SBT19_ARATH
ID SBT19_ARATH Reviewed; 736 AA.
AC Q9FHA4;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Subtilisin-like protease SBT1.9 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 1 member 9 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT1.9 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT1.9 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g67090 {ECO:0000312|Araport:AT5G67090};
GN ORFNames=K21H1.5 {ECO:0000312|EMBL:BAB10943.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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; AB020742; BAB10943.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98299.1; -; Genomic_DNA.
DR EMBL; BT012577; AAS99721.1; -; mRNA.
DR EMBL; AK222002; BAD94613.1; -; mRNA.
DR RefSeq; NP_569044.1; NM_126109.3.
DR AlphaFoldDB; Q9FHA4; -.
DR SMR; Q9FHA4; -.
DR STRING; 3702.AT5G67090.1; -.
DR MEROPS; S08.A16; -.
DR PaxDb; Q9FHA4; -.
DR PRIDE; Q9FHA4; -.
DR ProteomicsDB; 232901; -.
DR EnsemblPlants; AT5G67090.1; AT5G67090.1; AT5G67090.
DR GeneID; 836844; -.
DR Gramene; AT5G67090.1; AT5G67090.1; AT5G67090.
DR KEGG; ath:AT5G67090; -.
DR Araport; AT5G67090; -.
DR TAIR; locus:2155583; AT5G67090.
DR eggNOG; ENOG502QT5U; Eukaryota.
DR HOGENOM; CLU_000625_3_1_1; -.
DR InParanoid; Q9FHA4; -.
DR OMA; INFLCHE; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9FHA4; -.
DR BRENDA; 3.4.21.62; 399.
DR PRO; PR:Q9FHA4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHA4; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0006508; P:proteolysis; IDA:TAIR.
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; IPR023827; Peptidase_S8_Asp-AS.
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; IPR041469; Subtilisin-like_FN3.
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; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..101
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q9MAP7"
FT /id="PRO_0000435178"
FT CHAIN 102..?
FT /note="Subtilisin-like protease SBT1.9"
FT /id="PRO_5004325411"
FT PROPEP ?..736
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435179"
FT DOMAIN 25..101
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 103..582
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 367..441
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 529
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 736 AA; 79777 MW; D29871E52E6D7591 CRC64;
MGMTVVIILV FSFFVAIVTA ETSPYIIHMD LSAKPLPFSD HRSWFSTTLT SVITNRKPKI
IYAYTDSVHG FSAVLTNSEL QRLKHKPGYV SFTKDLPVKL HTTFSPKFIG LNSTSGTWPV
SNYGAGIVIG IIDTGIWPDS PSFHDDGVGS VPSKWKGACE FNSSSLCNKK LIGAKVFNKG
LFANNPDLRE TKIGQYSSPY DTIGHGTHVA AIAAGNHVKN ASYFSYAQGT ASGIAPHAHL
AIYKAAWEEG IYSSDVIAAI DQAIRDGVHV ISLSLGLSFE DDDDNDGFGL ENDPIAVASF
AAIQKGVFVV TSGGNDGPYY WSLINGAPWI MTVGAGTIGR QFQGTLTFGN RVSFSFPSLF
PGEFPSVQFP VTYIESGSVE NKTLANRIVV CNENINIGSK LHQIRSTGAA AVVLITDKLL
EEQDTIKFQF PVAFIGSKHR ETIESYASSN KNNATAKLEF RKTVIGTKPA PEVGTYSSRG
PFTSFPQILK PDILAPGTLI LSAWPSVEQI TGTRALPLFS GFNLLTGTSM AAPHVAGVAA
LIKQVHPNWS PSAIKSAIMT TALTLDNPLA VGAGHVSTNK VLNPGLIYDT TPQDFINFLC
HEAKQSRKLI NIITRSNISD ACKKPSPYLN YPSIIAYFTS DQSSPKIFKR TLTNVGEAKR
SYIVRVRGLK GLNVVVEPKK LMFSEKNEKL SYTVRLESPR GLQENVVYGL VSWVDEDEAE
FEVSCSVVAT SLVQES
