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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
 
 
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