SBT3B_ARATH
ID SBT3B_ARATH Reviewed; 762 AA.
AC Q1PDX5; Q9LYH9;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Subtilisin-like protease SBT3.11 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 11 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.11 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.11 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g11940 {ECO:0000312|Araport:AT5G11940};
GN ORFNames=F14F18.110 {ECO:0000312|EMBL:CAB87667.1};
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:ABE66153.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87667.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163812; CAB87667.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91742.1; -; Genomic_DNA.
DR EMBL; DQ446943; ABE66153.1; -; mRNA.
DR PIR; T48553; T48553.
DR RefSeq; NP_568255.1; NM_121232.1.
DR AlphaFoldDB; Q1PDX5; -.
DR SMR; Q1PDX5; -.
DR STRING; 3702.AT5G11940.1; -.
DR MEROPS; S08.A37; -.
DR PaxDb; Q1PDX5; -.
DR PRIDE; Q1PDX5; -.
DR ProteomicsDB; 232797; -.
DR EnsemblPlants; AT5G11940.1; AT5G11940.1; AT5G11940.
DR GeneID; 831067; -.
DR Gramene; AT5G11940.1; AT5G11940.1; AT5G11940.
DR KEGG; ath:AT5G11940; -.
DR Araport; AT5G11940; -.
DR TAIR; locus:2143014; AT5G11940.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR InParanoid; Q1PDX5; -.
DR OMA; AYTVQNI; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q1PDX5; -.
DR PRO; PR:Q1PDX5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q1PDX5; 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; IPR022398; Peptidase_S8_His-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; PS00137; SUBTILASE_HIS; 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..16
FT /evidence="ECO:0000255"
FT PROPEP 17..116
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435206"
FT CHAIN 117..?
FT /note="Subtilisin-like protease SBT3.11"
FT /id="PRO_5004195439"
FT PROPEP ?..762
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435207"
FT DOMAIN 37..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 120..609
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 540
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 762 AA; 82927 MW; 5577CA566DF7CB4E CRC64;
MMSSIVSWWF FWVISAVCIL KVEFNIVEGG AYEETKVHIV YLGEKEHNDP ELVTSSHLRM
LESLLGSKKD ASESIVHSYR NGFSGFAAHL TDSQAEQISE HPDVVQVTPN TFYELQTTRT
FDYLGLSHST PKGLLHEAKM GEDIIIGVLD SGVWPESQSF NDKGLGPIPK RWKGMCVDGE
DFDSKKHCNK KLIGARYYMD SLFRRNKTDS GIPDTEYMSA RESLPHGTHV ASTAGGSFVS
NVSDNGFGVG TIRGGAPRAR IAVYKVCWQR VDRTCASADI IKAMDDAIAD GVDLITISIG
RPNPVLTEVD VYNQISYGAF HAVAKGIPVL SAGGNFGPGA YTVQNIAPWI ITVAATTLDR
WYPTPLTLGN NVTLMARTPY KGNEIQGDLM FVYSPDEMTS AAKGKVVLTF TTGSEESQAG
YVTKLFQVEA KSVIIAAKRN DVIKVSEGLP IIMVDYEHGS TIWKYLSITR MPTIKISSAI
ALNGRLVATK VADFSGRGPN SISPYVLKPD VAAPGVAIVA ASTPESMGTE EGFAIQSGTS
MSTPVVAGLV ALLRAVHPDW SPAALKSALI TTASTTDPYG EPIFSEGMTR KLADPFDFGG
GLVNPNKAAD PGLVYDISAE DYRLFLCASH YDEKQITKIS KTHTPYRCPS PKPSMLDLNL
PSITIPFLKE DVTLTRTVTN VGPVDSVYKL IVEPPLGVKI SVTPNTLLFN SNVKILSYKV
TVSTTHKSNS IYYFGSLTWT DGSHKVTIPL SVRTQMLMYF DQ
