SBT4C_ARATH
ID SBT4C_ARATH Reviewed; 736 AA.
AC Q8L7D2; Q9FGU4;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Subtilisin-like protease SBT4.12 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 4 member 12 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT4.12 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT4.12 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g59090 {ECO:0000312|Araport:AT5G59090};
GN ORFNames=K18B18.9 {ECO:0000312|EMBL:BAB10784.1};
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 {ECO:0000312|EMBL:AAM97000.1};
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;
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).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION BY JASMONATE.
RC STRAIN=cv. Columbia;
RX PubMed=19832941; DOI=10.1111/j.1399-3054.2009.01281.x;
RA Kuroha T., Okuda A., Arai M., Komatsu Y., Sato S., Kato T., Tabata S.,
RA Satoh S.;
RT "Identification of Arabidopsis subtilisin-like serine protease specifically
RT expressed in root stele by gene trapping.";
RL Physiol. Plantarum 137:281-288(2009).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist. {ECO:0000305};
CC Name=1;
CC IsoId=Q8L7D2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Specifically expressed in root stele of the root
CC hair zone. {ECO:0000269|PubMed:19832941}.
CC -!- INDUCTION: Accumulates in roots after methyl jasmonate (MeJA)
CC treatment. {ECO:0000269|PubMed:19832941}.
CC -!- PTM: The C-terminal propeptide is autocleaved.
CC {ECO:0000250|UniProtKB:Q39547}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10784.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB024027; BAB10784.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97139.1; -; Genomic_DNA.
DR EMBL; AY136334; AAM97000.1; -; mRNA.
DR EMBL; BT000127; AAN15446.1; -; mRNA.
DR RefSeq; NP_568895.1; NM_125299.3. [Q8L7D2-1]
DR AlphaFoldDB; Q8L7D2; -.
DR SMR; Q8L7D2; -.
DR STRING; 3702.AT5G59090.1; -.
DR MEROPS; S08.A20; -.
DR PaxDb; Q8L7D2; -.
DR PRIDE; Q8L7D2; -.
DR ProteomicsDB; 232900; -. [Q8L7D2-1]
DR EnsemblPlants; AT5G59090.1; AT5G59090.1; AT5G59090. [Q8L7D2-1]
DR GeneID; 836026; -.
DR Gramene; AT5G59090.1; AT5G59090.1; AT5G59090. [Q8L7D2-1]
DR KEGG; ath:AT5G59090; -.
DR Araport; AT5G59090; -.
DR TAIR; locus:2153291; AT5G59090.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR InParanoid; Q8L7D2; -.
DR OMA; KASMFEN; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q8L7D2; -.
DR PRO; PR:Q8L7D2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7D2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
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 Alternative splicing; Autocatalytic cleavage; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..110
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435249"
FT CHAIN 111..?
FT /note="Subtilisin-like protease SBT4.12"
FT /evidence="ECO:0000255"
FT /id="PRO_5004310879"
FT PROPEP ?..736
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435250"
FT DOMAIN 32..110
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 114..580
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 353..437
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 519
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 173
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 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 736 AA; 78097 MW; A6B8EED0850615C6 CRC64;
MANLAASTCL YSWLLVLLLS SVSAIIDEDT QVYIVYMGSL SSRADYIPTS DHMSILQQVT
GESSIEGRLV RSYKRSFNGF AARLTESERT LIAEIEGVVS VFPNKILQLH TTTSWDFMGV
KEGKNTKRNL AIESDTIIGV IDTGIWPESK SFSDKGFGPP PKKWKGVCSG GKNFTCNNKL
IGARDYTSEG TRDTSGHGTH TASTAAGNAV KDTSFFGIGN GTVRGGVPAS RIAAYKVCTD
SGCSSEALLS SFDDAIADGV DLITISIGFQ FPSIFEDDPI AIGAFHAMAK GILTVSSAGN
SGPKPTTVSH VAPWIFTVAA STTNRGFITK VVLGNGKTLA GRSVNAFDMK GKKYPLVYGK
SAASSACDAK TAALCAPACL NKSRVKGKIL VCGGPSGYKI AKSVGAIAII DKSPRPDVAF
THHLPASGLK AKDFKSLVSY IESQDSPQAA VLKTETIFNR TSPVIASFSS RGPNTIAVDI
LKPDITAPGV EILAAFSPNG EPSEDDTRRV KYSVFSGTSM ACPHVAGVAA YVKTFYPRWS
PSMIQSAIMT TAWPVKAKGR GIASTEFAYG AGHVDPMAAL NPGLVYELDK ADHIAFLCGM
NYTSKTLKII SGDTVKCSKK NKILPRNLNY PSMSAKLSGT DSTFSVTFNR TLTNVGTPNS
TYKSKVVAGH GSKLSIKVTP SVLYFKTVNE KQSFSVTVTG SDVDSEVPSS ANLIWSDGTH
NVRSPIVVYI MVVDEA
