SBT44_ARATH
ID SBT44_ARATH Reviewed; 741 AA.
AC Q9FGU3;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Subtilisin-like protease SBT4.4 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 4 member 4 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT4.4 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT4.4 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g59100 {ECO:0000312|Araport:AT5G59100};
GN ORFNames=K18B18.10 {ECO:0000312|EMBL:BAB10785.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 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 [5]
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 -!- PTM: The C-terminal propeptide is autocleaved.
CC {ECO:0000250|UniProtKB:Q39547}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AB024027; BAB10785.1; -; Genomic_DNA.
DR EMBL; AB016890; BAB10785.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED97142.1; -; Genomic_DNA.
DR EMBL; AY099705; AAM20556.1; -; mRNA.
DR EMBL; BT000313; AAN15632.1; -; mRNA.
DR RefSeq; NP_568896.1; NM_125300.3.
DR AlphaFoldDB; Q9FGU3; -.
DR SMR; Q9FGU3; -.
DR STRING; 3702.AT5G59100.1; -.
DR MEROPS; S08.A19; -.
DR iPTMnet; Q9FGU3; -.
DR PaxDb; Q9FGU3; -.
DR PRIDE; Q9FGU3; -.
DR EnsemblPlants; AT5G59100.1; AT5G59100.1; AT5G59100.
DR GeneID; 836027; -.
DR Gramene; AT5G59100.1; AT5G59100.1; AT5G59100.
DR KEGG; ath:AT5G59100; -.
DR Araport; AT5G59100; -.
DR TAIR; locus:2153296; AT5G59100.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR HOGENOM; CLU_000625_4_3_1; -.
DR InParanoid; Q9FGU3; -.
DR OMA; LCEPKCL; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; Q9FGU3; -.
DR PRO; PR:Q9FGU3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGU3; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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 2: Evidence at transcript level;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..112
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435232"
FT CHAIN 113..?
FT /note="Subtilisin-like protease SBT4.4"
FT /evidence="ECO:0000255"
FT /id="PRO_5004325407"
FT PROPEP ?..741
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435233"
FT DOMAIN 34..111
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 116..589
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 359..445
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 528
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 623
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"
SQ SEQUENCE 741 AA; 79598 MW; F12B613C79413AEA CRC64;
MAKGTTFIFL FSSLLVLSLS SVSADKDDHG DQQVYIVYLG SLPSREEYTP MSDHMSILQE
ITGESLIENR LVRSYKKSFN GFAARLTESE RKRLAGMERV VSVFPSRKLK LQTTSSWNFM
GLKEGIKTKR TRSIESDTII GVIDSGIYPE SDSFSDQGFG PPPKKWKGTC AGGKNFTCNN
KVIGARDYTA KSKANQTARD YSGHGTHTAS IAAGNAVANS NFYGLGNGTA RGGVPAARIA
VYKVCDNEGC DGEAMMSAFD DAIADGVDVI SISIVLDNIP PFEEDPIAIG AFHAMAVGVL
TVNAAGNNGP KISTVTSTAP WVFSVAASVT NRAFMAKVVL GDGKILIGRS VNTYDMNGTN
YPLVYGKSAA LSTCSVDKAR LCEPKCLDGK LVKGKIVLCD STKGLIEAQK LGAVGSIVKN
PEPDRAFIRS FPVSFLSNDD YKSLVSYMNS TKNPKATVLK SEEISNQRAP LVASFSSRGP
SSIVSDILKP DITAPGVEIL AAYSPDSSPT ESEFDTRRVK YSVLSGTSMA CPHVAGVAAY
VKTFHPQWSP SMIQSAIMTT AWPMNASGSG FVSTEFAYGS GHVDPIDAIN PGLVYELTKA
DHINFLCGLN YTSDHLRIIS GDNSTCTKEI SKTLPRNLNY PTMSAKVSGT KPFNITFQRT
VTNVGMQKST YNAKVVKFPG SKLSIKVSPR VLSMKSMNEK QSFMVTVSSD SIGTKQPVSA
NLIWSDGTHN VRSPIIVYAM S
