ID   MSK3_MEDSA              Reviewed;         411 AA.
AC   P51139;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Glycogen synthase kinase-3 homolog MsK-3;
DE            EC=2.7.11.1;
GN   Name=MSK-3;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8401615; DOI=10.1111/j.1365-313x.1993.00847.x;
RA   Paz A., Jonak C., Boegre L., Meskiene I., Mairinger T., Szalay A.,
RA   Heberle-Bors E., Hirt H.;
RT   "The MsK family of alfalfa protein kinase genes encodes homologues of
RT   shaggy/glycogen synthase kinase-3 and shows differential expression
RT   patterns in plant organs and development.";
RL   Plant J. 3:847-856(1993).
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: Absent in leaves and petioles, very low levels are
CC       seen in the stems and roots while a moderate expression is seen in the
CC       nodes.
CC   -!- DEVELOPMENTAL STAGE: High levels are seen in early flower development,
CC       gradually decreases in later stages and is absent after fertilization.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. GSK-3 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA48472.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X68409; CAA48472.1; ALT_INIT; mRNA.
DR   PIR; S37642; S37642.
DR   AlphaFoldDB; P51139; -.
DR   SMR; P51139; -.
DR   BRENDA; 2.7.11.26; 3078.
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..411
FT                   /note="Glycogen synthase kinase-3 homolog MsK-3"
FT                   /id="PRO_0000086402"
FT   DOMAIN          74..358
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         80..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         234
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  46272 MW;  2754A9099551CA5E CRC64;
     MASGGVAPAS GFIDKNASSV GVEKLPEEMN DMKIRDDKEM EAATIVDGNG TETGHIIVTT
     IGGKNGQPKQ TISYMAERVV GHGSFGVVFQ AKCLETGETV AIKKVLQDKR YKNRELQTMR
     LLDHPNVVSL KHCFFSTTEK DELYLNLVLE YVPETVSRVI RHYNKMNQRM PMIYVKLYSY
     QICRALAYIH NSIGVCHRDI KPQNLLVNPH THQLKICDFG SAKVLVKGEP NISYICSRYY
     RAPELIFGAT EYTTAIDIWS AGCVLGELLL GQPLFPGESG VDQLVEIIKV LGTPTREEIK
     CMNPNYTEFK FPQIKAHPWH KIFHKRMPPE AVDLVSRLLQ YSPNLRSTAL EALVHPFYDD
     VRDPNTRLPN GRFLPPLFNF KVNELKGVPA EMLVKLVPPH ARKQCALFGS S