ID SBT56_ARATH Reviewed; 791 AA.
AC Q9FK76;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JUL-2024, entry version 151.
DE RecName: Full=Subtilisin-like protease SBT5.6 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 5 member 6 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT5.6 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT5.6 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g45650 {ECO:0000312|Araport:AT5G45650};
GN ORFNames=MRA19.5 {ECO:0000312|EMBL:BAB09208.1};
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
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; AB012245; BAB09208.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95280.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70243.1; -; Genomic_DNA.
DR EMBL; AK118053; BAC42684.1; -; mRNA.
DR EMBL; BT005679; AAO64099.1; -; mRNA.
DR RefSeq; NP_001318744.1; NM_001344636.1.
DR RefSeq; NP_199378.1; NM_123933.3.
DR AlphaFoldDB; Q9FK76; -.
DR SMR; Q9FK76; -.
DR STRING; 3702.Q9FK76; -.
DR MEROPS; S08.082; -.
DR GlyCosmos; Q9FK76; 6 sites, No reported glycans.
DR iPTMnet; Q9FK76; -.
DR PaxDb; 3702-AT5G45650-1; -.
DR ProteomicsDB; 232930; -.
DR EnsemblPlants; AT5G45650.1; AT5G45650.1; AT5G45650.
DR EnsemblPlants; AT5G45650.2; AT5G45650.2; AT5G45650.
DR GeneID; 834605; -.
DR Gramene; AT5G45650.1; AT5G45650.1; AT5G45650.
DR Gramene; AT5G45650.2; AT5G45650.2; AT5G45650.
DR KEGG; ath:AT5G45650; -.
DR Araport; AT5G45650; -.
DR TAIR; AT5G45650; -.
DR eggNOG; ENOG502QRC5; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; Q9FK76; -.
DR OMA; EEHHHSY; -.
DR OrthoDB; 11910at2759; -.
DR PhylomeDB; Q9FK76; -.
DR PRO; PR:Q9FK76; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK76; 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; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF562; SUBTILISIN-LIKE PROTEASE SBT5.5-RELATED; 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; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..108
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435259"
FT CHAIN 109..?
FT /note="Subtilisin-like protease SBT5.6"
FT /evidence="ECO:0000255"
FT /id="PRO_5004325448"
FT PROPEP ?..791
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435260"
FT DOMAIN 26..104
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 134..645
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 400..494
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 578
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
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 666
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 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 791 AA; 85146 MW; E3A11A3ECD036D41 CRC64;
MKKLTSLFPL LFLIPLLASC AEEKQVYIVY FGEHKGDKAF HEIEEHHHSY LQSVKESEED
ARASLLYSYK HSINGFAAEL TPDQASKLEK LAEVVSVFKS HPRKYEAHTT RSWEFVGLEE
EETDSDVPRR KNDADDRFRV GRNFLKKAKH GDGIIVGVLD SGVWPESKSF NDKGMGPVPK
SWKGICQTGV AFNSSHCNRK IIGARYYVKG YERYYGAFNA TANKDFLSPR DPDGHGSHTA
STAVGRRVLG ASALGGFAKG SASGGAPLAR LAIYKACWAK PNAEKVEGNI CLEEDMLAAI
DDAIADGVHV ISISIGTTEP FPFTQDGIAM GALHAVKRNI VVAASAGNSG PKPGTLSNLA
PWIITVGAST LDRAFVGGLV LGNGYTIKTD SITAFKMDKF APLVYASNVV VPGIALNETS
QCLPNSLKPE LVSGKVVLCL RGAGSRIGKG MEVKRAGGAG MILGNIAANG NEVPSDSHFV
PTAGVTPTVV DKILEYIKTD KNPKAFIKPG KTVYKYQAAP SMTGFSSRGP NVVDPNILKP
DITAPGLYIL AAWSGADSPS KMSVDQRVAG YNIYSGTSMS CPHVAGAIAL LKAIHPKWSS
AAIRSALMTT AWMTNDKKKP IQDTTGLPAN PFALGSGHFR PTKAADPGLV YDASYRAYLL
YGCSVNITNI DPTFKCPSKI PPGYNHNYPS IAVPNLKKTV TVKRTVTNVG TGNSTSTYLF
SVKPPSGISV KAIPNILSFN RIGQKQRFKI VIKPLKNQVM NATEKGQYQF GWFSWTDKVH
VVRSPIAVSL A
//
