SBT11_ARATH
ID SBT11_ARATH Reviewed; 774 AA.
AC Q84WS0; Q9LPD1;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Subtilisin-like protease SBT1.1 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Subtilase subfamily 1 member 1 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT1.1 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBTI1.1 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At1g01900 {ECO:0000312|Araport:AT1G01900};
GN ORFNames=F22M8.3 {ECO:0000312|EMBL:AAF76468.1};
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, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND MUTAGENESIS OF SER-552.
RX PubMed=18643977; DOI=10.1111/j.1365-313x.2008.03598.x;
RA Srivastava R., Liu J.X., Howell S.H.;
RT "Proteolytic processing of a precursor protein for a growth-promoting
RT peptide by a subtilisin serine protease in Arabidopsis.";
RL Plant J. 56:219-227(2008).
CC -!- FUNCTION: Serine protease that cleaves the phytosulfokines PSK3, PSK2
CC and PSK5 in vitro. Phytosulfokines are plant growth factors or peptide
CC hormones that promotes plant cell differentiation, organogenesis and
CC somatic embryogenesis as well as cell proliferation.
CC {ECO:0000269|PubMed:18643977}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:18643977};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18643977}.
CC -!- INDUCTION: By auxin-rich callus induction medium (CIM) in root explants
CC followed by a transfer onto cytokinin-containing shoot induction medium
CC (SIM). {ECO:0000269|PubMed:18643977}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76468.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC020622; AAF76468.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE27347.1; -; Genomic_DNA.
DR EMBL; BT002840; AAO22659.1; -; mRNA.
DR PIR; G86150; G86150.
DR RefSeq; NP_563639.2; NM_100070.5.
DR AlphaFoldDB; Q84WS0; -.
DR SMR; Q84WS0; -.
DR STRING; 3702.AT1G01900.1; -.
DR MEROPS; S08.155; -.
DR PaxDb; Q84WS0; -.
DR PRIDE; Q84WS0; -.
DR ProteomicsDB; 226590; -.
DR EnsemblPlants; AT1G01900.1; AT1G01900.1; AT1G01900.
DR GeneID; 839318; -.
DR Gramene; AT1G01900.1; AT1G01900.1; AT1G01900.
DR KEGG; ath:AT1G01900; -.
DR Araport; AT1G01900; -.
DR TAIR; locus:2025457; AT1G01900.
DR eggNOG; ENOG502QPRW; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; Q84WS0; -.
DR OMA; IGLWNKT; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q84WS0; -.
DR PRO; PR:Q84WS0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84WS0; baseline and differential.
DR Genevisible; Q84WS0; AT.
DR GO; GO:0031012; C:extracellular matrix; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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; 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; 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; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Extracellular matrix; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..774
FT /note="Subtilisin-like protease SBT1.1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431964"
FT DOMAIN 56..120
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 122..623
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 379..472
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 552
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 552
FT /note="S->A: Loss of protease activity."
FT /evidence="ECO:0000269|PubMed:18643977"
SQ SEQUENCE 774 AA; 83247 MW; 5559D6E06E01709E CRC64;
MHRFLLMLLF PFSDNRPMMF FRSFIVFFFL IFFASNVSSR KQTYVIHTVT TSTKHIVTSL
FNSLQTENIN DDDFSLPEIH YIYENAMSGF SATLTDDQLD TVKNTKGFIS AYPDELLSLH
TTYSHEFLGL EFGIGLWNET SLSSDVIIGL VDTGISPEHV SFRDTHMTPV PSRWRGSCDE
GTNFSSSECN KKIIGASAFY KGYESIVGKI NETTDFRSTR DAQGHGTHTA STAAGDIVPK
ANYFGQAKGL ASGMRFTSRI AAYKACWALG CASTDVIAAI DRAILDGVDV ISLSLGGSSR
PFYVDPIAIA GFGAMQKNIF VSCSAGNSGP TASTVSNGAP WLMTVAASYT DRTFPAIVRI
GNRKSLVGSS LYKGKSLKNL PLAFNRTAGE ESGAVFCIRD SLKRELVEGK IVICLRGASG
RTAKGEEVKR SGGAAMLLVS TEAEGEELLA DPHVLPAVSL GFSDGKTLLN YLAGAANATA
SVRFRGTAYG ATAPMVAAFS SRGPSVAGPE IAKPDIAAPG LNILAGWSPF SSPSLLRSDP
RRVQFNIISG TSMACPHISG IAALIKSVHG DWSPAMIKSA IMTTARITDN RNRPIGDRGA
AGAESAATAF AFGAGNVDPT RAVDPGLVYD TSTVDYLNYL CSLNYTSERI LLFSGTNYTC
ASNAVVLSPG DLNYPSFAVN LVNGANLKTV RYKRTVTNVG SPTCEYMVHV EEPKGVKVRV
EPKVLKFQKA RERLSYTVTY DAEASRNSSS SSFGVLVWIC DKYNVRSPIA VTWE
