoS Pathog. 9:E1003445-E1003445(2013).
CC -!- FUNCTION: Serine protease that plays a role in the control of the
CC establishment of immune priming and systemic induced resistance.
CC {ECO:0000269|PubMed:23818851}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:23818851}.
CC -!- INDUCTION: By hydrogen peroxide and infection with the bacterial
CC pathogen Pseudomonas syringae pv. tomato strain DC3000.
CC {ECO:0000269|PubMed:23818851}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have enhanced disease susceptibility to
CC the pathogens P.syringae DC3000 and Hyaloperonospora arabidopsidis.
CC {ECO:0000269|PubMed:23818851}.
CC -!- MISCELLANEOUS: Plants over-expressing SBT3.3 show enhanced disease
CC resistance and enhanced activation of MPK3, MPK4, MPK6, MPK11 and OXI1.
CC {ECO:0000269|PubMed:23818851}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AC006424; AAF31276.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31544.1; -; Genomic_DNA.
DR EMBL; AY099740; AAM20591.1; -; mRNA.
DR EMBL; BT010347; AAQ56790.1; -; mRNA.
DR PIR; C86454; C86454.
DR RefSeq; NP_564414.2; NM_103029.3.
DR AlphaFoldDB; Q9MAP5; -.
DR SMR; Q9MAP5; -.
DR STRING; 3702.AT1G32960.1; -.
DR MEROPS; S08.A35; -.
DR iPTMnet; Q9MAP5; -.
DR PaxDb; Q9MAP5; -.
DR PRIDE; Q9MAP5; -.
DR ProteomicsDB; 232932; -.
DR EnsemblPlants; AT1G32960.1; AT1G32960.1; AT1G32960.
DR GeneID; 840190; -.
DR Gramene; AT1G32960.1; AT1G32960.1; AT1G32960.
DR KEGG; ath:AT1G32960; -.
DR Araport; AT1G32960; -.
DR TAIR; locus:2037935; AT1G32960.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR InParanoid; Q9MAP5; -.
DR OMA; CESLNFI; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9MAP5; -.
DR PRO; PR:Q9MAP5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAP5; baseline and differential.
DR Genevisible; Q9MAP5; AT.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0009682; P:induced systemic resistance; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW Extracellular matrix; Glycoprotein; Hydrolase; Plant defense; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..111
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:23818851"
FT /id="PRO_0000430827"
FT CHAIN 112..777
FT /note="Subtilisin-like protease SBT3.3"
FT /evidence="ECO:0000305|PubMed:23818851"
FT /id="PRO_0000430828"
FT DOMAIN 32..109
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 115..624
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 403..481
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 555
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 777 AA; 83640 MW; A5D0A3BA6245D63C CRC64;
MRSFRSSILL VLLSLITVLN ATRARSETES KVHIVYLGEK KHHDPEFVTE SHHQMLASLL
GSKKDADDSM VYSYRHGFSG FAAKLTKSQA KKIADLPEVV HVIPDGFHEL ATTRTWEYLG
LSSANPKNLL NDTNMGDQVI IGVIDTGVWP ESESFNDNGV GPIPRKWKGG CESGENFRST
DCNRKLIGAK YFINGFLAEN KGFNTTESRD YISARDFDGH GTHVASIAGG SFVPNVSYKG
LAGGTLRGGA PRARIAMYKA CWFHEELKGV TCSDSDIMKA IDEAIHDGVD VLSISLVGQI
PLNSETDIRD EFATGLFHAV AKGIVVVCAG GNDGPAAQTV VNIAPWILTV AATTLDRSFP
TPITLGNNKV ILGQATYTGP ELGLTSLVYP ENARNNNETF SGVCESLNLN PNYTMAMKVV
LCFTASRTNA AISRAASFVK AAGGLGLIIS RNPVYTLSPC NDDFPCVAVD YELGTDILSY
IRSTRSPVVK IQRSRTLSGQ PVGTKVVNFS SRGPNSMSPA ILKPDIAAPG VRILAATSPN
DTLNVGGFAM LSGTSMATPV ISGVIALLKA LHPEWSPAAF RSAIVTTAWR TDPFGEQIFA
EGSSRKVSDP FDYGGGIVNP EKAAEPGLIY DMGPQDYILY LCSAGYNDSS ISQLVGQITV
CSNPKPSVLD VNLPSITIPN LKDEVTLTRT VTNVGLVDSV YKVSVEPPLG VRVVVTPETL
VFNSKTISVS FTVRVSTTHK INTGYYFGSL TWTDSVHNVV IPLSVRTQIL QNYYDEN
