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SBT15_ARATH
ID   SBT15_ARATH             Reviewed;         775 AA.
AC   Q9LUM3; Q8LGA0; Q9C5N5;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 146.
DE   RecName: Full=Subtilisin-like protease SBT1.5 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 1 member 5 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT1.5 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT1.5 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At3g14240 {ECO:0000312|Araport:AT3G14240};
GN   ORFNames=MLN21.2 {ECO:0000312|EMBL:BAB01030.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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   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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AB022220; BAB01030.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75493.1; -; Genomic_DNA.
DR   EMBL; AF360129; AAK25839.1; -; mRNA.
DR   EMBL; AY084387; AAM60964.1; -; mRNA.
DR   RefSeq; NP_566483.1; NM_112282.3.
DR   AlphaFoldDB; Q9LUM3; -.
DR   SMR; Q9LUM3; -.
DR   STRING; 3702.AT3G14240.1; -.
DR   MEROPS; S08.A44; -.
DR   PaxDb; Q9LUM3; -.
DR   PRIDE; Q9LUM3; -.
DR   ProteomicsDB; 232844; -.
DR   EnsemblPlants; AT3G14240.1; AT3G14240.1; AT3G14240.
DR   GeneID; 820644; -.
DR   Gramene; AT3G14240.1; AT3G14240.1; AT3G14240.
DR   KEGG; ath:AT3G14240; -.
DR   Araport; AT3G14240; -.
DR   TAIR; locus:2091010; AT3G14240.
DR   eggNOG; ENOG502QTK5; Eukaryota.
DR   HOGENOM; CLU_000625_3_1_1; -.
DR   InParanoid; Q9LUM3; -.
DR   OMA; YSASMCL; -.
DR   OrthoDB; 337164at2759; -.
DR   PhylomeDB; Q9LUM3; -.
DR   PRO; PR:Q9LUM3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LUM3; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..103
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q9MAP7"
FT                   /id="PRO_0000435174"
FT   CHAIN           104..?
FT                   /note="Subtilisin-like protease SBT1.5"
FT                   /id="PRO_5004330100"
FT   PROPEP          ?..775
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435175"
FT   DOMAIN          27..103
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          107..617
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          367..459
FT                   /note="PA"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        137
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        549
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        599
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        762
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        5
FT                   /note="F -> S (in Ref. 3; AAK25839)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="F -> L (in Ref. 4; AAM60964)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="D -> N (in Ref. 4; AAM60964)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="K -> T (in Ref. 4; AAM60964)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        579
FT                   /note="I -> M (in Ref. 4; AAM60964)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        604
FT                   /note="M -> T (in Ref. 4; AAM60964)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        615
FT                   /note="K -> R (in Ref. 4; AAM60964)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        641
FT                   /note="R -> G (in Ref. 4; AAM60964)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        754
FT                   /note="I -> M (in Ref. 4; AAM60964)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   775 AA;  82584 MW;  CC909DE4DABDE0E8 CRC64;
     MAFFFYFFFL LTLSSPSSSA SSSNSLTYIV HVDHEAKPSI FPTHFHWYTS SLASLTSSPP
     SIIHTYDTVF HGFSARLTSQ DASQLLDHPH VISVIPEQVR HLHTTRSPEF LGLRSTDKAG
     LLEESDFGSD LVIGVIDTGV WPERPSFDDR GLGPVPIKWK GQCIASQDFP ESACNRKLVG
     ARFFCGGYEA TNGKMNETTE FRSPRDSDGH GTHTASISAG RYVFPASTLG YAHGVAAGMA
     PKARLAAYKV CWNSGCYDSD ILAAFDTAVA DGVDVISLSV GGVVVPYYLD AIAIGAFGAI
     DRGIFVSASA GNGGPGALTV TNVAPWMTTV GAGTIDRDFP ANVKLGNGKM ISGVSVYGGP
     GLDPGRMYPL VYGGSLLGGD GYSSSLCLEG SLDPNLVKGK IVLCDRGINS RATKGEIVRK
     NGGLGMIIAN GVFDGEGLVA DCHVLPATSV GASGGDEIRR YISESSKSRS SKHPTATIVF
     KGTRLGIRPA PVVASFSARG PNPETPEILK PDVIAPGLNI LAAWPDRIGP SGVTSDNRRT
     EFNILSGTSM ACPHVSGLAA LLKAAHPDWS PAAIRSALIT TAYTVDNSGE PMMDESTGNT
     SSVMDYGSGH VHPTKAMDPG LVYDITSYDY INFLCNSNYT RTNIVTITRR QADCDGARRA
     GHVGNLNYPS FSVVFQQYGE SKMSTHFIRT VTNVGDSDSV YEIKIRPPRG TTVTVEPEKL
     SFRRVGQKLS FVVRVKTTEV KLSPGATNVE TGHIVWSDGK RNVTSPLVVT LQQPL
 
 
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