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SBT41_ARATH
ID   SBT41_ARATH             Reviewed;         775 AA.
AC   F4IG09; Q8S8T2;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Subtilisin-like protease SBT4.1 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 4 member 1 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT4.1 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT4.1 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At2g39850 {ECO:0000312|Araport:AT2G39850};
GN   ORFNames=T5I7.15 {ECO:0000312|EMBL:AAM14853.1};
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=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   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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM14853.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC003000; AAM14853.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09738.1; -; Genomic_DNA.
DR   RefSeq; NP_565915.2; NM_129544.4.
DR   AlphaFoldDB; F4IG09; -.
DR   SMR; F4IG09; -.
DR   STRING; 3702.AT2G39850.1; -.
DR   MEROPS; S08.A46; -.
DR   PaxDb; F4IG09; -.
DR   PRIDE; F4IG09; -.
DR   ProteomicsDB; 232799; -.
DR   EnsemblPlants; AT2G39850.1; AT2G39850.1; AT2G39850.
DR   GeneID; 818572; -.
DR   Gramene; AT2G39850.1; AT2G39850.1; AT2G39850.
DR   KEGG; ath:AT2G39850; -.
DR   Araport; AT2G39850; -.
DR   TAIR; locus:2061131; AT2G39850.
DR   eggNOG; ENOG502QRA7; Eukaryota.
DR   HOGENOM; CLU_000625_4_3_1; -.
DR   InParanoid; F4IG09; -.
DR   OMA; CENITCN; -.
DR   OrthoDB; 337164at2759; -.
DR   PRO; PR:F4IG09; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IG09; 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   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; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
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; PS00137; SUBTILASE_HIS; 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..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..106
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435225"
FT   CHAIN           107..?
FT                   /note="Subtilisin-like protease SBT4.1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003311433"
FT   PROPEP          ?..775
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435226"
FT   DOMAIN          29..105
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          110..606
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          365..459
FT                   /note="PA"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        136
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        196
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        551
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        601
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   775 AA;  87920 MW;  66852498047A4973 CRC64;
     MAIAFHTFLL QLLLFFFASF AEANDSRKTY LVQMKVGGHR YGSSSGHQEL LGEVLDDDST
     LADAFIYSYK ESFTGFSASL TPRERQKLMR RREVLEVSRS RNLKLQTTRS WDFMNLTLKA
     ERNPENESDL VVAVIDSGIW PYSELFGSDS PPPPGWENKC ENITCNNKIV GARSYYPKKE
     KYKWVEEKSV IDVTGHGTHV ASIVAGRKVE KAGYFGLAEG TMRGGVPNAK IAVYKTCWRV
     IRKNGREDSV CREDNILKAI DDAIADKVDI ISYSQGFQFT PLQKDKVSWA FLRALKNGIL
     TSAAAGNYAN NGKFYYTVAN GAPWVMTVAA SLKDRIFETK LELEGEDKPI IVYDTINTFE
     TQDSFYPLLN EKAPPESTRK RELIAERNGY SILSNYDEKD KGKDVFFEFA QINLLDEAIK
     EREKGAIVLG GKSYDFNESI KLQFPIASIF LDEQKKGKLW DYYKKDQSKE RLAKIHKTEE
     IPREEGWVPT VAHLSSRGPN CDSFLANILK PDIAAPGLDI IAGWPENVKL SSDRPANDYR
     HLRFNIMSGT SMACPHATGL ALYLKSFKRW SPSAIKSALM TTSSEMTDDD NEFAYGSGHL
     NATKVRDPGL VYETHYQDYI DYLCKLGYNT EKLRSHVGSD KIDCSKTEID HDADLNYPTM
     TARVPLPLDT PFKKVFHRTV TNVNDGEFTY LREINYRGDK DFDEIIVDPP QLKFSELGET
     KTFTVTVTGI SKRNWNKNRA FMTRNTWLTW TEKDGSRQVR SPIVIYSIKG PKACM
 
 
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