SBT4B_ARATH
ID SBT4B_ARATH Reviewed; 736 AA.
AC Q9FIG1; F4KHS8; Q84WF9;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Subtilisin-like protease SBT4.11 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 4 member 11 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT4.11 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT4.11 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g59130 {ECO:0000312|Araport:AT5G59130};
GN ORFNames=MNC17.4 {ECO:0000312|EMBL:BAB09759.1};
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] (ISOFORM 2).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist. {ECO:0000305};
CC Name=1;
CC IsoId=Q9FIG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FIG1-2; Sequence=VSP_058032;
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=AED97146.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB09759.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016890; BAB09759.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97146.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; ANM68397.1; -; Genomic_DNA.
DR EMBL; BT003861; AAO41911.1; -; mRNA.
DR RefSeq; NP_001330156.1; NM_001345336.1.
DR RefSeq; NP_001330157.1; NM_001345337.1. [Q9FIG1-1]
DR RefSeq; NP_568899.1; NM_125303.2.
DR AlphaFoldDB; Q9FIG1; -.
DR SMR; Q9FIG1; -.
DR STRING; 3702.AT5G59130.1; -.
DR MEROPS; S08.A15; -.
DR PaxDb; Q9FIG1; -.
DR EnsemblPlants; AT5G59130.4; AT5G59130.4; AT5G59130. [Q9FIG1-1]
DR GeneID; 836031; -.
DR Gramene; AT5G59130.4; AT5G59130.4; AT5G59130. [Q9FIG1-1]
DR KEGG; ath:AT5G59130; -.
DR Araport; AT5G59130; -.
DR TAIR; locus:2168444; AT5G59130.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:Q9FIG1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIG1; 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 Alternative splicing; Autocatalytic cleavage; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..113
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435246"
FT CHAIN 114..?
FT /note="Subtilisin-like protease SBT4.11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435247"
FT PROPEP ?..736
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435248"
FT DOMAIN 35..112
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 117..579
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 355..437
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 200
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 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 215
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 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 109..136
FT /note="Missing (in isoform 2)"
FT /id="VSP_058032"
SQ SEQUENCE 736 AA; 78895 MW; 6FD447154BBE651B CRC64;
MAKRGAFSSF HSFLIVLLFL NSVLAVTHGH QDKQVYIVYM GSLPSRADYT PMSHHMNILQ
EVARESSIEG RLVRSYKRSF NGFVARLTES ERERVADMEG VVSVFPNKKL KLQTSASWDF
MGLKEGKGTK RNPSVESDTI IGVFDGGIWP ESESFSDKGF GPPPKKWKGI CAGGKNFTCN
NKLIGARHYS PGDARDSTGH GTHTASIAAG NAVANTSFFG IGNGTVRGAV PASRIAVYRV
CAGECRDDAI LSAFDDAISD GVDIITISIG DINVYPFEKD PIAIGAFHAM SKGILTVNAA
GNTGPDTASI TSLAPWLLTV AASTANREFV SKVVLGDGKT LVGKSVNGFD LKGKKFPLVY
GKSAALSLSQ AKCAEDCTPE CLDASLVKGK ILVCNRFLPY VAYTKRAVAA IFEDGSDWAQ
INGLPVSGLQ KDDFESVLSY FKSEKSPEAA VLKSESIFYQ TAPKILSFSS RGPNIIVADI
LKPDITAPGL EILAANSLRA SPFYDTAYVK YSVESGTSMS CPHAAGVAAY VKTFHPQWSP
SMIKSAIMTT AWSMNASQSG YASTEFAYGA GHVDPIAATN PGLVYEITKT DYFAFLCGMN
YNKTTVKLIS GEAVTCSEKI SPRNLNYPSM SAKLSGSNIS FIVTFNRTVT NVGTPNSTYK
SKVVLNHGSK LNVKVSPSVL SMKSMNEKQS FTVTVSASEL HSELPSSANL IWSDGTHNVR
SPIVVYTGDF SQPSSS
