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SBT18_ARATH
ID   SBT18_ARATH             Reviewed;         754 AA.
AC   Q9ZUF6;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Subtilisin-like protease SBT1.8 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 1 member 8 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT1.8 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT1.8 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At2g05920 {ECO:0000312|Araport:AT2G05920};
GN   ORFNames=T6P5.12 {ECO:0000312|EMBL:AAC95169.1};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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   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   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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AC005970; AAC95169.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05985.1; -; Genomic_DNA.
DR   EMBL; AY035090; AAK59595.1; -; mRNA.
DR   EMBL; AY142613; AAN13182.1; -; mRNA.
DR   PIR; A84473; A84473.
DR   RefSeq; NP_565330.1; NM_126605.4.
DR   AlphaFoldDB; Q9ZUF6; -.
DR   SMR; Q9ZUF6; -.
DR   STRING; 3702.AT2G05920.1; -.
DR   MEROPS; S08.A24; -.
DR   PaxDb; Q9ZUF6; -.
DR   PRIDE; Q9ZUF6; -.
DR   ProteomicsDB; 232845; -.
DR   EnsemblPlants; AT2G05920.1; AT2G05920.1; AT2G05920.
DR   GeneID; 815145; -.
DR   Gramene; AT2G05920.1; AT2G05920.1; AT2G05920.
DR   KEGG; ath:AT2G05920; -.
DR   Araport; AT2G05920; -.
DR   TAIR; locus:2064696; AT2G05920.
DR   eggNOG; ENOG502QRTY; Eukaryota.
DR   HOGENOM; CLU_000625_4_6_1; -.
DR   InParanoid; Q9ZUF6; -.
DR   OMA; SGPYYRD; -.
DR   OrthoDB; 337164at2759; -.
DR   PhylomeDB; Q9ZUF6; -.
DR   PRO; PR:Q9ZUF6; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZUF6; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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   1: Evidence at protein level;
KW   Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..102
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q9MAP7"
FT                   /id="PRO_0000435176"
FT   CHAIN           103..?
FT                   /note="Subtilisin-like protease SBT1.8"
FT                   /id="PRO_5004337788"
FT   PROPEP          ?..754
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435177"
FT   DOMAIN          29..102
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          98..604
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          367..452
FT                   /note="PA"
FT                   /evidence="ECO:0000255"
FT   REGION          191..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        134
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        208
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        536
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        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        641
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   754 AA;  80015 MW;  F8CC63F11578CEF7 CRC64;
     MASSSSSSSS ITIITTFLFL LLHTTAKKTY IIRVNHSDKP ESFLTHHDWY TSQLNSESSL
     LYTYTTSFHG FSAYLDSTEA DSLLSSSNSI LDIFEDPLYT LHTTRTPEFL GLNSEFGVHD
     LGSSSNGVII GVLDTGVWPE SRSFDDTDMP EIPSKWKGEC ESGSDFDSKL CNKKLIGARS
     FSKGFQMASG GGFSSKRESV SPRDVDGHGT HTSTTAAGSA VRNASFLGYA AGTARGMATR
     ARVATYKVCW STGCFGSDIL AAMDRAILDG VDVLSLSLGG GSAPYYRDTI AIGAFSAMER
     GVFVSCSAGN SGPTRASVAN VAPWVMTVGA GTLDRDFPAF ANLGNGKRLT GVSLYSGVGM
     GTKPLELVYN KGNSSSSNLC LPGSLDSSIV RGKIVVCDRG VNARVEKGAV VRDAGGLGMI
     MANTAASGEE LVADSHLLPA IAVGKKTGDL LREYVKSDSK PTALLVFKGT VLDVKPSPVV
     AAFSSRGPNT VTPEILKPDV IGPGVNILAG WSDAIGPTGL DKDSRRTQFN IMSGTSMSCP
     HISGLAGLLK AAHPEWSPSA IKSALMTTAY VLDNTNAPLH DAADNSLSNP YAHGSGHVDP
     QKALSPGLVY DISTEEYIRF LCSLDYTVDH IVAIVKRPSV NCSKKFSDPG QLNYPSFSVL
     FGGKRVVRYT REVTNVGAAS SVYKVTVNGA PSVGISVKPS KLSFKSVGEK KRYTVTFVSK
     KGVSMTNKAE FGSITWSNPQ HEVRSPVAFS WNRF
 
 
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