SBT35_ARATH
ID SBT35_ARATH Reviewed; 774 AA.
AC Q9MAP7;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Subtilisin-like protease SBT3.5 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Subtilase subfamily 3 member 5 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT3.5 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT3.5 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At1g32940 {ECO:0000312|Araport:AT1G32940};
GN ORFNames=F9L11.11 {ECO:0000312|EMBL:AAF31278.1};
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=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 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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24665109; DOI=10.1093/aob/mcu035;
RA Senechal F., Graff L., Surcouf O., Marcelo P., Rayon C., Bouton S.,
RA Mareck A., Mouille G., Stintzi A., Hoefte H., Lerouge P., Schaller A.,
RA Pelloux J.;
RT "Arabidopsis PECTIN METHYLESTERASE17 is co-expressed with and processed by
RT SBT3.5, a subtilisin-like serine protease.";
RL Ann. Bot. 114:1161-1175(2014).
CC -!- FUNCTION: Serine protease that cleaves the pectin methylesterase 17
CC (PME17) protein to release the PME17 mature form in the apoplasm.
CC {ECO:0000269|PubMed:24665109}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:24665109}. Note=Identified in cell-wall-enriched
CC root protein extracts. {ECO:0000269|PubMed:24665109}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flower buds,
CC developing siliques and mature seeds. {ECO:0000269|PubMed:24665109}.
CC -!- DISRUPTION PHENOTYPE: Transient delay during the first day of seed
CC germination and increased length of the primary root.
CC {ECO:0000269|PubMed:24665109}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; AC006424; AAF31278.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31542.1; -; Genomic_DNA.
DR EMBL; AY074326; AAL67022.1; -; mRNA.
DR EMBL; BT006147; AAP04132.1; -; mRNA.
DR PIR; A86454; A86454.
DR RefSeq; NP_564412.1; NM_103027.3.
DR AlphaFoldDB; Q9MAP7; -.
DR SMR; Q9MAP7; -.
DR STRING; 3702.AT1G32940.1; -.
DR MEROPS; S08.A36; -.
DR PaxDb; Q9MAP7; -.
DR PRIDE; Q9MAP7; -.
DR ProteomicsDB; 232958; -.
DR EnsemblPlants; AT1G32940.1; AT1G32940.1; AT1G32940.
DR GeneID; 840188; -.
DR Gramene; AT1G32940.1; AT1G32940.1; AT1G32940.
DR KEGG; ath:AT1G32940; -.
DR Araport; AT1G32940; -.
DR TAIR; locus:2037895; AT1G32940.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9MAP7; -.
DR PRO; PR:Q9MAP7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAP7; baseline and differential.
DR Genevisible; Q9MAP7; AT.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; 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; IPR003137; PA_domain.
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; PF02225; PA; 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 1: Evidence at protein level;
KW Cell wall; Glycoprotein; Growth regulation; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..108
FT /note="Removed in mature form"
FT /evidence="ECO:0000303|PubMed:24665109"
FT /id="PRO_0000430829"
FT CHAIN 109..774
FT /note="Subtilisin-like protease SBT3.5"
FT /evidence="ECO:0000303|PubMed:24665109"
FT /id="PRO_0000430830"
FT DOMAIN 29..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 112..621
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 383..478
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 217
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 552
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 755
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 774 AA; 82912 MW; E42D972624B38A09 CRC64;
MRNCRVLLVL VLSLVIVLNV VRASDESKVH IVYLGEKQHD DPEFVSESHH QMLSSLLGSK
VDAHESMVYS YRHGFSGFAA KLTESQAKKL ADSPEVVHVM ADSFYELATT RTWDYLGLSV
ANPNNLLNDT NMGDQVIIGF IDTGVWPESE SFNDNGVGPI PSHWKGGCES GEKFISTNCN
RKLIGAKYFI NGFLAENEGF NTTESRDYIS ARDFIGHGTH TASIAGGSFV PNISYKGLAG
GNLRGGAPRA RIAIYKACWY VDQLGAVACS SSDILKAMDE SMHDGVDVLS LSLGAQIPLY
PETDLRDRIA TGAFHAVAKG IIVVCAGGNS GPAAQTVLNT APWIITVAAT TLDRSFPTPI
TLGNRKVILG QALYTGQELG FTSLVYPENA GFTNETFSGV CERLNLNPNR TMAGKVVLCF
TTNTLFTAVS RAASYVKAAG GLGVIIARNP GYNLTPCRDD FPCVAIDYEL GTDVLLYIRS
TRSPVVKIQP SRTLVGQPVG TKVATFSSRG PNSISPAILK PDIGAPGVSI LAATSPDSNS
SVGGFDILAG TSMAAPVVAG VVALLKALHP NWSPAAFRSA IVTTAWRTDP FGEQIFAEGS
SRKVADPFDY GGGIVNPEKA ADPGLIYDMG PRDYILYLCS AGYNDSSITQ LVGNVTVCST
PKTSVLDVNL PSITIPDLKD EVTLTRTVTN VGTVDSVYKV VVEPPLGIQV VVAPETLVFN
SKTKNVSFTV RVSTTHKINT GFYFGNLIWT DSMHNVTIPV SVRTQILQNY YDEN
