SBT3H_ARATH
ID SBT3H_ARATH Reviewed; 753 AA.
AC Q9C7U8;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Subtilisin-like protease SBT3.17 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 17 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.17 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.17 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At1g66220 {ECO:0000312|Araport:AT1G66220};
GN ORFNames=T6J19.4 {ECO:0000312|EMBL:AAG51764.1};
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 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).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AC066691; AAG51764.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34478.1; -; Genomic_DNA.
DR PIR; B96687; B96687.
DR RefSeq; NP_564869.1; NM_105293.1.
DR AlphaFoldDB; Q9C7U8; -.
DR SMR; Q9C7U8; -.
DR STRING; 3702.AT1G66220.1; -.
DR MEROPS; S08.A33; -.
DR PaxDb; Q9C7U8; -.
DR PRIDE; Q9C7U8; -.
DR ProteomicsDB; 232798; -.
DR EnsemblPlants; AT1G66220.1; AT1G66220.1; AT1G66220.
DR GeneID; 842937; -.
DR Gramene; AT1G66220.1; AT1G66220.1; AT1G66220.
DR KEGG; ath:AT1G66220; -.
DR Araport; AT1G66220; -.
DR TAIR; locus:2205278; AT1G66220.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR InParanoid; Q9C7U8; -.
DR OMA; PICEQER; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9C7U8; -.
DR PRO; PR:Q9C7U8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7U8; differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
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; 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 3: Inferred from homology;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..116
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435219"
FT CHAIN 117..?
FT /note="Subtilisin-like protease SBT3.17"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435220"
FT PROPEP ?..753
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435221"
FT DOMAIN 38..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 120..603
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 227
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 534
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 753 AA; 80793 MW; B2128AFDCC17BDA1 CRC64;
MGNSFLIADT SSLVIGLLLI LNGVFISAAK HYGLNKIHIV HLGAKQHDTP ELVTKSHYQI
LEPLLGSKEA AKNSLVYNYK HGFSGFAAKL TASQAKNLSA HPEVLRVVPS RVMRLKTTRT
FDYLGLLPTS PKSLLHKTKM GSEAIIGVID SGIWPESQSF NDTGLGPIPK RWKGKCLSGN
GFDAKKHCNK KLIGAEYLTV GLMEMTDGIY DYPSLGESMS PRDHVGHGTH VAAIAAGSFV
ANANYKGLAG GTARGAAPHA RIAMYKVCWR EVGCITADLL KAIDHSIRDG VDVISISIGT
DAPASFDIDQ SDIGFGSFHA VMKGIPVVAS AGNEGPNAQT VDNVAPWIIT VAATSLDRSF
PIPITLGNNL TILGEGLNTF PEVGFTNLIL SDEMLSRSIE QGKTQGTIVL AFTANDEMIR
KANSITNAGC AGIIYAQSVI DPTVCSSVDV PCAVVDYEYG TDILYYMQTT VVPKAKLSPS
KTLIGRPIAS RVPRFSCRGP NSVSPAILKP DIAAPGVNVL SAVSGVYKFM SGTSMATPAV
SGIVGLLRQT HPHWSPAAIR SALVTTAWKT DPSGEPIFSE GSTRKLADPF DYGGGLINPE
KVTHPGLIYD MGIDDYLHYL CSAEYDDDSI SKLLGKTYNC TSPKPSMLDF NLPSITIPSL
TGEVTVTRTV RNVGPARSVY RPVIESPLGI ELDVKPKTLV FGSNITKITF SVRVKSSHRV
NTDFYFGSLC WTDGVHNVTI PVSVRTKFMR NYV
