位置:首页 > 蛋白库 > SBT22_ARATH
SBT22_ARATH
ID   SBT22_ARATH             Reviewed;         856 AA.
AC   Q9SUN6; F4JVJ6;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Subtilisin-like protease SBT2.2 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 2 member 2 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT2.2 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT2.2 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At4g20430 {ECO:0000312|Araport:AT4G20430};
GN   ORFNames=F9F13.80 {ECO:0000312|EMBL:CAB45809.1};
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=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   [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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SUN6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SUN6-2; Sequence=VSP_058024;
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL080253; CAB45809.1; -; Genomic_DNA.
DR   EMBL; AL161553; CAB79043.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84328.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84329.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66822.1; -; Genomic_DNA.
DR   PIR; T10585; T10585.
DR   RefSeq; NP_001190781.1; NM_001203852.1. [Q9SUN6-2]
DR   RefSeq; NP_001320010.1; NM_001341438.1. [Q9SUN6-1]
DR   RefSeq; NP_567601.1; NM_118162.3. [Q9SUN6-1]
DR   AlphaFoldDB; Q9SUN6; -.
DR   SMR; Q9SUN6; -.
DR   STRING; 3702.AT4G20430.1; -.
DR   MEROPS; S08.A01; -.
DR   PaxDb; Q9SUN6; -.
DR   PRIDE; Q9SUN6; -.
DR   ProteomicsDB; 232931; -. [Q9SUN6-1]
DR   EnsemblPlants; AT4G20430.1; AT4G20430.1; AT4G20430. [Q9SUN6-1]
DR   EnsemblPlants; AT4G20430.2; AT4G20430.2; AT4G20430. [Q9SUN6-2]
DR   EnsemblPlants; AT4G20430.3; AT4G20430.3; AT4G20430. [Q9SUN6-1]
DR   GeneID; 827791; -.
DR   Gramene; AT4G20430.1; AT4G20430.1; AT4G20430. [Q9SUN6-1]
DR   Gramene; AT4G20430.2; AT4G20430.2; AT4G20430. [Q9SUN6-2]
DR   Gramene; AT4G20430.3; AT4G20430.3; AT4G20430. [Q9SUN6-1]
DR   KEGG; ath:AT4G20430; -.
DR   Araport; AT4G20430; -.
DR   TAIR; locus:2128595; AT4G20430.
DR   eggNOG; ENOG502QSVR; Eukaryota.
DR   InParanoid; Q9SUN6; -.
DR   OMA; KSRYWRS; -.
DR   OrthoDB; 337164at2759; -.
DR   PhylomeDB; Q9SUN6; -.
DR   PRO; PR:Q9SUN6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SUN6; 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; 3.40.50.200; -; 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; 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; 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   3: Inferred from homology;
KW   Alternative splicing; Autocatalytic cleavage; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..159
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q9MAP7"
FT                   /id="PRO_0000435182"
FT   CHAIN           160..?
FT                   /note="Subtilisin-like protease SBT2.2"
FT                   /id="PRO_5004337287"
FT   PROPEP          ?..856
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435183"
FT   DOMAIN          40..159
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          164..709
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          432..528
FT                   /note="PA"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        269
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        634
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        412
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        540
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        704
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        730
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        738
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        748
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        767
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        782
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        823
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   VAR_SEQ         450..474
FT                   /note="MYVGECQDYGSFDKDVIRGNLLICS -> I (in isoform 2)"
FT                   /id="VSP_058024"
SQ   SEQUENCE   856 AA;  91815 MW;  0C9FD624F5DF81E2 CRC64;
     MRRVLMVNFG VLLLFCFGVL SNSFGQDNGG DSDINSTTAV YIVTLRQASS LHLFQQEAEE
     VKRVRDQSKH GDTSKFTRPK LQPRNISRSR YWRSRRSAIA QAHDSLLRNA LKGEKYIKLY
     SFHYLINGFA VFVSSQQAET LSRRREVANI VLDFSVRTAT TYTPQFMGLP KGAWVKEGGY
     ETAGEGIVIG FIDTGIDPTH PSFNGTDTSQ RQYPIPNHFS GVCEVTPDFP SGSCNRKLVG
     ARHFAQSAIT RGIFNSSEDY ASPFDGDGHG THTASIAAGN HGVSAVVSGH NFGSASGIAP
     RAHISVYKAL YKSFGGFAAD VVAAIDQAAQ DGVDILSLSI TPNRRPPGVA TFFNPLDMAM
     LSAVKAGIFV VQAAGNTGPS PKSMSSFSPW IFTVGAASHD RDYSNSIVLG NNVSIPGVGL
     ALRTDEGKKY TMISALDALK NKSSVVDKDM YVGECQDYGS FDKDVIRGNL LICSYSIRFV
     LGLSTIKQAL AVAKNLSAKG VVFYMDPYVL GFQINPTPMD MPGIIIPSAE DSKVLLKYYN
     SSLVRDGTTK EIVRFGAVAA IAGGQNANFS NRAPKIMYYS ARGPDPQDSL FNDADILKPN
     LVAPGNSIWG AWSSAATEST EFEGESFAMM SGTSMAAPHV AGVAALVKQK FRKFSPSAIA
     SALSTTSVLF DNKGEAIMAQ RAYANPDQTI SPATPFDMGN GFVNATAALD PGLIFDTSFE
     DYMSFLCGIN GSAPVVFNYT GTNCLRNNAT ISGSDLNLPS ITVSKLNNTR TVQRLMTNIA
     GNETYTVSLI TPFDVLINVS PTQFSIASGE TKLLSVILTA KRNSSISSFG GIKLLGNAGH
     IVRIPVSVTV KIASKQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024