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SBT16_ARATH
ID   SBT16_ARATH             Reviewed;         764 AA.
AC   O49607;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Subtilisin-like protease SBT1.6 {ECO:0000303|PubMed:16193095};
DE            EC=3.4.21.- {ECO:0000305};
DE   AltName: Full=Subtilase subfamily 1 member 6 {ECO:0000303|PubMed:16193095};
DE            Short=AtSBT1.6 {ECO:0000303|PubMed:16193095};
DE   AltName: Full=Subtilisin-like serine protease 2 {ECO:0000303|PubMed:12702015};
DE            Short=At-SLP2 {ECO:0000303|PubMed:12702015};
DE   Flags: Precursor;
GN   Name=SBT1.6 {ECO:0000303|PubMed:16193095};
GN   Synonyms=SLP2 {ECO:0000303|PubMed:12702015};
GN   OrderedLocusNames=At4g34980 {ECO:0000312|Araport:AT4G34980};
GN   ORFNames=M4E13.40 {ECO:0000312|EMBL:CAA17763.1};
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=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 [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   TISSUE SPECIFICITY, AND INDUCTION BY METHYL JASMONATE.
RX   PubMed=12702015; DOI=10.1034/j.1399-3054.2003.00087.x;
RA   Golldack D., Vera P., Dietz K.J.;
RT   "Expression of subtilisin-like serine proteases in Arabidopsis thaliana is
RT   cell-specific and responds to jasmonic acid and heavy metals with
RT   developmental differences.";
RL   Physiol. Plantarum 118:64-73(2003).
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   -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers of mature
CC       plants. {ECO:0000269|PubMed:12702015}.
CC   -!- INDUCTION: By methyl jasmonate. {ECO:0000269|PubMed:12702015}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AL022023; CAA17763.1; -; Genomic_DNA.
DR   EMBL; AL161586; CAB80215.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86443.1; -; Genomic_DNA.
DR   EMBL; AY074375; AAL67071.1; -; mRNA.
DR   EMBL; AY096357; AAM19998.1; -; mRNA.
DR   PIR; T05768; T05768.
DR   RefSeq; NP_567972.1; NM_119664.3.
DR   AlphaFoldDB; O49607; -.
DR   SMR; O49607; -.
DR   STRING; 3702.AT4G34980.1; -.
DR   MEROPS; S08.A39; -.
DR   PaxDb; O49607; -.
DR   PRIDE; O49607; -.
DR   ProMEX; O49607; -.
DR   ProteomicsDB; 232957; -.
DR   EnsemblPlants; AT4G34980.1; AT4G34980.1; AT4G34980.
DR   GeneID; 829650; -.
DR   Gramene; AT4G34980.1; AT4G34980.1; AT4G34980.
DR   KEGG; ath:AT4G34980; -.
DR   Araport; AT4G34980; -.
DR   TAIR; locus:2131566; AT4G34980.
DR   eggNOG; ENOG502QPQR; Eukaryota.
DR   HOGENOM; CLU_000625_4_6_1; -.
DR   InParanoid; O49607; -.
DR   OMA; GRMFPVV; -.
DR   OrthoDB; 337164at2759; -.
DR   PhylomeDB; O49607; -.
DR   PRO; PR:O49607; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O49607; baseline and differential.
DR   Genevisible; O49607; AT.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008236; F:serine-type peptidase activity; ISS:TAIR.
DR   GO; GO:0009827; P:plant-type cell wall modification; TAS:TAIR.
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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Serine protease;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..764
FT                   /note="Subtilisin-like protease SBT1.6"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431965"
FT   DOMAIN          46..99
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          103..606
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          377..457
FT                   /note="PA"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        131
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        538
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        578
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   764 AA;  81046 MW;  EBB3827F26F33F50 CRC64;
     MASSTIVLLL FLSFPFISFA ASQAAKTFIF RIDGGSMPSI FPTHYHWYST EFAEESRIVH
     VYHTVFHGFS AVVTPDEADN LRNHPAVLAV FEDRRRELHT TRSPQFLGLQ NQKGLWSESD
     YGSDVIIGVF DTGIWPERRS FSDLNLGPIP KRWRGVCESG ARFSPRNCNR KIIGARFFAK
     GQQAAVIGGI NKTVEFLSPR DADGHGTHTS STAAGRHAFK ASMSGYASGV AKGVAPKARI
     AAYKVCWKDS GCLDSDILAA FDAAVRDGVD VISISIGGGD GITSPYYLDP IAIGSYGAAS
     KGIFVSSSAG NEGPNGMSVT NLAPWVTTVG ASTIDRNFPA DAILGDGHRL RGVSLYAGVP
     LNGRMFPVVY PGKSGMSSAS LCMENTLDPK QVRGKIVICD RGSSPRVAKG LVVKKAGGVG
     MILANGASNG EGLVGDAHLI PACAVGSNEG DRIKAYASSH PNPIASIDFR GTIVGIKPAP
     VIASFSGRGP NGLSPEILKP DLIAPGVNIL AAWTDAVGPT GLPSDPRKTE FNILSGTSMA
     CPHVSGAAAL LKSAHPDWSP AVIRSAMMTT TNLVDNSNRS LIDESTGKSA TPYDYGSGHL
     NLGRAMNPGL VYDITNDDYI TFLCSIGYGP KTIQVITRTP VRCPTTRKPS PGNLNYPSIT
     AVFPTNRRGL VSKTVIRTAT NVGQAEAVYR ARIESPRGVT VTVKPPRLVF TSAVKRRSYA
     VTVTVNTRNV VLGETGAVFG SVTWFDGGKH VVRSPIVVTQ MDTL
 
 
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