BSK12_ARATH
ID BSK12_ARATH Reviewed; 465 AA.
AC Q7XJT7;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable inactive receptor-like kinase BSK12 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 12 {ECO:0000305};
DE AltName: Full=Protein SHORT SUSPENSOR {ECO:0000303|PubMed:19286558};
GN Name=BSK12 {ECO:0000305}; Synonyms=SSP {ECO:0000303|PubMed:19286558};
GN OrderedLocusNames=At2g17090; ORFNames=F6P23.23;
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=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 MYRISTOYLATION AT GLY-2.
RX PubMed=12912986; DOI=10.1074/jbc.m307321200;
RA Boisson B., Giglione C., Meinnel T.;
RT "Unexpected protein families including cell defense components feature in
RT the N-myristoylome of a higher eukaryote.";
RL J. Biol. Chem. 278:43418-43429(2003).
RN [4]
RP FUNCTION, MUTAGENESIS OF GLY-2; 3-CYS-CYS-4; LYS-78; 300-TYR--LYS-465 AND
RP 431-TRP--LYS-465, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-3 AND
RP CYS-4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19286558; DOI=10.1126/science.1167784;
RA Bayer M., Nawy T., Giglione C., Galli M., Meinnel T., Lukowitz W.;
RT "Paternal control of embryonic patterning in Arabidopsis thaliana.";
RL Science 323:1485-1488(2009).
RN [5]
RP INTERACTION WITH YDA.
RX PubMed=28821747; DOI=10.1038/s41598-017-08230-4;
RA Yuan G.L., Li H.J., Yang W.C.;
RT "The integration of Gbeta and MAPK signaling cascade in zygote
RT development.";
RL Sci. Rep. 7:8732-8732(2017).
CC -!- FUNCTION: Probable inactive protein kinase that activates the YODA MAP
CC kinase cascade, which regulates the asymmetric first division and
CC embryo polarity, by promoting the elongation of the zygote and the
CC development of its basal daughter cell into the extra-embryonic
CC suspensor. Acts as an adapter at the plasma membrane, possibly by
CC recruiting and binding an activator. {ECO:0000269|PubMed:19286558}.
CC -!- SUBUNIT: Interacts with YDA. {ECO:0000269|PubMed:28821747}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19286558};
CC Lipid-anchor {ECO:0000269|PubMed:19286558}.
CC -!- TISSUE SPECIFICITY: Expressed at the mRNA level in the sperm cells in
CC mature pollen, but the protein is only detectable in the zygote and the
CC micropylar endosperm upon fertilization. {ECO:0000269|PubMed:19286558}.
CC -!- DEVELOPMENTAL STAGE: Transiently expressed at the protein level in the
CC zygote upon fertilization. No longer detected by the time of the first
CC division. {ECO:0000269|PubMed:19286558}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- PTM: Diacylation-mediated membrane association is essential for BSK12
CC function. {ECO:0000269|PubMed:19286558}.
CC -!- MISCELLANEOUS: BSK12 exerts a paternal effect on embryonic patterning.
CC Transcripts produced but not translated in the sperm cells are
CC delivered to the seed where they become translated, resulting in a
CC transient accumulation of the protein in both products of the double
CC fertilization, the zygote and the central cell.
CC {ECO:0000269|PubMed:19286558}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; CP002685; AEC06585.1; -; Genomic_DNA.
DR PIR; A84548; A84548.
DR RefSeq; NP_179301.1; NM_127264.2.
DR AlphaFoldDB; Q7XJT7; -.
DR SMR; Q7XJT7; -.
DR STRING; 3702.AT2G17090.1; -.
DR iPTMnet; Q7XJT7; -.
DR PaxDb; Q7XJT7; -.
DR PRIDE; Q7XJT7; -.
DR EnsemblPlants; AT2G17090.1; AT2G17090.1; AT2G17090.
DR GeneID; 816214; -.
DR Gramene; AT2G17090.1; AT2G17090.1; AT2G17090.
DR KEGG; ath:AT2G17090; -.
DR Araport; AT2G17090; -.
DR TAIR; locus:2827634; AT2G17090.
DR eggNOG; ENOG502QQT6; Eukaryota.
DR HOGENOM; CLU_000288_15_0_1; -.
DR InParanoid; Q7XJT7; -.
DR OMA; AHETIHG; -.
DR OrthoDB; 478216at2759; -.
DR PhylomeDB; Q7XJT7; -.
DR PRO; PR:Q7XJT7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7XJT7; baseline and differential.
DR Genevisible; Q7XJT7; AT.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IBA:GO_Central.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010098; P:suspensor development; IMP:TAIR.
DR GO; GO:0080159; P:zygote elongation; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR045845; BSK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR45863; PTHR45863; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Brassinosteroid signaling pathway; Cell membrane;
KW Developmental protein; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12912986,
FT ECO:0000305|PubMed:19286558"
FT CHAIN 2..465
FT /note="Probable inactive receptor-like kinase BSK12"
FT /id="PRO_0000378324"
FT DOMAIN 50..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 78
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:0000269|PubMed:12912986,
FT ECO:0000305|PubMed:19286558"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:19286558"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:19286558"
FT MUTAGEN 2
FT /note="G->A: Loss of both N-myristoylation and S-
FT palmitoylation; cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:19286558"
FT MUTAGEN 3..4
FT /note="CC->SS: No effect on N-myristoylation in vitro, but
FT cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:19286558"
FT MUTAGEN 78
FT /note="K->R: No effect."
FT /evidence="ECO:0000269|PubMed:19286558"
FT MUTAGEN 300..465
FT /note="Missing: Loss of function."
FT /evidence="ECO:0000269|PubMed:19286558"
FT MUTAGEN 431..465
FT /note="Missing: Loss of function."
FT /evidence="ECO:0000269|PubMed:19286558"
SQ SEQUENCE 465 AA; 52281 MW; FD4C7A97D162DC39 CRC64;
MGCCYSLSST VDPVQDHTTD ASSEPRNGGG EDPPLTKFSF SALKTATNHF SPENIVSDQT
SDVVFKGRLQ NGGFVAIKRF NNMAWSDPKL FLEEAQRVGK LRHKRLVNLI GYCCDGDKRF
LVADFMANDT LAKRLFQRKY QTMDWSIRLR VAYFVAEALD YCNTAGFASY NNLSAYKVLF
DEDGDACLSC FGLMKEINND QITTGSVNPE NVIYRFGTVL VNLLSGKQIP PSHAPEMIHR
KNVFKLMDPY LKGKFSIDEA NVVYKLASQC LKYEGQESPN TKEIVATLET LQTRTEAPSY
EVVEMTNQEK DASSSSNLSP LGEACLRMDL ASIHSILVLA GYDDDKDIIE LSFEEWIQEV
KELQDVRRNG DRAFVEQDFK TAIACYSQFV EERSLVYPSV YARRSLSYLF CDEPEKALLD
GMHAQGVFPD WPTAFYLQSV ALAKLDMNTD SADTLKEAAL LEVKK
