ID SBT25_ARATH Reviewed; 815 AA.
AC O64481;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 24-JAN-2024, entry version 169.
DE RecName: Full=Subtilisin-like protease SBT2.5 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Subtilase subfamily 2 member 5 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT2.5 {ECO:0000303|PubMed:16193095};
DE AltName: Full=Subtilisin-like serine protease 3 {ECO:0000303|PubMed:12702015};
DE Short=At-SLP3 {ECO:0000303|PubMed:12702015};
DE Flags: Precursor;
GN Name=SBT2.5 {ECO:0000303|PubMed:16193095};
GN Synonyms=SLP3 {ECO:0000303|PubMed:12702015};
GN OrderedLocusNames=At2g19170 {ECO:0000312|Araport:AT2G19170};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 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 TISSUE SPECIFICITY, AND INDUCTION BY METHYL JASMONATE.
RX PubMed=12702015; DOI=10.1034/j.1399-3054.2003.00087.x;
RA Golldack D., Vera P., Dietz K.J.;
RT "Expression of subtilisin-like serine proteases in Arabidopsis thaliana is
RT cell-specific and responds to jasmonic acid and heavy metals with
RT developmental differences.";
RL Physiol. Plantarum 118:64-73(2003).
RN [5]
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 -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers of mature
CC plants. {ECO:0000269|PubMed:12702015}.
CC -!- INDUCTION: By methyl jasmonate. {ECO:0000269|PubMed:12702015}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AC002392; AAD12040.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06854.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61987.1; -; Genomic_DNA.
DR EMBL; AY051009; AAK93686.1; -; mRNA.
DR EMBL; AY133826; AAM91760.1; -; mRNA.
DR PIR; T00538; T00538.
DR RefSeq; NP_001324171.1; NM_001335625.1.
DR RefSeq; NP_565447.1; NM_127474.4.
DR AlphaFoldDB; O64481; -.
DR SMR; O64481; -.
DR STRING; 3702.O64481; -.
DR MEROPS; S08.A02; -.
DR GlyCosmos; O64481; 3 sites, No reported glycans.
DR PaxDb; 3702-AT2G19170-1; -.
DR ProteomicsDB; 232795; -.
DR EnsemblPlants; AT2G19170.1; AT2G19170.1; AT2G19170.
DR EnsemblPlants; AT2G19170.2; AT2G19170.2; AT2G19170.
DR GeneID; 816434; -.
DR Gramene; AT2G19170.1; AT2G19170.1; AT2G19170.
DR Gramene; AT2G19170.2; AT2G19170.2; AT2G19170.
DR KEGG; ath:AT2G19170; -.
DR Araport; AT2G19170; -.
DR TAIR; AT2G19170; SLP3.
DR eggNOG; ENOG502QS8I; Eukaryota.
DR HOGENOM; CLU_000625_3_1_1; -.
DR InParanoid; O64481; -.
DR OMA; NTPCNYD; -.
DR OrthoDB; 11910at2759; -.
DR PhylomeDB; O64481; -.
DR PRO; PR:O64481; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64481; baseline and differential.
DR Genevisible; O64481; AT.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-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; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF722; SUBTILISIN-LIKE PROTEASE SBT2.5; 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; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Serine protease;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..815
FT /note="Subtilisin-like protease SBT2.5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431967"
FT DOMAIN 21..124
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 120..671
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 397..501
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 596
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 815 AA; 87667 MW; CD41FA92159AA200 CRC64;
MDIGLRIFVV FVLLVAVTAE VYIVTMEGDP IISYKGGENG FEATAVESDE KIDTSSELVT
VYARHLERKH DMILGMLFEE GSYKKLYSYK HLINGFAAHV SPEQAETLRR APGVRSVDKD
WKVRRLTTHT PEFLGLPTDV WPTGGGFDRA GEDIVIGFVD SGIYPHHPSF ASHHRLPYGP
LPHYKGKCEE DPHTKKSFCN RKIVGAQHFA EAAKAAGAFN PDIDYASPMD GDGHGSHTAA
IAAGNNGIPL RMHGYEFGKA SGMAPRARIA VYKALYRLFG GFVADVVAAI DQAVHDGVDI
LSLSVGPNSP PTTTKTTFLN PFDATLLGAV KAGVFVAQAA GNGGPFPKTL VSYSPWITTV
AAAIDDRRYK NHLTLGNGKM LAGMGLSPPT RPHRLYTLVS ANDVLLDSSV SKYNPSDCQR
PEVFNKKLVE GNILLCGYSF NFVVGTASIK KVVATAKHLG AAGFVLVVEN VSPGTKFDPV
PSAIPGILIT DVSKSMDLID YYNASTSRDW TGRVKSFKAE GSIGDGLAPV LHKSAPQVAL
FSARGPNTKD FSFQDADLLK PDILAPGYLI WAAWCPNGTD EPNYVGEGFA LISGTSMAAP
HIAGIAALVK QKHPQWSPAA IKSALMTTST VIDRAGRLLQ AQQYSDTEAV TLVKATPFDY
GSGHVNPSAA LDPGLIFDAG YEDYLGFLCT TPGISAHEIR NYTNTACNYD MKHPSNFNAP
SIAVSHLVGT QTVTRKVTNV AEVEETYTIT ARMQPSIAIE VNPPAMTLRP GATRTFSVTM
TVRSVSGVYS FGEVKLKGSR GHKVRIPVVA LGHRR
//
