SBT21_ARATH
ID SBT21_ARATH Reviewed; 832 AA.
AC Q9SA75;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Subtilisin-like protease SBT2.1 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 2 member 1 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT2.1 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT2.1 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At1g30600 {ECO:0000312|Araport:AT1G30600};
GN ORFNames=T5I8.5 {ECO:0000312|EMBL:AAD25747.1};
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 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 -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AC007060; AAD25747.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31248.1; -; Genomic_DNA.
DR EMBL; AY072142; AAL59964.1; -; mRNA.
DR EMBL; AY096410; AAM20050.1; -; mRNA.
DR PIR; C86431; C86431.
DR RefSeq; NP_174348.1; NM_102797.4.
DR AlphaFoldDB; Q9SA75; -.
DR SMR; Q9SA75; -.
DR STRING; 3702.AT1G30600.1; -.
DR MEROPS; S08.A03; -.
DR PaxDb; Q9SA75; -.
DR PRIDE; Q9SA75; -.
DR ProteomicsDB; 232883; -.
DR EnsemblPlants; AT1G30600.1; AT1G30600.1; AT1G30600.
DR GeneID; 839940; -.
DR Gramene; AT1G30600.1; AT1G30600.1; AT1G30600.
DR KEGG; ath:AT1G30600; -.
DR Araport; AT1G30600; -.
DR TAIR; locus:2204619; AT1G30600.
DR eggNOG; ENOG502QSVR; Eukaryota.
DR HOGENOM; CLU_000625_3_1_1; -.
DR InParanoid; Q9SA75; -.
DR OMA; SHFFIAM; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9SA75; -.
DR PRO; PR:Q9SA75; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA75; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; 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; 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..24
FT /evidence="ECO:0000255"
FT PROPEP 25..138
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q9MAP7"
FT /id="PRO_0000435180"
FT CHAIN 139..?
FT /note="Subtilisin-like protease SBT2.1"
FT /id="PRO_5004332544"
FT PROPEP ?..832
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435181"
FT DOMAIN 36..136
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 145..684
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 408..503
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 247
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 609
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 832 AA; 88545 MW; F7AEFD2B1DDEE630 CRC64;
MDESSLVRFV FLLCLVSSSV FCLAESDQNA TVSSAVYIVT LKDRPSVHFS GRESSDSKHS
LTATSSQIYR TLNRSASIIR VHDSLLRNVL RKENYLKLYS YHYLINGFSA VLTRKQADRL
AAREEVENVV LDFLVEKATT HTPQFLGLPR GAWLRDGGSE YAGEGVVIGF IDTGIDPTHP
SFSDKISGHT YSVPPHFTGV CEVTIGFPPG SCNRKLIGAR HFAESALSRG VLNSSQDDAS
PFDGEGHGTH TASVAAGNHG IPVVVAGHRL GNASGMAPRA HIAIYKALYK RFGGFAADII
AAIDQAAQDG VDIINLSITP NRRPPGIATF FNPIDMALLS AVKAGIFVVQ AAGNTGPAPK
SMSSFSPWIF TVGATSHDRV YSNSIILGNN VTIPGVGLAS GTRIMHKLVL ATHALRNGTT
VMDAIYVGEC QDSSSFDQKL VQGKILVCSY TVRFILGVST IKQALLTAKN LTAAGLVFYI
DPSATGFQMT SSPMDIPGIL ISSPQDSQAL LRYYNSSLLR ENGSGKIVGS ASVAKIVGGM
RPTYGITAPK VMYFSARGPD PEDDSFVDAD IMKPNLVAPG NAIWGAWSPL GIGTNDFQGE
RFAMESGTSM SAPHVTGIAA LIKQKFPHFT PAAIASALST TASLSDRKGE HIMAQRTVLN
PDISQSPATP FDMGSGFVNA TAALDPGLIF DIGYNEYMKF LCGINGSSPV VLNYTGESCS
SYNSSLAASD LNLPSVTIAK LVGTRAVLRW VTNIATTATN ETYIVGWMAP DSVSVKVSPA
KFTIGNGQTR VLSLVFRAMK NVSMASFGRI GLFGDRGHVV NIPVAVIYKI AV
