SBT31_ARATH
ID SBT31_ARATH Reviewed; 764 AA.
AC F4JJH4; O81899;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Subtilisin-like protease SBT3.1 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 1 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.1 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.1 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At4g21323 {ECO:0000312|Araport:AT4G21323};
GN ORFNames=T6K22.50 {ECO:0000312|EMBL:CAA20197.1};
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|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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=AEE84440.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA20197.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g21320 has been split into 3 genes: At4g21320, At4g21323 and At4g21326.; Evidence={ECO:0000305};
CC Sequence=CAB79131.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g21320 has been split into 3 genes: At4g21320, At4g21323 and At4g21326.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL031187; CAA20197.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79131.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84440.1; ALT_SEQ; Genomic_DNA.
DR PIR; T05174; T05174.
DR RefSeq; NP_567624.1; NM_118251.2.
DR AlphaFoldDB; F4JJH4; -.
DR SMR; F4JJH4; -.
DR STRING; 3702.AT4G21323.1; -.
DR MEROPS; S08.A32; -.
DR PaxDb; F4JJH4; -.
DR PRIDE; F4JJH4; -.
DR ProteomicsDB; 226593; -.
DR GeneID; 827881; -.
DR KEGG; ath:AT4G21323; -.
DR Araport; AT4G21323; -.
DR TAIR; locus:505006503; AT4G21323.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR InParanoid; F4JJH4; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:F4JJH4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JJH4; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0009860; P:pollen tube growth; IEP:TAIR.
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 3: Inferred from homology;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT PROPEP 33..120
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435188"
FT CHAIN 121..?
FT /note="Subtilisin-like protease SBT3.1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435189"
FT PROPEP ?..764
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435190"
FT DOMAIN 41..116
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 124..610
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 230
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 541
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 764 AA; 82638 MW; B929C2230A4FA412 CRC64;
MIQTLKTDSS FRLCFAAIAF GFVFIMNGKL SSGTTPHEFP VYIFYLGERK HDDPNLVTQS
HLEILKSVLG SEEATNKSMV YSYHHGFSGF AAKLKPAEAE KLKKHPEVII LLENRKLGLQ
TTRTWDYLGQ FSTPTSSKSL LHETNMGSGA IIGVIDSGIW SESGSFDDDG YGPIPKHWKG
QCVSADQFSP ADCNKKLIGA KYYIDGLNAD LETSINSTTE YLSPRDHNGH GTQVSSTAAG
SFVSNMTLLG LSSGSIMRGG APKAHIAMYK ACWDVEGGMC SVADVWKAFD EAIHDGVDVL
SVSVGGSALK TLDVEIDIAI PALHAVNKGI PVVSPAGNEG SRSSSVINVS PWILTVAATT
LDRSFSTLIT LENNKTYLGQ SLYTGPEISF TDVICTGDHS NVDQITKGKV IMHFSMGPVR
PLTPDVVQKN GGIGLIYVRN PGDSRVECPV NFPCIYLDME VGSELYTYIQ TRSSMKIKIS
PYKTIIGESV ASKVAKSSAR GPSSFSPAIL KPDIAAPGLT LLTPRIPTDE DTREFVYSGT
SMATPVIAGI VALLKISHPN WSPAVIKSAL VTTAMKTDPY GERLTVDGGN YKVADAFDYG
GGLVNLEKAT DPGLVYDMDI NDYTHYLCSQ TLYTDKKVSA LTGNVNNKCP SSSSSILDLN
VPSITIPDLK GTVNVTRTVT NVGRVKSVYK PVIEAPFGFN VVVSPKKLKF NKTRNKLAFT
VTVSPGSHRV NTAFYFGSLT WSDKVHNVTI PISLRTRFID NFFL
