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SBT3C_ARATH
ID   SBT3C_ARATH             Reviewed;         754 AA.
AC   F4JJH5; A7Y5V8; O81899;
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 SBT3.12 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE   AltName: Full=Subtilase subfamily 3 member 12 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT3.12 {ECO:0000303|PubMed:16193095};
DE   Flags: Precursor;
GN   Name=SBT3.12 {ECO:0000303|PubMed:16193095};
GN   OrderedLocusNames=At4g21326 {ECO:0000312|Araport:AT4G21326};
GN   ORFNames=T6K22.50 {ECO:0000312|EMBL:CAA20197.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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 [GENOMIC DNA] OF 61-754.
RC   STRAIN=cv. Cvi-0;
RX   PubMed=17656687; DOI=10.1126/science.1143153;
RA   Tang C., Toomajian C., Sherman-Broyles S., Plagnol V., Guo Y.-L., Hu T.T.,
RA   Clark R.M., Nasrallah J.B., Weigel D., Nordborg M.;
RT   "The evolution of selfing in Arabidopsis thaliana.";
RL   Science 317:1070-1072(2007).
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).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA20197.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g21320 has been split into 3 genes: At4g21320, At4g21323 and At4g21326.; Evidence={ECO:0000305};
CC       Sequence=CAB79131.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g21320 has been split into 3 genes: At4g21320, At4g21323 and At4g21326.; Evidence={ECO:0000305};
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DR   EMBL; AL031187; CAA20197.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161554; CAB79131.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; EF637083; ABV21208.1; -; Genomic_DNA.
DR   PIR; T05174; T05174.
DR   AlphaFoldDB; F4JJH5; -.
DR   SMR; F4JJH5; -.
DR   STRING; 3702.AT4G21326.1; -.
DR   MEROPS; S08.A30; -.
DR   MEROPS; S08.A32; -.
DR   PaxDb; F4JJH5; -.
DR   PeptideAtlas; F4JJH5; -.
DR   PRIDE; F4JJH5; -.
DR   ProteomicsDB; 232690; -.
DR   Araport; AT4G21326; -.
DR   TAIR; locus:505006504; AT4G21326.
DR   eggNOG; ENOG502QSF0; Eukaryota.
DR   HOGENOM; CLU_369061_0_0_1; -.
DR   InParanoid; F4JJH5; -.
DR   PhylomeDB; F4JJH5; -.
DR   PRO; PR:F4JJH5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JJH5; 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; IPR041469; Subtilisin-like_FN3.
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..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..117
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435208"
FT   CHAIN           118..?
FT                   /note="Subtilisin-like protease SBT3.12"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003311531"
FT   PROPEP          ?..754
FT                   /evidence="ECO:0000250|UniProtKB:Q39547"
FT                   /id="PRO_0000435209"
FT   DOMAIN          39..116
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          121..606
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        151
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        224
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        537
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        629
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        740
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        167
FT                   /note="E -> G (in Ref. 3; ABV21208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        399
FT                   /note="G -> S (in Ref. 3; ABV21208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        726
FT                   /note="G -> D (in Ref. 3; ABV21208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        749
FT                   /note="I -> T (in Ref. 3; ABV21208)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   754 AA;  81507 MW;  51D01AFA87832E15 CRC64;
     MGIVKGRSRA GLFIGFLFIV NVGFCVFAQE SSNEERKIYV VHLGVRRHDD SELVSESHQR
     MLESVFESAE AARESIVYNY HHGFSGFAAR LTDSQAKQLS DRPDVFSVAP NRKVELQSTR
     IYDYLGLSPS FPSGVLHESN MGSDLVIGFL DSGVWPESPA YNDEGLEPIP KHWKGKCVAG
     EDFDPAKHCN KKLVGAKYFT DGFDENNSGI SEEDFMSPRG YRGHGTMVSS IAASSFVPNV
     SYGGLAPGVM RGAAPKARIA MYKIVWDRAL LMSSTATMVK AFDEAINDGV DVLSISLASA
     APFRPIDSIT GDLELGSFHA VMKGIPVIAG ASNTGPEAYT VANVFPWMLT VAATNIDRTF
     YADMTFGNNI TIIGQAQYTG KEVSAGLVYI EHYKTDTSGM LGKVVLTFVK EDWEMASALA
     TTTINKAAGL IVARSGDYQS DIVYNQPFIY VDYEVGAKIL RYIRSSSSPT IKISTGKTLV
     GRPIATQVCG FSSRGPNGLS PAILKPDIAA PGVTILGATS QAYPDSFGGY FLGTGTSYAT
     PVVAGLVVLL KALHPDWSPA ALKSAIMTTA WKTDPSGEPI FAEGEPRKLA DPFDYGAGLV
     NAERAKDPGL VYDMNIDDYI HYFCATGYND TSITIITGKP TKCSSPLPSI LDLNYPAITI
     PDLEEEVTVT RTVTNVGPVD SVYRAVVEPP RGVEIVVEPE TLVFCSNTKK LGFKVRVSSS
     HKSNTGFFFG SFTWTDGTRN VTIPLSVRIR VLNP
 
 
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