SBT34_ARATH
ID SBT34_ARATH Reviewed; 773 AA.
AC F4HPF1; Q9MAP6;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Subtilisin-like protease SBT3.4 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 3 member 4 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.4 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.4 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At1g32950 {ECO:0000312|Araport:AT1G32950};
GN ORFNames=F9L11.12 {ECO:0000312|EMBL:AAF31277.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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=AAF31277.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006424; AAF31277.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31543.1; -; Genomic_DNA.
DR PIR; B86454; B86454.
DR RefSeq; NP_564413.2; NM_103028.3.
DR AlphaFoldDB; F4HPF1; -.
DR SMR; F4HPF1; -.
DR STRING; 3702.AT1G32950.1; -.
DR MEROPS; S08.A27; -.
DR PaxDb; F4HPF1; -.
DR PRIDE; F4HPF1; -.
DR EnsemblPlants; AT1G32950.1; AT1G32950.1; AT1G32950.
DR GeneID; 840189; -.
DR Gramene; AT1G32950.1; AT1G32950.1; AT1G32950.
DR KEGG; ath:AT1G32950; -.
DR Araport; AT1G32950; -.
DR TAIR; locus:2037915; AT1G32950.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR InParanoid; F4HPF1; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:F4HPF1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HPF1; 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; 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..23
FT /evidence="ECO:0000255"
FT PROPEP 24..108
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435193"
FT CHAIN 109..?
FT /note="Subtilisin-like protease SBT3.4"
FT /id="PRO_5003309464"
FT PROPEP ?..773
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435194"
FT DOMAIN 29..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 112..620
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 382..474
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 551
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 773 AA; 82445 MW; 9AF89066D81FB870 CRC64;
MRNFRSSVLV VLSLIIVLNV ARASAKSKVH IVYLGEKQHD DPKFVTESHH QMLSSLLGSK
DDAHESMVYS YRHGFSGFAA KLTKSQAKKI ADSPEVIHVI PDSYYELATT RIWDYLGPSA
DNSKNLVSDT NMGDQTIIGV IDTGVWPESE SFNDYGVGPV PSHWKGGCEP GENFISTNCN
RKLIGAKYFI NGFLAENQFN ATESPDYISA RDFDGHGTHV ASIAGGSFVP NVSYKGLGRG
TLRGGAPRAR IAMYKACWYI NELDGVTCSF SDIMKAIDEA IHDGVDVLSI SLGGRVPLNS
ETDLRDGIAT GAFHAVAKGI VVVCAGGNAG PSSQTVVNTA PWILTVAATT LDRSFATPII
LGNNQVILGQ AMYIGPELGF TSLVYPEDPG NSIDTFSGVC ESLNLNSNRT MAGKVVLCFT
TARDFTVVST AASIVKAAGG LGLIIARNPG YNLAPCSDDF PCVAIDNELG TDILFYIRYT
GSPVVKIQPS RTLVGEPVGT KVATFSSRGP NSISPAILKP DIAAPGVSIL AATSPNDTLN
AGGFVMRSGT SMAAPVISGV IALLKSLHPD WSPAAFRSAI VTTAWRTDPF GEQIAAESSS
LKVPDPFDYG GGLVNPEKAA EPGLILDMDS QDYVLYLCSA GYNDSSISRL VGKVTVCSNP
KPSVLDINLP SITIPNLKDE VTLTRTVTNV GPVDSVYKVL VEPPLGIQVV VTPETLVFNS
KTKSVSFTVI VSTTHKINTG FYFGSLTWTD SIHNVVIPVS VRTQILQNYY DEN
