SBT1_SOYBN
ID SBT1_SOYBN Reviewed; 789 AA.
AC I1N462;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 3.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Subtilisin-like protease Glyma18g48580;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Subtilase peptide GmSubPep;
DE AltName: Full=Glycine max subtilase peptide;
DE Short=GmSubPep;
DE Flags: Precursor;
GN OrderedLocusNames=Glyma18g48580;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. A3525;
RX PubMed=20679205; DOI=10.1073/pnas.1007568107;
RA Pearce G., Yamaguchi Y., Barona G., Ryan C.A.;
RT "A subtilisin-like protein from soybean contains an embedded, cryptic
RT signal that activates defense-related genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14921-14925(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [3]
RP FUNCTION.
RC STRAIN=cv. A3525;
RX PubMed=21478368; DOI=10.1104/pp.111.173096;
RA Yamaguchi Y., Barona G., Ryan C.A., Pearce G.;
RT "GmPep914, an eight-amino acid peptide isolated from soybean leaves,
RT activates defense-related genes.";
RL Plant Physiol. 156:932-942(2011).
CC -!- FUNCTION: [Subtilase peptide GmSubPep]: Produces a rapid alkalinization
CC of the cellular media and the induction of defense-related genes,
CC including chitinase 1b, chalcone synthase and CYP93A1. The receptor for
CC GmSubPep is probably different from the receptor(s) for GmPep890 and
CC GmPep914. {ECO:0000269|PubMed:20679205, ECO:0000269|PubMed:21478368}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers and young
CC leaves. Barely detectable in matures leaves.
CC {ECO:0000269|PubMed:20679205}.
CC -!- INDUCTION: Not induced by wounding, methyl jasmonate, methyl salicylate
CC or etephon. {ECO:0000269|PubMed:20679205}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: The full-length coding region in cv. A3525 has been amplified
CC by RT-PCR and sequenced, but not submitted to the EMBL/GenBank/DDBJ
CC databases (PubMed:20679205). {ECO:0000305|PubMed:20679205}.
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DR AlphaFoldDB; I1N462; -.
DR SMR; I1N462; -.
DR STRING; 3847.GLYMA18G48580.1; -.
DR PRIDE; I1N462; -.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; I1N462; -.
DR Proteomes; UP000008827; Unplaced.
DR Genevisible; I1N462; GM.
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 GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
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 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..789
FT /note="Subtilisin-like protease Glyma18g48580"
FT /id="PRO_0000430187"
FT PEPTIDE 471..482
FT /note="Subtilase peptide GmSubPep"
FT /id="PRO_0000430188"
FT DOMAIN 32..116
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 120..644
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 401..489
FT /note="PA"
FT REGION 468..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 576
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 789 AA; 85087 MW; 43E0F32352ECFF33 CRC64;
MGSSIFCLHL ILSSFFLFTF LLAAVNGSKK CYIVYMGAHS HGPSPTSADL ELATDSHYDL
LGSIFGSREK AKEAIIYSYN RHINGFAALL EEEEAADIAK NPNVVSVFLS KEHKLHTTRS
WEFLGLHRRG QNSAWQKGRF GENTIIGNID TGVWPESQSF SDKGYGTVPS KWRGGLCQIN
KLPGSMKNTC NRKLIGARYY NKAFEAHNGQ LDPLLHTARD FVGHGTHTLS TAGGNFVPGA
RVFAVGNGTA KGGSPRARVA AYKVCWSLTD PASCYGADVL AAIDQAIDDG VDVINVSFGV
SYVVTAEGIF TDEISIGAFH AISKNILLVA SAGNDGPTPG TVANVAPWVF TIAASTLDRD
FSSNLTINNQ LIEGASLFVN LPPNQAFSLI LSTDAKLANA TFRDAQLCRR GTLDRTKVNG
KIVLCTREGK IKSVAEGLEA LTAGARGMIL NNQMQNGKTL SAEPHVFSTV NTPPRRAKSR
PHGVKTTAIG DEDDPLKTGD TIKMSRARTL FGRKPAPVMA SFSSRGPNKI QPSILKPDVT
APGVNILAAY SEFASASSLL VDNRRGFKFN VLQGTSMSCP HASGIAGLLK TRHPSWSPAA
IKSAIMTTAT TLDNTNRPIQ DAFDKTLADA FAYGSGHVRP DLAIEPGLVY DLSLTDYLNF
LCASGYDQQL ISALNFNRTF ICSGSHSVND LNYPSITLPN LRLKPVTIAR TVTNVGPPST
YTVSTRSPNG YSIAVVPPSL TFTKIGERKT FKVIVQASSA ATRRKYEFGD LRWTDGKHIV
RSPITVKRR