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SBT4F_ARATH
ID   SBT4F_ARATH             Reviewed;         766 AA.
AC   Q9LZS6;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Subtilisin-like protease SBT4.15 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 4 member 15 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT4.15 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT4.15 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At5g03620 {ECO:0000312|Araport:AT5G03620};
GN   ORFNames=F17C15.40 {ECO:0000312|EMBL:CAB82927.1};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   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; AL162506; CAB82927.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90634.1; -; Genomic_DNA.
DR   PIR; T48389; T48389.
DR   RefSeq; NP_568124.1; NM_120443.2.
DR   AlphaFoldDB; Q9LZS6; -.
DR   SMR; Q9LZS6; -.
DR   STRING; 3702.AT5G03620.1; -.
DR   MEROPS; S08.A13; -.
DR   iPTMnet; Q9LZS6; -.
DR   PaxDb; Q9LZS6; -.
DR   PRIDE; Q9LZS6; -.
DR   ProteomicsDB; 232737; -.
DR   EnsemblPlants; AT5G03620.1; AT5G03620.1; AT5G03620.
DR   GeneID; 831777; -.
DR   Gramene; AT5G03620.1; AT5G03620.1; AT5G03620.
DR   KEGG; ath:AT5G03620; -.
DR   Araport; AT5G03620; -.
DR   TAIR; locus:2144583; AT5G03620.
DR   eggNOG; ENOG502QRA7; Eukaryota.
DR   HOGENOM; CLU_000625_4_3_1; -.
DR   InParanoid; Q9LZS6; -.
DR   OMA; MGEDKVM; -.
DR   OrthoDB; 337164at2759; -.
DR   PhylomeDB; Q9LZS6; -.
DR   PRO; PR:Q9LZS6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LZS6; 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; 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; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..113
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435253"
FT   CHAIN           114..?
FT                   /note="Subtilisin-like protease SBT4.15"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004329362"
FT   PROPEP          ?..766
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435254"
FT   DOMAIN          35..113
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          117..601
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          365..460
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        210
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        543
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        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        624
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        638
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        668
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   766 AA;  82595 MW;  41D51BABC3EE2120 CRC64;
     MVSNQRVRLF MLCFCLVNNA VIAATEDENV ERKPYIVYMG EATENSLVEA AENHHNLLMT
     VIGDESKARE LKIYSYGKNI NGFVARLFPH EAEKLSREEG VVSVFKNTQR QLHTTRSWDF
     LGLVESKYKR SVGIESNIIV GVLDTGIDVE SPSFNDKGVG PPPAKWKGKC VTGNNFTRCN
     NKVIGAKYFH IQSEGLPDGE GDTAADHDGH GTHTSSTIAG VSVSSASLFG IANGTARGGV
     PSARIAAYKV CWDSGCTDMD MLAAFDEAIS DGVDIISISI GGASLPFFED PIAIGAFHAM
     KRGILTTCSA GNNGPGLFTV SNLAPWVMTV AANSLDRKFE TVVKLGNGLT ASGISLNGFN
     PRKKMYPLTS GSLASNLSAG GYGEPSTCEP GTLGEDKVMG KVVYCEAGRE EGGNGGQGQD
     HVVRSLKGAG VIVQLLEPTD MATSTLIAGS YVFFEDGTKI TEYINSTKNP QAVIFKTKTT
     KMLAPSISSF SARGPQRISP NILKPDISAP GLNILAAYSK LASVTGYPDD NRRTLFSIMS
     GTSMACPHAA AAAAYVKSFH PDWSPAAIKS ALMTTATPMR IKGNEAELSY GSGQINPRRA
     IHPGLVYDIT EDAYLRFLCK EGYNSTSIGL LTGDNSNNTT KKEYNCENIK RGLGSDGLNY
     PSLHKQVNST EAKVSEVFYR TVTNVGYGPS TYVARVWAPK GLRVEVVPKV MSFERPKEKR
     NFKVVIDGVW DETMKGIVSA SVEWDDSRGH LVRSPILLFR SDNDYR
 
 
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