SBT24_ARATH
ID SBT24_ARATH Reviewed; 832 AA.
AC F4HYR6; O48798; Q948Q4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Subtilisin-like protease SBT2.4 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Protein ABNORMAL LEAF SHAPE 1 {ECO:0000303|PubMed:11731449};
DE AltName: Full=Subtilase subfamily 2 member 4 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT2.4 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT2.4 {ECO:0000303|PubMed:16193095};
GN Synonyms=ALE1 {ECO:0000303|PubMed:11731449};
GN OrderedLocusNames=At1g62340 {ECO:0000312|Araport:AT1G62340};
GN ORFNames=F2401.7 {ECO:0000312|EMBL:AAF70850.1};
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 [MRNA], FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLY-230.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11731449; DOI=10.1242/dev.128.23.4681;
RA Tanaka H., Onouchi H., Kondo M., Hara-Nishimura I., Nishimura M.,
RA Machida C., Machida Y.;
RT "A subtilisin-like serine protease is required for epidermal surface
RT formation in Arabidopsis embryos and juvenile plants.";
RL Development 128:4681-4689(2001).
RN [2]
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 [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).
RN [5]
RP FUNCTION.
RX PubMed=17376810; DOI=10.1242/dev.003533;
RA Tanaka H., Watanabe M., Sasabe M., Hiroe T., Tanaka T., Tsukaya H.,
RA Ikezaki M., Machida C., Machida Y.;
RT "Novel receptor-like kinase ALE2 controls shoot development by specifying
RT epidermis in Arabidopsis.";
RL Development 134:1643-1652(2007).
RN [6]
RP FUNCTION.
RX PubMed=23318634; DOI=10.1242/dev.088898;
RA Xing Q., Creff A., Waters A., Tanaka H., Goodrich J., Ingram G.C.;
RT "ZHOUPI controls embryonic cuticle formation via a signalling pathway
RT involving the subtilisin protease ABNORMAL LEAF-SHAPE1 and the receptor
RT kinases GASSHO1 and GASSHO2.";
RL Development 140:770-779(2013).
CC -!- FUNCTION: Serine protease required for epidermal surface formation in
CC embryos and juvenile plants (PubMed:11731449, PubMed:17376810,
CC PubMed:23318634). Involved in embryonic cuticle formation downstream of
CC BHLH95/ZOU (PubMed:23318634). {ECO:0000269|PubMed:11731449,
CC ECO:0000269|PubMed:17376810, ECO:0000269|PubMed:23318634}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the endosperm cells during embryo
CC development. {ECO:0000269|PubMed:11731449}.
CC -!- DISRUPTION PHENOTYPE: Seedlings lethality when homozygous due to water
CC loss. Mutant seedling grown under high humidity can survive and show
CC small, crinkled cotyledons and fused leaves due to impaired cuticule
CC formation. {ECO:0000269|PubMed:11731449}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF70850.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB060809; BAB70678.1; -; mRNA.
DR EMBL; AC003113; AAF70850.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33956.1; -; Genomic_DNA.
DR PIR; T01444; T01444.
DR RefSeq; NP_564793.2; NM_104914.2.
DR AlphaFoldDB; F4HYR6; -.
DR SMR; F4HYR6; -.
DR STRING; 3702.AT1G62340.1; -.
DR MEROPS; S08.014; -.
DR PaxDb; F4HYR6; -.
DR PRIDE; F4HYR6; -.
DR ProteomicsDB; 226592; -.
DR EnsemblPlants; AT1G62340.1; AT1G62340.1; AT1G62340.
DR GeneID; 842532; -.
DR Gramene; AT1G62340.1; AT1G62340.1; AT1G62340.
DR KEGG; ath:AT1G62340; -.
DR Araport; AT1G62340; -.
DR TAIR; locus:2027139; AT1G62340.
DR eggNOG; ENOG502QUPZ; Eukaryota.
DR HOGENOM; CLU_000625_3_1_1; -.
DR InParanoid; F4HYR6; -.
DR OMA; YSFKHIV; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:F4HYR6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HYR6; baseline and differential.
DR Genevisible; F4HYR6; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0090558; P:plant epidermis development; IMP:TAIR.
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; IPR023827; Peptidase_S8_Asp-AS.
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; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..832
FT /note="Subtilisin-like protease SBT2.4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431966"
FT DOMAIN 74..138
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 150..690
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 425..524
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 252
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 618
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 230
FT /note="G->E: In ale1-2; Seedlings lethality when homozygous
FT due to water loss. Mutant seedling grown under high
FT humidity can survive and show small, crinkled cotyledons
FT and fused leaves."
FT /evidence="ECO:0000269|PubMed:11731449"
FT CONFLICT 15
FT /note="C -> W (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 36..42
FT /note="EGKGEND -> QGKDENN (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="I -> V (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="D -> E (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="I -> F (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="G -> R (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="Q -> P (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="L -> I (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="F -> L (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="N -> S (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="V -> I (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="S -> A (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="P -> S (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="G -> D (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 552..556
FT /note="VFAGK -> IFAGQ (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="T -> N (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="N -> T (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="D -> N (in Ref. 1; BAB70678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 832 AA; 89066 MW; 1BD16943C17913AC CRC64;
METNPRKLRS YSYICLIVCI FVLVVCAILS RAEEKEGKGE NDDHIPKIYS ILVEGEPLAF
RASTNINSKA MALEAKKIEE IHDEILGSTL EKGSYTKLYS FKHVINAIAV RTTASQAKKL
GKTKGVKAVE EDKGVKLMTT YTPDFLELPQ QVWQKISNEG DRRAGEDIVI GFVDTGINPT
HPSFAALDLT NPYSSNLSRL HFSGDCEIGP FFPPGSCNGK IISARFFSAG ARASGALNSS
LDILSPFDAS GHGSHVASIA AGNAGVPVIV DGFFYGRASG MAPRSRIAVY KAIYPSIGTL
VDVIAAIDQA IMDGVDVLTL SVGPDEPPVD KPTVLGIFDL AMLLARKAGV FVVQAVGNNG
PSPSSVLSYS PWVVGVAAGN TDRSYPAPLI LDGGQTVQGV GLSGPTLGAP LVQHRLVLAK
DAVRTNGSVL QPLTRDIEEC QRPENFDPAA VFGSIVICTF SDGFYNQMST VLAITQTART
LGFMGFILIA NPRFGDYVAE PVIFSAPGIL IPTVSAAQII LRYYEEKTFR DTRGVATQFG
ARARIGEGRN SVFAGKAPVV SRFSSRGPAF IDATRSPLDV LKPDILAPGH QIWGAWSLPS
AFDPILTGRS FAILSGTSMA TPHIAGIGAL IKQLNPSWTP AMIASAISTT ANEYDSNGEI
ISAEYYELSR LFPSNHFDHG AGHVNPARAL DPGLVLPAGF EDYISFLCSL PNISPATIRD
ATGVLCTTTL SHPANLNHPS VTISALKESL VVRRSFQDVS NKTETYLGSV LPPNGTTVRL
TPTWFTVPPQ KTQDLDIEFN VTQVLNKFTF GEVVLTGSLN HIIRIPLSVK TI
