SBT14_ARATH
ID SBT14_ARATH Reviewed; 777 AA.
AC Q9LVJ1; B9DHY1; Q0WWH7;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Subtilisin-like protease SBT1.4 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 1 member 4 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT1.4 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT1.4 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At3g14067 {ECO:0000312|Araport:AT3G14067};
GN ORFNames=MDC16.21 {ECO:0000312|EMBL:BAB02339.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-777.
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
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; AB019229; BAB02339.1; -; Genomic_DNA.
DR EMBL; AP000600; BAB02339.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE75461.1; -; Genomic_DNA.
DR EMBL; BT011692; AAS49055.1; -; mRNA.
DR EMBL; BT012275; AAS76762.1; -; mRNA.
DR EMBL; AK226374; BAE98521.1; -; mRNA.
DR EMBL; AK229057; BAF00939.1; -; mRNA.
DR EMBL; AK317689; BAH20348.1; -; mRNA.
DR RefSeq; NP_566473.2; NM_112261.4.
DR AlphaFoldDB; Q9LVJ1; -.
DR SMR; Q9LVJ1; -.
DR IntAct; Q9LVJ1; 1.
DR STRING; 3702.AT3G14067.1; -.
DR MEROPS; S08.A28; -.
DR iPTMnet; Q9LVJ1; -.
DR PaxDb; Q9LVJ1; -.
DR PRIDE; Q9LVJ1; -.
DR ProMEX; Q9LVJ1; -.
DR ProteomicsDB; 232929; -.
DR EnsemblPlants; AT3G14067.1; AT3G14067.1; AT3G14067.
DR GeneID; 820621; -.
DR Gramene; AT3G14067.1; AT3G14067.1; AT3G14067.
DR KEGG; ath:AT3G14067; -.
DR Araport; AT3G14067; -.
DR TAIR; locus:2087512; AT3G14067.
DR eggNOG; ENOG502QZDA; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; Q9LVJ1; -.
DR OMA; TGIWSER; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9LVJ1; -.
DR BRENDA; 3.4.21.62; 399.
DR PRO; PR:Q9LVJ1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVJ1; baseline and differential.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0010150; P:leaf senescence; IEP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0010223; P:secondary shoot formation; IMP:TAIR.
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; 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; 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..25
FT /evidence="ECO:0000255"
FT PROPEP 26..110
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q9MAP7"
FT /id="PRO_0000435172"
FT CHAIN 111..?
FT /note="Subtilisin-like protease SBT1.4"
FT /id="PRO_5004329314"
FT PROPEP ?..777
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435173"
FT DOMAIN 32..110
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 115..614
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 376..461
FT /note="PA"
FT /evidence="ECO:0000255"
FT REGION 199..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 546
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 206
FT /note="K -> M (in Ref. 5; BAE98521)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="E -> D (in Ref. 6; BAH20348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 81817 MW; 06F2AF7FBEB44B42 CRC64;
MAKLSLSSIF FVFPLLLCFF SPSSSSSDGL ESYIVHVQRS HKPSLFSSHN NWHVSLLRSL
PSSPQPATLL YSYSRAVHGF SARLSPIQTA ALRRHPSVIS VIPDQAREIH TTHTPAFLGF
SQNSGLWSNS NYGEDVIVGV LDTGIWPEHP SFSDSGLGPI PSTWKGECEI GPDFPASSCN
RKLIGARAFY RGYLTQRNGT KKHAAKESRS PRDTEGHGTH TASTAAGSVV ANASLYQYAR
GTATGMASKA RIAAYKICWT GGCYDSDILA AMDQAVADGV HVISLSVGAS GSAPEYHTDS
IAIGAFGATR HGIVVSCSAG NSGPNPETAT NIAPWILTVG ASTVDREFAA NAITGDGKVF
TGTSLYAGES LPDSQLSLVY SGDCGSRLCY PGKLNSSLVE GKIVLCDRGG NARVEKGSAV
KLAGGAGMIL ANTAESGEEL TADSHLVPAT MVGAKAGDQI RDYIKTSDSP TAKISFLGTL
IGPSPPSPRV AAFSSRGPNH LTPVILKPDV IAPGVNILAG WTGMVGPTDL DIDPRRVQFN
IISGTSMSCP HVSGLAALLR KAHPDWSPAA IKSALVTTAY DVENSGEPIE DLATGKSSNS
FIHGAGHVDP NKALNPGLVY DIEVKEYVAF LCAVGYEFPG ILVFLQDPTL YDACETSKLR
TAGDLNYPSF SVVFASTGEV VKYKRVVKNV GSNVDAVYEV GVKSPANVEI DVSPSKLAFS
KEKSVLEYEV TFKSVVLGGG VGSVPGHEFG SIEWTDGEHV VKSPVAVQWG QGSVQSF
