SBT4D_ARATH
ID SBT4D_ARATH Reviewed; 732 AA.
AC Q9FIG2;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Subtilisin-like protease SBT4.13 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 4 member 13 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT4.13 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT4.13 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g59120 {ECO:0000312|Araport:AT5G59120};
GN ORFNames=MNC17.3 {ECO:0000312|EMBL:BAB09758.1};
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 -!- PTM: The C-terminal propeptide is autocleaved.
CC {ECO:0000250|UniProtKB:Q39547}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AB016890; BAB09758.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97145.1; -; Genomic_DNA.
DR EMBL; AY093059; AAM13058.1; -; mRNA.
DR EMBL; BT010334; AAQ56777.1; -; mRNA.
DR RefSeq; NP_568898.2; NM_125302.5.
DR AlphaFoldDB; Q9FIG2; -.
DR SMR; Q9FIG2; -.
DR STRING; 3702.AT5G59120.1; -.
DR MEROPS; S08.A21; -.
DR PaxDb; Q9FIG2; -.
DR PRIDE; Q9FIG2; -.
DR ProteomicsDB; 232956; -.
DR EnsemblPlants; AT5G59120.1; AT5G59120.1; AT5G59120.
DR GeneID; 836030; -.
DR Gramene; AT5G59120.1; AT5G59120.1; AT5G59120.
DR KEGG; ath:AT5G59120; -.
DR Araport; AT5G59120; -.
DR TAIR; locus:2168434; AT5G59120.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR HOGENOM; CLU_000625_4_3_1; -.
DR InParanoid; Q9FIG2; -.
DR OMA; YKVCTPT; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9FIG2; -.
DR PRO; PR:Q9FIG2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIG2; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..109
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435251"
FT CHAIN 110..?
FT /note="Subtilisin-like protease SBT4.13"
FT /evidence="ECO:0000255"
FT /id="PRO_5004325421"
FT PROPEP ?..732
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435252"
FT DOMAIN 31..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 113..579
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 352..436
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 518
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 732 AA; 76869 MW; F4B9191BA3D00871 CRC64;
MATLAASSSL LSCLLVLFLS SVSAVTDDKQ VYIVYMGSLS SRADYTPTSD HMNILQEVTG
ESSIEGRLVR SYKRSFNGFA ARLTESERER VAKMVGVVSV FPNKKLQLQT TTSWDFMGLK
EGIKTKRNPT VESDTIIGVI DSGITPESQS FSDKGFGPPP QKWKGVCSGG KNFTCNNKLI
GARDYTSEGT RDMDGHGTHT ASTAAGNAVV DASFFGIGNG TVRGGVPASR VAAYKVCTPT
GCSSEALLSA FDDAIADGVD LITISIGDKT ASMFQNDPIA IGAFHAMAKG VLTVNSAGNS
GPKPISVSGV APWILTVAAS TTNRGFVTKV VLGNGKTLVG KSVNAYEMKG KDYPLVYGKS
AASSACDAES AGLCELSCVD KSRVKGKILV CGGPGGLKIV ESVGAVGLIY RTPKPDVAFI
HPLPAAGLLT EDFESLVSYL ESTDSPQAIV LKTEAIFNRT SPVIASFSSR GPNTIAVDIL
KPDITAPGVE ILAAYSPAGE PSQDDTRHVK YSVLSGTSMS CPHVAGVAAY VKTFNPKWSP
SMIQSAIMTT AWPVNATGTG IASTEFAYGS GHVDPIAASN PGLVYELDKS DHIAFLCGMN
YTSQVLKVIS GETVTCSEAK KILPRNLNYP SMSAKLSGSG TTFTVTFNRT LTNVGTPNST
YTSKVVAGHG SKLDVKITPS VLSFKTVNEK QSFTVTVTGS NLDSEVPSSA NLIWSDGTHN
VRSPIVVYTS DY
