IBS1_ARATH
ID IBS1_ARATH Reviewed; 709 AA.
AC F4ICB6; Q9M9T8;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein IMPAIRED IN BABA-INDUCED STERILITY 1 {ECO:0000303|PubMed:15722464};
DE EC=2.7.11.- {ECO:0000255|PROSITE-ProRule:PRU00159};
GN Name=IBS1 {ECO:0000303|PubMed:15722464};
GN OrderedLocusNames=At1g18670 {ECO:0000312|Araport:AT1G18670};
GN ORFNames=F6A14.22 {ECO:0000312|EMBL:AAF27112.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=15722464; DOI=10.1105/tpc.104.029728;
RA Ton J., Jakab G., Toquin V., Flors V., Iavicoli A., Maeder M.N.,
RA Metraux J.-P., Mauch-Mani B.;
RT "Dissecting the beta-aminobutyric acid-induced priming phenomenon in
RT Arabidopsis.";
RL Plant Cell 17:987-999(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=22209872; DOI=10.1104/pp.111.191593;
RA Slaughter A., Daniel X., Flors V., Luna E., Hohn B., Mauch-Mani B.;
RT "Descendants of primed Arabidopsis plants exhibit resistance to biotic
RT stress.";
RL Plant Physiol. 158:835-843(2012).
CC -!- FUNCTION: Required for beta-aminobutyric acid (BABA)-induced resistance
CC (BABA-IR) against bacteria (e.g. P.syringae) and oomycetes (e.g.
CC H.parasitica) via priming for salicylate (SA)-dependent defense
CC responses such as pathogenesis-related PR-1 gene expression and
CC trailing necrosis. Involved in BABA-mediated sterility
CC (PubMed:15722464, PubMed:22209872). Necessary for the inheritance of
CC BABA-priming to next generation, especially for the primed to be primed
CC phenotype which consists in an enhanced second BABA-priming in
CC transgenerationally primed plants (PubMed:22209872).
CC {ECO:0000269|PubMed:15722464, ECO:0000269|PubMed:22209872}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000312|Araport:AT1G18670};
CC Name=1;
CC IsoId=F4ICB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4ICB6-2; Sequence=VSP_059055, VSP_059056;
CC -!- DISRUPTION PHENOTYPE: Impaired in beta-aminobutyric acid (BABA)-induced
CC sterility. Altered BABA-induced resistance (BABA-IR) against bacteria
CC (e.g. P.syringae) and oomycetes (e.g. H.parasitica) associated with
CC reduction in priming for salicylate (SA)-dependent defense responses
CC (e.g. trailing necrosis and pathogenesis-related PR-1 gene expression)
CC (PubMed:15722464, PubMed:22209872). Reduced primed to be primed
CC phenotype in transgenerationally primed plants exposed to a second
CC BABA-priming (PubMed:22209872). {ECO:0000269|PubMed:15722464,
CC ECO:0000269|PubMed:22209872}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Seeking past shelter - Issue
CC 196 of October 2017;
CC URL="https://web.expasy.org/spotlight/back_issues/196/";
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DR EMBL; AC011809; AAF27112.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29744.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58799.1; -; Genomic_DNA.
DR PIR; D86320; D86320.
DR RefSeq; NP_001321210.1; NM_001332357.1. [F4ICB6-2]
DR RefSeq; NP_173302.2; NM_101725.3. [F4ICB6-1]
DR AlphaFoldDB; F4ICB6; -.
DR SMR; F4ICB6; -.
DR STRING; 3702.AT1G18670.1; -.
DR iPTMnet; F4ICB6; -.
DR PaxDb; F4ICB6; -.
DR PRIDE; F4ICB6; -.
DR ProteomicsDB; 248568; -. [F4ICB6-1]
DR EnsemblPlants; AT1G18670.1; AT1G18670.1; AT1G18670. [F4ICB6-1]
DR EnsemblPlants; AT1G18670.2; AT1G18670.2; AT1G18670. [F4ICB6-2]
DR GeneID; 838448; -.
DR Gramene; AT1G18670.1; AT1G18670.1; AT1G18670. [F4ICB6-1]
DR Gramene; AT1G18670.2; AT1G18670.2; AT1G18670. [F4ICB6-2]
DR KEGG; ath:AT1G18670; -.
DR Araport; AT1G18670; -.
DR TAIR; locus:2034944; AT1G18670.
DR eggNOG; KOG0600; Eukaryota.
DR HOGENOM; CLU_000288_78_4_1; -.
DR InParanoid; F4ICB6; -.
DR OMA; KDEICVR; -.
DR PRO; PR:F4ICB6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4ICB6; baseline and differential.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1902290; P:positive regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Kinase; Lipoprotein; Myristate;
KW Nucleotide-binding; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..709
FT /note="Protein IMPAIRED IN BABA-INDUCED STERILITY 1"
FT /id="PRO_0000441251"
FT DOMAIN 131..418
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 53..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 137..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 660..662
FT /note="GYE -> VRL (in isoform 2)"
FT /id="VSP_059055"
FT VAR_SEQ 663..709
FT /note="Missing (in isoform 2)"
FT /id="VSP_059056"
SQ SEQUENCE 709 AA; 79535 MW; 4622C8C118FA9AEF CRC64;
MGCVNSKQTV SVTPAIDHSG VFRDNVCSGS GRIVVEDLPP VTETKLLSWW SKSGKKSSSK
KSGSELGSDF GELSESGRAS SNCRSESVSF RLGNLSKYLE AEQVAAGWPA WLSNVAGEAI
HGWVPFRSDA FEKLEKIGQG TYSSVFRARE TETGRIVALK KVRFDNFEPE SVRFMAREIL
ILRKLNHPNI IKLEGIVTSK LSCSIHLVFE YMEHDLTGLL SSPDIDFTTP QIKCYMKQLL
SGLDHCHARG VMHRDIKGSN LLVNNEGILK VADFGLANFC NASGNKQPLT SRVVTLWYRP
PELLLGATEY GASVDLWSVG CVFAELLIGK PVLQGRTEVE QLHKIFKLCG SPPEDYWKKS
KLPHAMLFKP QQHYDGCLRE TLKLKGLSDA DINLIETLLS IQPHKRGTAS TALVSQYFTS
KPFACDPSSL PVYSPSKEID AKHREDTTRK KISGNGRRGT ESRKPTRKPP AFAKLAPAED
VRHHSQKFQK RNGHSVHNSI DSDSTLFEKM QKPSNHEKDE ASHVKNASQG DVPFSGPLQV
SVSSGFAWAK RRKDDICVRS HNRSLSRGHI PNLLGPSPAF SENTDVDSKN NEKEKEEKHG
ERTDSQDREA YEMLKLSMLK KWRQLERPDS FGGSDEYHSQ ELSLELYQRE EKAAKLGHLG
YEDNDEKIEF SGPLLSKSYG VDELLERHER QIRQLVRKSW FQKGKKQGK
