SBT54_ARATH
ID SBT54_ARATH Reviewed; 778 AA.
AC F4JXC5; Q8GXU1; Q9FJF3;
DT 11-JUN-2014, 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 SBT5.4 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Subtilase subfamily 5 member 4 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT5.4 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT5.4 {ECO:0000303|PubMed:16193095}; OrderedLocusNames=At5g59810;
GN ORFNames=MMN10.6;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF SER-567.
RX PubMed=19588163; DOI=10.1007/s00425-009-0976-5;
RA Liu J.X., Srivastava R., Howell S.;
RT "Overexpression of an Arabidopsis gene encoding a subtilase (AtSBT5.4)
RT produces a clavata-like phenotype.";
RL Planta 230:687-697(2009).
CC -!- FUNCTION: Serine protease. Has a substrate preference for the
CC hydrophobic residues Phe and Ala and the basic residue Asp in the P1
CC position, and for Asp, Leu or Ala in the P1' position (By similarity).
CC Interferes with CLAVATA 3 (CLV3) signaling, but does not cleave CLV3.
CC {ECO:0000250, ECO:0000269|PubMed:19588163}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000305|PubMed:19588163}. Cell membrane
CC {ECO:0000305|PubMed:19588163}.
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature of roots and leaves,
CC stomata, sepals, stigma, anthers and siliques.
CC {ECO:0000269|PubMed:19588163}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19588163}.
CC -!- MISCELLANEOUS: Plants over-expressing SBT5.4 show a clavata-like
CC phenotype with fasciated inflorescence stems and compounded terminal
CC buds. This phenotype is abolished by mutating Ser-567 to Ala which
CC completely disrupts the catalytic center of the protease
CC (PubMed:19588163). {ECO:0000305|PubMed:19588163}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08348.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42673.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB015475; BAB08348.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97236.1; -; Genomic_DNA.
DR EMBL; AK118042; BAC42673.1; ALT_SEQ; mRNA.
DR RefSeq; NP_200789.2; NM_125373.3.
DR AlphaFoldDB; F4JXC5; -.
DR SMR; F4JXC5; -.
DR STRING; 3702.AT5G59810.1; -.
DR MEROPS; S08.A26; -.
DR iPTMnet; F4JXC5; -.
DR PaxDb; F4JXC5; -.
DR PRIDE; F4JXC5; -.
DR ProteomicsDB; 232793; -.
DR EnsemblPlants; AT5G59810.1; AT5G59810.1; AT5G59810.
DR GeneID; 836102; -.
DR Gramene; AT5G59810.1; AT5G59810.1; AT5G59810.
DR KEGG; ath:AT5G59810; -.
DR Araport; AT5G59810; -.
DR TAIR; locus:2168057; AT5G59810.
DR eggNOG; ENOG502RKXZ; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; F4JXC5; -.
DR OMA; VAHSHRT; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:F4JXC5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JXC5; baseline and differential.
DR Genevisible; F4JXC5; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0010074; P:maintenance of meristem identity; IGI: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; IPR041469; Subtilisin-like_FN3.
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 membrane; Endoplasmic reticulum; Glycoprotein; Growth regulation;
KW Hydrolase; Membrane; Protease; Reference proteome; Serine protease; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..778
FT /note="Subtilisin-like protease SBT5.4"
FT /id="PRO_0000429357"
FT DOMAIN 41..126
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 130..634
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 401..486
FT /note="PA"
FT ACT_SITE 163
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 230
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 567
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 567
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19588163"
SQ SEQUENCE 778 AA; 83456 MW; A8A17C29F3762BAA CRC64;
MSMTRRYSST QYSNKMSLQS LSSLLLLVTL FFSPAFALKK SYIVYLGSHA HLPQISSAHL
DGVAHSHRTF LASFVGSHEN AKEAIFYSYK RHINGFAAIL DENEAAEIAK HPDVVSVFPN
KGRKLHTTHS WNFMLLAKNG VVHKSSLWNK AGYGEDTIIA NLDTGVWPES KSFSDEGYGA
VPARWKGRCH KDVPCNRKLI GARYFNKGYL AYTGLPSNAS YETCRDHDGH GSHTLSTAAG
NFVPGANVFG IGNGTASGGS PKARVAAYKV CWPPVDGAEC FDADILAAIE AAIEDGVDVL
SASVGGDAGD YMSDGIAIGS FHAVKNGVTV VCSAGNSGPK SGTVSNVAPW VITVGASSMD
REFQAFVELK NGQSFKGTSL SKPLPEEKMY SLISAADANV ANGNVTDALL CKKGSLDPKK
VKGKILVCLR GDNARVDKGM QAAAAGAAGM VLCNDKASGN EIISDAHVLP ASQIDYKDGE
TLFSYLSSTK DPKGYIKAPT ATLNTKPAPF MASFSSRGPN TITPGILKPD ITAPGVNIIA
AFTEATGPTD LDSDNRRTPF NTESGTSMSC PHISGVVGLL KTLHPHWSPA AIRSAIMTTS
RTRNNRRKPM VDESFKKANP FSYGSGHVQP NKAAHPGLVY DLTTGDYLDF LCAVGYNNTV
VQLFAEDPQY TCRQGANLLD FNYPSITVPN LTGSITVTRK LKNVGPPATY NARFREPLGV
RVSVEPKQLT FNKTGEVKIF QMTLRPLPVT PSGYVFGELT WTDSHHYVRS PIVVQLSS
