SBT3C_ARATH
ID SBT3C_ARATH Reviewed; 754 AA.
AC F4JJH5; A7Y5V8; O81899;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Subtilisin-like protease SBT3.12 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 12 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.12 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.12 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At4g21326 {ECO:0000312|Araport:AT4G21326};
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-754.
RC STRAIN=cv. Cvi-0;
RX PubMed=17656687; DOI=10.1126/science.1143153;
RA Tang C., Toomajian C., Sherman-Broyles S., Plagnol V., Guo Y.-L., Hu T.T.,
RA Clark R.M., Nasrallah J.B., Weigel D., Nordborg M.;
RT "The evolution of selfing in Arabidopsis thaliana.";
RL Science 317:1070-1072(2007).
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=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};
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DR EMBL; AL031187; CAA20197.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79131.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EF637083; ABV21208.1; -; Genomic_DNA.
DR PIR; T05174; T05174.
DR AlphaFoldDB; F4JJH5; -.
DR SMR; F4JJH5; -.
DR STRING; 3702.AT4G21326.1; -.
DR MEROPS; S08.A30; -.
DR MEROPS; S08.A32; -.
DR PaxDb; F4JJH5; -.
DR PeptideAtlas; F4JJH5; -.
DR PRIDE; F4JJH5; -.
DR ProteomicsDB; 232690; -.
DR Araport; AT4G21326; -.
DR TAIR; locus:505006504; AT4G21326.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_369061_0_0_1; -.
DR InParanoid; F4JJH5; -.
DR PhylomeDB; F4JJH5; -.
DR PRO; PR:F4JJH5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JJH5; 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; IPR041469; Subtilisin-like_FN3.
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..28
FT /evidence="ECO:0000255"
FT PROPEP 29..117
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435208"
FT CHAIN 118..?
FT /note="Subtilisin-like protease SBT3.12"
FT /evidence="ECO:0000255"
FT /id="PRO_5003311531"
FT PROPEP ?..754
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435209"
FT DOMAIN 39..116
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 121..606
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 537
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 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 167
FT /note="E -> G (in Ref. 3; ABV21208)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="G -> S (in Ref. 3; ABV21208)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="G -> D (in Ref. 3; ABV21208)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="I -> T (in Ref. 3; ABV21208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 81507 MW; 51D01AFA87832E15 CRC64;
MGIVKGRSRA GLFIGFLFIV NVGFCVFAQE SSNEERKIYV VHLGVRRHDD SELVSESHQR
MLESVFESAE AARESIVYNY HHGFSGFAAR LTDSQAKQLS DRPDVFSVAP NRKVELQSTR
IYDYLGLSPS FPSGVLHESN MGSDLVIGFL DSGVWPESPA YNDEGLEPIP KHWKGKCVAG
EDFDPAKHCN KKLVGAKYFT DGFDENNSGI SEEDFMSPRG YRGHGTMVSS IAASSFVPNV
SYGGLAPGVM RGAAPKARIA MYKIVWDRAL LMSSTATMVK AFDEAINDGV DVLSISLASA
APFRPIDSIT GDLELGSFHA VMKGIPVIAG ASNTGPEAYT VANVFPWMLT VAATNIDRTF
YADMTFGNNI TIIGQAQYTG KEVSAGLVYI EHYKTDTSGM LGKVVLTFVK EDWEMASALA
TTTINKAAGL IVARSGDYQS DIVYNQPFIY VDYEVGAKIL RYIRSSSSPT IKISTGKTLV
GRPIATQVCG FSSRGPNGLS PAILKPDIAA PGVTILGATS QAYPDSFGGY FLGTGTSYAT
PVVAGLVVLL KALHPDWSPA ALKSAIMTTA WKTDPSGEPI FAEGEPRKLA DPFDYGAGLV
NAERAKDPGL VYDMNIDDYI HYFCATGYND TSITIITGKP TKCSSPLPSI LDLNYPAITI
PDLEEEVTVT RTVTNVGPVD SVYRAVVEPP RGVEIVVEPE TLVFCSNTKK LGFKVRVSSS
HKSNTGFFFG SFTWTDGTRN VTIPLSVRIR VLNP