ID M1BGF3_SOLTU Unreviewed; 524 AA.
AC M1BGF3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Xylem serine proteinase 1 {ECO:0000313|EnsemblPlants:PGSC0003DMT400044595};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400044595, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400044595}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400044595};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR AlphaFoldDB; M1BGF3; -.
DR STRING; 4113.M1BGF3; -.
DR PaxDb; 4113-PGSC0003DMT400044595; -.
DR EnsemblPlants; PGSC0003DMT400044595; PGSC0003DMT400044595; PGSC0003DMG400017309.
DR Gramene; PGSC0003DMT400044595; PGSC0003DMT400044595; PGSC0003DMG400017309.
DR eggNOG; ENOG502QT1T; Eukaryota.
DR HOGENOM; CLU_000625_0_0_1; -.
DR InParanoid; M1BGF3; -.
DR OMA; GHIQPNF; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 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; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF688; SUBTILISIN-LIKE PROTEASE SBT5.3; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..524
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004013472"
FT DOMAIN 28..114
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 146..399
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 400..473
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
SQ SEQUENCE 524 AA; 55831 MW; 8AC41DAD8032EA35 CRC64;
MGENFASLCL LSILFMFLLS PTFAIKKSYV VYMGAHTHGK EVSSIDYDKV RDSHHEFLGS
YLGGSNEKAK EAIFYSYTRH INGFSAMLED EEAIEISKHP QVVSVFENRG RKLHTTRSWN
FLGLEHNDGV IPSSSLWEKA RFGEDSIIGN LDTGSWPEAE SFSDQGYGPI PSKWRGICQS
DSDPTFHCNR KLIGARYFNK GYATLAGSLN STFNTPRDTD GHGSHTLSTA GGNFVEGSNV
FGYGNGTAKG GSPKARVAAY KVCWTPISGN ECFDADILAA FDMAIHDGVD VLSVSLGGEA
VAYANDSVAI GSFHAVKHGI VVVTSAGNSG PAVSTVSNVA PWVITVGAST MDRQFPSYVT
LGNNKRYKGE SLSVEALPKG KLFPIITAAS AKATHATTYD AQLCKAGALD PKKVKGTILV
CLRGENARVD KGQQAALAGA VAMVLANDYA SGNEIIADPH VLPATQISYT DGLDVIAYVN
STRAPTASIT HPTTQLGTKP APVMAAFSSI GPNTVTPQIL KVLR
//