SBT4E_ARATH
ID SBT4E_ARATH Reviewed; 749 AA.
AC Q9LLL8; O81324;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Subtilisin-like protease SBT4.14 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Cucumisin-like protein;
DE AltName: Full=Subtilase subfamily 4 member 14 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT4.14 {ECO:0000303|PubMed:16193095};
DE AltName: Full=Xylem serine proteinase 1 {ECO:0000303|PubMed:10889267};
DE Short=AtXSP1 {ECO:0000303|PubMed:10889267};
DE Flags: Precursor;
GN Name=SBT4.14 {ECO:0000303|PubMed:16193095};
GN Synonyms=XSP1 {ECO:0000303|PubMed:10889267}; OrderedLocusNames=At4g00230;
GN ORFNames=F6N15.3;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Xylem;
RX PubMed=10889267; DOI=10.1104/pp.123.3.1185;
RA Zhao C., Johnson B.J., Kositsup B., Beers E.P.;
RT "Exploiting secondary growth in Arabidopsis. Construction of xylem and bark
RT cDNA libraries and cloning of three xylem endopeptidases.";
RL Plant Physiol. 123:1185-1196(2000).
RN [2]
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 [3]
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 [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 -!- TISSUE SPECIFICITY: Expressed only in roots, particularly in xylem.
CC {ECO:0000269|PubMed:10889267}.
CC -!- PTM: The C-terminal propeptide is autocleaved. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC19302.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80781.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF190794; AAF25830.1; -; mRNA.
DR EMBL; AF069299; AAC19302.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161471; CAB80781.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81840.1; -; Genomic_DNA.
DR PIR; T01351; T01351.
DR RefSeq; NP_567155.1; NM_116240.5.
DR AlphaFoldDB; Q9LLL8; -.
DR SMR; Q9LLL8; -.
DR STRING; 3702.AT4G00230.1; -.
DR MEROPS; S08.A14; -.
DR iPTMnet; Q9LLL8; -.
DR PaxDb; Q9LLL8; -.
DR PRIDE; Q9LLL8; -.
DR ProteomicsDB; 232736; -.
DR EnsemblPlants; AT4G00230.1; AT4G00230.1; AT4G00230.
DR GeneID; 827949; -.
DR Gramene; AT4G00230.1; AT4G00230.1; AT4G00230.
DR KEGG; ath:AT4G00230; -.
DR Araport; AT4G00230; -.
DR TAIR; locus:2126896; AT4G00230.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR HOGENOM; CLU_000625_4_3_1; -.
DR InParanoid; Q9LLL8; -.
DR OMA; LCHEGYK; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9LLL8; -.
DR PRO; PR:Q9LLL8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9LLL8; baseline and differential.
DR Genevisible; Q9LLL8; AT.
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; 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; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..115
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027202"
FT CHAIN 116..?
FT /note="Subtilisin-like protease SBT4.14"
FT /id="PRO_0000027203"
FT PROPEP ?..749
FT /evidence="ECO:0000250"
FT /id="PRO_0000027204"
FT DOMAIN 38..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 119..595
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 536
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 749 AA; 80329 MW; FB8134FB9250C152 CRC64;
MIRSKCSCHH HLLVLVMVVL WISPRYASAE DEHAKDFYII YLGDRPDNTE ETIKTHINLL
SSLNISQEEA KERKVYSYTK AFNAFAAKLS PHEAKKMMEM EEVVSVSRNQ YRKLHTTKSW
DFVGLPLTAK RHLKAERDVI IGVLDTGITP DSESFLDHGL GPPPAKWKGS CGPYKNFTGC
NNKIIGAKYF KHDGNVPAGE VRSPIDIDGH GTHTSSTVAG VLVANASLYG IANGTARGAV
PSARLAMYKV CWARSGCADM DILAGFEAAI HDGVEIISIS IGGPIADYSS DSISVGSFHA
MRKGILTVAS AGNDGPSSGT VTNHEPWILT VAASGIDRTF KSKIDLGNGK SFSGMGISMF
SPKAKSYPLV SGVDAAKNTD DKYLARYCFS DSLDRKKVKG KVMVCRMGGG GVESTIKSYG
GAGAIIVSDQ YLDNAQIFMA PATSVNSSVG DIIYRYINST RSASAVIQKT RQVTIPAPFV
ASFSSRGPNP GSIRLLKPDI AAPGIDILAA FTLKRSLTGL DGDTQFSKFT ILSGTSMACP
HVAGVAAYVK SFHPDWTPAA IKSAIITSAK PISRRVNKDA EFAYGGGQIN PRRAASPGLV
YDMDDISYVQ FLCGEGYNAT TLAPLVGTRS VSCSSIVPGL GHDSLNYPTI QLTLRSAKTS
TLAVFRRRVT NVGPPSSVYT ATVRAPKGVE ITVEPQSLSF SKASQKRSFK VVVKAKQMTP
GKIVSGLLVW KSPRHSVRSP IVIYSPTSD
