ID   KSGT_BRANA              Reviewed;         468 AA.
AC   O04160;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Shaggy-related protein kinase theta;
DE            EC=2.7.11.1;
DE   AltName: Full=ASK-theta;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Topas;
RX   PubMed=9804971; DOI=10.1016/s0167-4781(98)00187-0;
RA   Tichtinsky G., Tavares R., Takvorian A., Schwebel-Dugue N., Twell D.,
RA   Kreis M.;
RT   "An evolutionary conserved group of plant GSK-3/shaggy-like protein kinase
RT   genes preferentially expressed in developing pollen.";
RL   Biochim. Biophys. Acta 1442:261-273(1998).
CC   -!- FUNCTION: May mediate extracellular signals to regulate transcription
CC       in differentiating cells. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- TISSUE SPECIFICITY: In developing pollen.
CC   -!- PTM: Autophosphorylated mainly on threonine and serine residues.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR   EMBL; Y12674; CAA73214.1; -; mRNA.
DR   PIR; T08139; T08139.
DR   RefSeq; NP_001303200.1; NM_001316271.1.
DR   RefSeq; XP_013684319.1; XM_013828865.1.
DR   AlphaFoldDB; O04160; -.
DR   SMR; O04160; -.
DR   GeneID; 106388722; -.
DR   KEGG; bna:106388722; -.
DR   BRENDA; 2.7.11.26; 944.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd14137; STKc_GSK3; 1.
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   InterPro; IPR039192; STKc_GSK3.
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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..468
FT                   /note="Shaggy-related protein kinase theta"
FT                   /id="PRO_0000086227"
FT   DOMAIN          134..418
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        259
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         140..148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         294
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q39011"
SQ   SEQUENCE   468 AA;  52630 MW;  C9EA6E4F3CD71E97 CRC64;
     MNVMRRLKSI ASGRTSISSD PGVDSSLKRP KLDQDNDNLS SRGDDPMQVD QSTDMVVVSQ
     DTVAGTSNVP PPPDQLPEVM NDMRLREDEP HANRGEEDKD MEPPIVNGCG TETGQVITTT
     VGGRDGKPKQ TISYMAQRVV GTGSFGVVFQ AKCLETGEQV AIKKVLQDKR YKNRELQIMR
     LQDHPNVVRL RHSFFSTTDK DELYLNLVLE FVPETVYRAL KHYTKMNQHM PIILVQLYTY
     QICRALNYLH RVVGVCHRDI KPQNLLVNTH THQLKICDFG SAKMLVPGEP NISYICSRYY
     RAPELIFGAT EYTNAIDMWS GGCVMAELLL GQPLFPGESG IDQLVEIIKI LGTPTREEIR
     CMNPNYTEFK FPQIKAHPWH KIFHKRMPPE AVDLVSRLLQ YSPNLRCTAL EACAHPFFDD
     LRAPNVSLPN GRALPPLFNF TAQELAGAST ELRQRLIPAH CQGTGNSS