SBT18_ARATH
ID SBT18_ARATH Reviewed; 754 AA.
AC Q9ZUF6;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Subtilisin-like protease SBT1.8 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 1 member 8 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT1.8 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT1.8 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At2g05920 {ECO:0000312|Araport:AT2G05920};
GN ORFNames=T6P5.12 {ECO:0000312|EMBL:AAC95169.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AC005970; AAC95169.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05985.1; -; Genomic_DNA.
DR EMBL; AY035090; AAK59595.1; -; mRNA.
DR EMBL; AY142613; AAN13182.1; -; mRNA.
DR PIR; A84473; A84473.
DR RefSeq; NP_565330.1; NM_126605.4.
DR AlphaFoldDB; Q9ZUF6; -.
DR SMR; Q9ZUF6; -.
DR STRING; 3702.AT2G05920.1; -.
DR MEROPS; S08.A24; -.
DR PaxDb; Q9ZUF6; -.
DR PRIDE; Q9ZUF6; -.
DR ProteomicsDB; 232845; -.
DR EnsemblPlants; AT2G05920.1; AT2G05920.1; AT2G05920.
DR GeneID; 815145; -.
DR Gramene; AT2G05920.1; AT2G05920.1; AT2G05920.
DR KEGG; ath:AT2G05920; -.
DR Araport; AT2G05920; -.
DR TAIR; locus:2064696; AT2G05920.
DR eggNOG; ENOG502QRTY; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; Q9ZUF6; -.
DR OMA; SGPYYRD; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9ZUF6; -.
DR PRO; PR:Q9ZUF6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUF6; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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; IPR003137; PA_domain.
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; 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; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..102
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q9MAP7"
FT /id="PRO_0000435176"
FT CHAIN 103..?
FT /note="Subtilisin-like protease SBT1.8"
FT /id="PRO_5004337788"
FT PROPEP ?..754
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435177"
FT DOMAIN 29..102
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 98..604
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 367..452
FT /note="PA"
FT /evidence="ECO:0000255"
FT REGION 191..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 536
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 754 AA; 80015 MW; F8CC63F11578CEF7 CRC64;
MASSSSSSSS ITIITTFLFL LLHTTAKKTY IIRVNHSDKP ESFLTHHDWY TSQLNSESSL
LYTYTTSFHG FSAYLDSTEA DSLLSSSNSI LDIFEDPLYT LHTTRTPEFL GLNSEFGVHD
LGSSSNGVII GVLDTGVWPE SRSFDDTDMP EIPSKWKGEC ESGSDFDSKL CNKKLIGARS
FSKGFQMASG GGFSSKRESV SPRDVDGHGT HTSTTAAGSA VRNASFLGYA AGTARGMATR
ARVATYKVCW STGCFGSDIL AAMDRAILDG VDVLSLSLGG GSAPYYRDTI AIGAFSAMER
GVFVSCSAGN SGPTRASVAN VAPWVMTVGA GTLDRDFPAF ANLGNGKRLT GVSLYSGVGM
GTKPLELVYN KGNSSSSNLC LPGSLDSSIV RGKIVVCDRG VNARVEKGAV VRDAGGLGMI
MANTAASGEE LVADSHLLPA IAVGKKTGDL LREYVKSDSK PTALLVFKGT VLDVKPSPVV
AAFSSRGPNT VTPEILKPDV IGPGVNILAG WSDAIGPTGL DKDSRRTQFN IMSGTSMSCP
HISGLAGLLK AAHPEWSPSA IKSALMTTAY VLDNTNAPLH DAADNSLSNP YAHGSGHVDP
QKALSPGLVY DISTEEYIRF LCSLDYTVDH IVAIVKRPSV NCSKKFSDPG QLNYPSFSVL
FGGKRVVRYT REVTNVGAAS SVYKVTVNGA PSVGISVKPS KLSFKSVGEK KRYTVTFVSK
KGVSMTNKAE FGSITWSNPQ HEVRSPVAFS WNRF