SBT3_LOTJA
ID SBT3_LOTJA Reviewed; 750 AA.
AC A9QY39;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Subtilisin-like protease 3 {ECO:0000303|PubMed:19220794};
DE Short=SbtM3 {ECO:0000303|PubMed:19220794};
DE Short=Subtilase 3 {ECO:0000303|PubMed:19220794};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10080};
DE Flags: Precursor;
GN Name=SBTM3 {ECO:0000303|PubMed:19220794};
OS Lotus japonicus (Lotus corniculatus var. japonicus).
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; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Miyakojima MG-20;
RX PubMed=18511435; DOI=10.1093/dnares/dsn008;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Kato T., Nakao M.,
RA Sasamoto S., Watanabe A., Ono A., Kawashima K., Fujishiro T., Katoh M.,
RA Kohara M., Kishida Y., Minami C., Nakayama S., Nakazaki N., Shimizu Y.,
RA Shinpo S., Takahashi C., Wada T., Yamada M., Ohmido N., Hayashi M.,
RA Fukui K., Baba T., Nakamichi T., Mori H., Tabata S.;
RT "Genome structure of the legume, Lotus japonicus.";
RL DNA Res. 15:227-239(2008).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY GLOMEROMYCOTA INTRARADICES,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Gifu / B-129, and cv. Miyakojima MG-20;
RX PubMed=19220794; DOI=10.1111/j.1365-313x.2009.03824.x;
RA Takeda N., Sato S., Asamizu E., Tabata S., Parniske M.;
RT "Apoplastic plant subtilases support arbuscular mycorrhiza development in
RT Lotus japonicus.";
RL Plant J. 58:766-777(2009).
CC -!- FUNCTION: Required for arbuscular mycorrhiza (AM) development during AM
CC symbiosis with AM fungi (e.g. Glomeromycota intraradices).
CC {ECO:0000269|PubMed:19220794}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:A9QY40}. Note=Accumulates in the intercellular
CC spaces and the periarbuscular space (PAS) during arbuscular mycorrhizal
CC (AM) symbiosis. {ECO:0000250|UniProtKB:A9QY40}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in root cells that are adjacent to
CC intra-radical fungal hyphae or in cells that harbor them during
CC arbuscular mycorrhizal (AM) symbiosis, especially in epidermal and
CC cortical cells. {ECO:0000269|PubMed:19220794}.
CC -!- INDUCTION: Rapidly induced in roots during development of arbuscular
CC mycorrhiza (AM) upon colonization by AM fungus (e.g. Glomeromycota
CC intraradices). {ECO:0000269|PubMed:19220794}.
CC -!- DISRUPTION PHENOTYPE: Decreased fungal colonization and impaired
CC arbuscular mycorrhiza (AM) development during AM symbiosis with AM
CC fungi (e.g. Glomeromycota intraradices). {ECO:0000269|PubMed:19220794}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009544; BAF95754.1; -; Genomic_DNA.
DR AlphaFoldDB; A9QY39; -.
DR SMR; A9QY39; -.
DR MEROPS; S08.006; -.
DR GO; GO:0048046; C:apoplast; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP: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; 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.
PE 2: Evidence at transcript level;
KW Apoplast; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..750
FT /note="Subtilisin-like protease 3"
FT /id="PRO_5002740671"
FT DOMAIN 44..120
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 127..603
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 369..457
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 211
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 536
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 750 AA; 79452 MW; 34044E8536BBD81C CRC64;
MTKVVQFSLL LALILVLSVS LASAASQNLE FTELEDEDQS NLSTYIVHVR KPQVIQSDDL
HTFYYSLLPE STKTTNQRIV FTYRNVVNGF AVKLTPEEAK ALQQNEEVVS ARPEKILSLH
TTHTPSFLGL QQGLGLWKGS NSGKGVIIGI LDTGISPFHP SFSDEGMPSP PAKWNGICEF
TGKRTCNNKI IGARNFVKTK NLTLPFDDVG HGTHTASTAA GRPVQGANVY GNANGTAVGM
APDAHIAMYK VCGLVGCSES AILAGMDTAV DDGVDVLSLS LGGPSGPFFE DPIALGAFGA
IQKGIFVSCS AANSGPAYSS LSNEAPWILT VGASSIDRTI MATAKLGNGK EYVGQSVFQP
KDFAPSLLPL VYAGANGNNN FSVFCAPESL NRSDVEGKVV LCEDGGFVPR VFKGKAVKDA
GGAAMILMNS VLEDFNPIAD VHVLPAVHIS YEAGLALKEY INSTSTPTAT ILFEGTVIGN
LLAPQVTSFS SRGPSKASPG ILKPDIIGPG LNILAAWPVS LDNSTTPPFN IISGTSMSCP
HLSGIAALLK NSHPDWSPAA IKSAIMTTAS QVNLGGTPIL DQRLVPADVF ATGAGHVNPV
KANDPGLVYD IEPNDYIPYL CGLNYTDREV GVILQQRVRC SEVNHIAEAE LNYPSFSILL
GNTTQLYTRT VANVGPANST YTAEIGVPVG VGMSLSPAQL TFTEVGQKLT YSVSFIPFSE
DRDNHTFAQG SLKWVSGKYS VRSPISFIFL
