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SBT45_ARATH
ID   SBT45_ARATH             Reviewed;         738 AA.
AC   F4JA91; Q9STF6;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Subtilisin-like protease SBT4.5 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 4 member 5 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT4.5 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT4.5 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At3g46840 {ECO:0000312|Araport:AT3G46840};
GN   ORFNames=T6H20.130 {ECO:0000312|EMBL:CAB51181.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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; AL096859; CAB51181.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78210.1; -; Genomic_DNA.
DR   PIR; T12964; T12964.
DR   RefSeq; NP_566887.2; NM_114551.2.
DR   AlphaFoldDB; F4JA91; -.
DR   SMR; F4JA91; -.
DR   STRING; 3702.AT3G46840.1; -.
DR   MEROPS; S08.A18; -.
DR   iPTMnet; F4JA91; -.
DR   PaxDb; F4JA91; -.
DR   PRIDE; F4JA91; -.
DR   ProteomicsDB; 226648; -.
DR   EnsemblPlants; AT3G46840.1; AT3G46840.1; AT3G46840.
DR   GeneID; 823837; -.
DR   Gramene; AT3G46840.1; AT3G46840.1; AT3G46840.
DR   KEGG; ath:AT3G46840; -.
DR   Araport; AT3G46840; -.
DR   TAIR; locus:2102792; AT3G46840.
DR   eggNOG; ENOG502QRA7; Eukaryota.
DR   HOGENOM; CLU_000625_4_3_1; -.
DR   InParanoid; F4JA91; -.
DR   OMA; CGLKYTG; -.
DR   OrthoDB; 337164at2759; -.
DR   PRO; PR:F4JA91; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; F4JA91; 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; 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   3: Inferred from homology;
KW   Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..112
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435234"
FT   CHAIN           113..738
FT                   /note="Subtilisin-like protease SBT4.5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003309744"
FT   PROPEP          ?..738
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435235"
FT   DOMAIN          35..111
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          116..589
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          362..433
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        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        527
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        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        450
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        564
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        598
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        610
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"
FT   CONFLICT        348
FT                   /note="T -> TV (in Ref. 1; CAB51181)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   738 AA;  79061 MW;  7DE1BD9C136146AC CRC64;
     MTKPAVSYCL LSCIFALLVV SFASADKDDQ DKQEYIVYMG ALPARVDYMP MSHHTSILQD
     VTGESSIEDR LVRNYKRSFN GFAARLTKSE REILASMDEV VSVFPNKKLK LQTTTSWNFM
     GLKESKRTKR NTIIESDTII GVIDSGIYPE SDSFSGKGFG PPPKKWKGVC KGGKNFTWNN
     KLIGARYYTP KLEGFPESAR DYMGHGSHTA STAAGNAVKH VSFYGLGNGT ARGGVPAARI
     AVYKVCDPGV DGCTTDGILA AFDDAIADKV DIITISIGGD NSSPFEEDPI AIGAFHAMAK
     GILIVNSAGN SGPEPSTVAS IAPWMFTVAA SNTNRAFVTK VVLGNGKTVG RSVNSFDLNG
     KKYPLVYGKS ASSSCGAASA GFCSPGCLDS KRVKGKIVLC DSPQNPDEAQ AMGAIASIVR
     SHRTDVASIF SFPVSVLLED DYNTVLSYMN STKNPKAAVL KSETIFNQRA PVVASYFSRG
     PNTIIPDILK PDITAPGSEI VAAYSPDAPP SISDTRRVKY SVDTGTSMSC PHVAGVAAYL
     KSFHPRWSPS MIQSAIMTTA WPMNASTSPF NELAEFAYGA GHVDPITAIH PGLVYEANKS
     DHIAFLCGLN YTAKNLRLIS GDSSSCTKEQ TKSLPRNLNY PSMTAQVSAA KPFKVIFRRT
     VTNVGRPNAT YKAKVVGSKL KVKVVPAVLS LKSLYEKKSF TVTASGAGPK AENLVSAQLI
     WSDGVHFVRS PIVVYATN
 
 
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