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SBT49_ARATH
ID   SBT49_ARATH             Reviewed;         713 AA.
AC   Q9FIM5;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Subtilisin-like protease SBT4.9 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 4 member 9 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT4.9 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT4.9 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At5g58840 {ECO:0000312|Araport:AT5G58840};
GN   ORFNames=K19M22.4 {ECO:0000312|EMBL:BAB09629.1};
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=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   [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].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) 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   -!- 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; AB016885; BAB09629.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97109.1; -; Genomic_DNA.
DR   EMBL; BT008543; AAP40370.1; -; mRNA.
DR   EMBL; BT008659; AAP40471.1; -; mRNA.
DR   EMBL; AK229679; BAF01520.1; -; mRNA.
DR   RefSeq; NP_568890.2; NM_125274.3.
DR   AlphaFoldDB; Q9FIM5; -.
DR   SMR; Q9FIM5; -.
DR   STRING; 3702.AT5G58840.1; -.
DR   MEROPS; S08.A07; -.
DR   iPTMnet; Q9FIM5; -.
DR   PaxDb; Q9FIM5; -.
DR   PRIDE; Q9FIM5; -.
DR   ProteomicsDB; 226650; -.
DR   EnsemblPlants; AT5G58840.1; AT5G58840.1; AT5G58840.
DR   GeneID; 836001; -.
DR   Gramene; AT5G58840.1; AT5G58840.1; AT5G58840.
DR   KEGG; ath:AT5G58840; -.
DR   Araport; AT5G58840; -.
DR   TAIR; locus:2154528; AT5G58840.
DR   eggNOG; ENOG502QRA7; Eukaryota.
DR   HOGENOM; CLU_000625_4_3_1; -.
DR   InParanoid; Q9FIM5; -.
DR   OMA; TISICAP; -.
DR   OrthoDB; 337164at2759; -.
DR   PhylomeDB; Q9FIM5; -.
DR   PRO; PR:Q9FIM5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIM5; 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   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..113
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435242"
FT   CHAIN           114..?
FT                   /note="Subtilisin-like protease SBT4.9"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004326411"
FT   PROPEP          ?..713
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435243"
FT   DOMAIN          34..112
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          117..560
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          356..415
FT                   /note="PA"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        145
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        200
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        499
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        215
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        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        536
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        583
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        627
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        637
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   713 AA;  75957 MW;  38DC8864572B5707 CRC64;
     MARRADSFCL ISCVLVSFVI SVSAVTDDSQ DKQVYVVYMG SLPSSRLEYT PMSHHMSILQ
     EVTGESSVEG RLVRSYKRSF NGFAARLTES ERERVAEMEG VVSVFPDINY KLQTTASWDF
     LGLKEGKNTK RNLAIESDTI IGFIDSGIWP ESESFSDKGF GPPPKKWKGV CSAGKNFTCN
     NKLIGARDYT NEGTRDIEGH GTHTASTAAG NAVKNTSFYG IGNGTARGGV PASRIAAYKA
     CSEMGCTTES VLSAFDDAIA DGVDLISISL GANLVRTYET DPIAIGAFHA MVKGILTVQS
     AGNGGPNPGS VMSVAPWILT VAASNTNRGF VTKVVLGNGK TFVGKSLNAF DLKGKNYPLY
     GGSTDGPLLR GKILVSEDKV SSEIVVANIN ENYHDYAYVS ILPSSALSKD DFDSVISYVN
     STKSPHGTVL KSEAIFNQAA PKVAGFSSRG PNTIAVDILK PDVTAPGVEI LAAFSPLNSP
     AQDKRDNRHV KYSVLSGTSM SCPHVAGVAA YIKTFHPEWS PSMIQSAIMT TAWPMNATGT
     AVASTEFAYG AGHVDPIAAI NPGLVYEIGK SDHIAFLCGL NYNATSLKLI AGEAVTCTGK
     TLPRNLNYPS MSAKLPKSES SFIVTFNRTV TNVGTPNSTY KSKIVLNHGS NLKVEVSPSV
     LSMKSVKEKQ SFTVTVSGSN IDPKLPSSAN LIWSDGTHNV RSPIVVYTYS VSD
 
 
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