SBT37_ARATH
ID SBT37_ARATH Reviewed; 777 AA.
AC Q9SZY2; Q9ZSA9;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Subtilisin-like protease SBT3.7 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 7 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.7 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.7 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At4g10510 {ECO:0000312|Araport:AT4G10510};
GN ORFNames=F3H7.15 {ECO:0000312|EMBL:AAD03438.1},
GN F7L13.90 {ECO:0000312|EMBL:CAB40044.1};
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=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=AAD03438.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE82892.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF118222; AAD03438.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL049524; CAB40044.1; -; Genomic_DNA.
DR EMBL; AL161517; CAB78174.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82892.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; ANM66249.1; -; Genomic_DNA.
DR PIR; T04186; T04186.
DR RefSeq; NP_001328158.1; NM_001340673.1.
DR RefSeq; NP_567358.1; NM_117119.2.
DR AlphaFoldDB; Q9SZY2; -.
DR SMR; Q9SZY2; -.
DR STRING; 3702.AT4G10510.1; -.
DR MEROPS; S08.A49; -.
DR PaxDb; Q9SZY2; -.
DR PRIDE; Q9SZY2; -.
DR EnsemblPlants; AT4G10510.3; AT4G10510.3; AT4G10510.
DR GeneID; 826643; -.
DR Gramene; AT4G10510.3; AT4G10510.3; AT4G10510.
DR KEGG; ath:AT4G10510; -.
DR Araport; AT4G10510; -.
DR TAIR; locus:2127696; AT4G10510.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR InParanoid; Q9SZY2; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:Q9SZY2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZY2; 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: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 3: Inferred from homology;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..113
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435197"
FT CHAIN 114..?
FT /note="Subtilisin-like protease SBT3.7"
FT /id="PRO_0000435198"
FT PROPEP ?..777
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435199"
FT DOMAIN 34..111
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 117..624
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 386..481
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 555
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 777 AA; 83695 MW; A564B2E641A87DCF CRC64;
MRNHRTSIFV VLSLVIILNG QSGFLPRAGA ESKVHIVYLG EKQHDDPEFV TESHHRMLWS
LLGSKEEAHG SMVHSFRHGF SGFAAKLTES QAKKIADLPE VVHVIPDRFY KPATTRTWDY
LGLSPTNPKN LLNQTNMGEQ MIIGIIDSGV WPESEVFNDN EIGPVPSHWK GGCESGEDFN
SSHCNKKLIG AKYFINAFLA THESFNSSES LDFISPRGYN GHGTHVATIA GGSYVPNTSY
KGLAGGTVRG GAPRARIAVY KTCWYLDLDI AACSSADILK AMDEAIHDGV DVLSLSLGFE
PLYPETDVRD GIATGAFHAV LKGITVVCAA GNAGPAAQTV GNTAPWILTV AATTLDRSFV
TPMTLGNNKV ILGQAIYTGT EVGFTSLVYP ENPGNSNESF SGTCERLLIN SNRTMAGKVV
LCFTESPYSI SVTRAAHYVK RAGGLGVIIA GQPGNVLRPC LDDFPCVAVD YELGTYILFY
IRSNGSPVVK IQPSRTLIGQ PVGTKVASFS SRGPNPISAA ILKPDIAAPG VSILAATTTN
TTFNDRGFIF LSGTSMATPT ISGIVALLKA LHPDWSPAAI RSAIVTTAWR TDPFGEQIFA
EGSPRKPADP FDYGGGLVNP EKATKPGLVY DLGLEDYVLY MCSVGYNETS ISQLVGKGTV
CSYPKPSVLD FNLPSITIPN LKEEVTLPRT LTNVGPLESV YRVAVEPPLG TQVTVTPETL
VFNSTTKRVS FKVSVSTTHK INTGYYFGSL TWSDSLHNVT IPLSVRTQLL PYYYDEN
