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Database: UniProt
Entry: SBT26_ARATH
LinkDB: SBT26_ARATH
Original site: SBT26_ARATH 
ID   SBT26_ARATH             Reviewed;         816 AA.
AC   Q9SZV5;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAY-2019, entry version 158.
DE   RecName: Full=Subtilisin-like protease SBT2.6 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 2 member 6 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT2.6 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT2.6 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At4g30020 {ECO:0000312|Araport:AT4G30020};
GN   ORFNames=F6G3.50 {ECO:0000312|EMBL:CAB43837.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
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.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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
RT   of the 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}.
DR   EMBL; AL078464; CAB43837.1; -; Genomic_DNA.
DR   EMBL; AL161576; CAB80995.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85709.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66536.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66537.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66538.1; -; Genomic_DNA.
DR   EMBL; AY139780; AAM98098.1; -; mRNA.
DR   EMBL; BT005822; AAO64757.1; -; mRNA.
DR   EMBL; AK226227; BAE98391.1; -; mRNA.
DR   PIR; T08978; T08978.
DR   RefSeq; NP_001328423.1; NM_001341988.1.
DR   RefSeq; NP_001328424.1; NM_001341989.1.
DR   RefSeq; NP_001328425.1; NM_001341990.1.
DR   RefSeq; NP_567839.1; NM_119148.4.
DR   SMR; Q9SZV5; -.
DR   STRING; 3702.AT4G30020.1; -.
DR   PaxDb; Q9SZV5; -.
DR   PRIDE; Q9SZV5; -.
DR   EnsemblPlants; AT4G30020.1; AT4G30020.1; AT4G30020.
DR   EnsemblPlants; AT4G30020.2; AT4G30020.2; AT4G30020.
DR   EnsemblPlants; AT4G30020.3; AT4G30020.3; AT4G30020.
DR   EnsemblPlants; AT4G30020.4; AT4G30020.4; AT4G30020.
DR   GeneID; 829125; -.
DR   Gramene; AT4G30020.1; AT4G30020.1; AT4G30020.
DR   Gramene; AT4G30020.2; AT4G30020.2; AT4G30020.
DR   Gramene; AT4G30020.3; AT4G30020.3; AT4G30020.
DR   Gramene; AT4G30020.4; AT4G30020.4; AT4G30020.
DR   KEGG; ath:AT4G30020; -.
DR   Araport; AT4G30020; -.
DR   TAIR; locus:2126485; AT4G30020.
DR   eggNOG; ENOG410IJRX; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   HOGENOM; HOG000238262; -.
DR   InParanoid; Q9SZV5; -.
DR   OMA; MLFKEGS; -.
DR   OrthoDB; 337164at2759; -.
DR   PhylomeDB; Q9SZV5; -.
DR   PRO; PR:Q9SZV5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SZV5; 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   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; IPR023827; Peptidase_S8_Asp-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; 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; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   2: Evidence at transcript level;
KW   Autocatalytic cleavage; Complete proteome; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   PROPEP       20    126       Activation peptide.
FT                                {ECO:0000250|UniProtKB:Q9MAP7}.
FT                                /FTId=PRO_0000435186.
FT   CHAIN       127      ?       Subtilisin-like protease SBT2.6.
FT                                /FTId=PRO_5004337366.
FT   PROPEP        ?    816       {ECO:0000250|UniProtKB:Q39547}.
FT                                /FTId=PRO_0000435187.
FT   DOMAIN       22    124       Inhibitor I9. {ECO:0000255}.
FT   DOMAIN      151    635       Peptidase S8. {ECO:0000255}.
FT   DOMAIN      418    492       PA. {ECO:0000255}.
FT   ACT_SITE    160    160       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10080}.
FT   ACT_SITE    235    235       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10081}.
FT   ACT_SITE    597    597       Charge relay system.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10082}.
FT   CARBOHYD    504    504       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    578    578       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    702    702       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
SQ   SEQUENCE   816 AA;  87505 MW;  6C77ECBC1F5D9B30 CRC64;
     MDIGCKVLVF FTCFLTVTAE IYIVTMEGEP IISYKGGDNG FEATAVESDE KIDTTSELVT
     SYARHLERKH DMLLGMLFVE GSYKKLYSYK HLINGFAAHV SPDQAEMLRR APGVKSVDRD
     WKVRKLTTHT PQFLGLPTDV WPTGGGYDRA GEDIVIGFID SGIFPHHPSF ASHHTTVPYG
     PHPSYKGKCE EDPHTKISFC NGKIIGAQHF AEAAKAAGAF NPDIDFASPM DGDGHGSHTA
     AIAAGNNGIP VRMHGYEFGK ASGMAPRARI AVYKALYRLF GGFVADVVAA IDQAVHDGVD
     ILSLSVGPNS PPATTKTTFL NPFDATLLGA VKAGVFVAQA AGNGGPFPKT LVSYSPWITT
     VAAAIDDRRY KNHLTLGNGK MLAGIGLSPS TRPHRSYKMV SANDVLLGSS GMKYNPSDCQ
     KPEVLNKKLV EGNILLCGYS FNFVAGSASI KKVAETAKHL GAAGFVLVVE NVSPGTKFDP
     VPSCIPGILI TDVSKSMDLI DYYNVTTSRD WMGRVKDFKA EGSIGDGLEP ILHKSAPEVA
     LFSARGPNTK DFSFQDADLL KPDILAPGSL IWSAWSANGT DEANYIGEGF ALISGTSMAA
     PHIAGIAALV KQKHPQWSPA AIKSALMTTS TVIDRAGRPL QAQQYSETET VTLVKATPFD
     YGSGHVNPSA ALDPGLIFDA GYEDYIGFLC TTPGIDAHEI KNFTNTPCNF KMVHPSNFNT
     PSIAISHLVR TQTVTRRVTN VAEEEETYTI TSRMEPAIAI EVSPPAMTVR AGASRTFSVT
     LTVRSVTGAY SFGQVTLKGS RGHKVTLPVV AMGQRR
//
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