ID   A6QLB8_BOVIN            Unreviewed;       495 AA.
AC   A6QLB8; F1MHW8;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=[tau protein] kinase {ECO:0000256|ARBA:ARBA00012407};
DE            EC=2.7.11.26 {ECO:0000256|ARBA:ARBA00012407};
GN   Name=GSK3A {ECO:0000313|EMBL:AAI47909.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI47909.1};
RN   [1] {ECO:0000313|EMBL:AAI47909.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI47909.1};
RC   TISSUE=Uterus {ECO:0000313|EMBL:AAI47909.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC         COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC         Evidence={ECO:0000256|ARBA:ARBA00023955};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC         Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26; Evidence={ECO:0000256|ARBA:ARBA00023915};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. GSK-3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005527}.
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DR   EMBL; BC147908; AAI47909.1; -; mRNA.
DR   RefSeq; NP_001095662.1; NM_001102192.1.
DR   AlphaFoldDB; A6QLB8; -.
DR   SMR; A6QLB8; -.
DR   iPTMnet; A6QLB8; -.
DR   GeneID; 536561; -.
DR   KEGG; bta:536561; -.
DR   CTD; 2931; -.
DR   eggNOG; KOG0658; Eukaryota.
DR   HOGENOM; CLU_000288_181_20_1; -.
DR   TreeFam; TF101104; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0051093; P:negative regulation of developmental process; IEA:UniProt.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR   CDD; cd14137; STKc_GSK3; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR24057; GLYCOGEN SYNTHASE KINASE-3 ALPHA; 1.
DR   PANTHER; PTHR24057:SF14; GLYCOGEN SYNTHASE KINASE-3 ALPHA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          119..403
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   495 AA;  52263 MW;  DC13D3A3922F51C8 CRC64;
     MSGGAPSGGG PGGSGRARTS SFAEPGGGGG GGGGGPGGSA SGPGGSGGGK TSVGAMGGGV
     GASSSGGGPG GSGGGGSGGP GAGTSFPPPG VKLGRDSGKV TTVVATLGQG PERSQEVAYT
     DIKVIGSGSF GVVYQARLAD TRELVAIKKV LQDKRFKNRE LQIMRKLDHC NIVRLRYFFY
     SSGEKKDELY LNLVLEYVPE TVYRVARHFT KAKLSIPIIY VKVYMYQLFR SLAYIHSQGV
     CHRDIKPQNL LVDPDTAVLK LCDFGSAKQL VRGEPNVSYI CSRYYRAPEL IFGATDYTSS
     IDVWSAGCVL AELLLGQPIF PGDSGVDQLV EIIKVLGTPS REQIREMNPN YTEFKFPQIK
     AHPWTKVFKS RTPPEAIALC SSLLEYTPSS RLSPLEACAH SFFDELRCPG TQLPNNRPLP
     PLFNFSPGEL TIQPSLNAIL IPPHLRSPAG TASLTPSSQA LSEAQTSSDW QSTDNTATLP
     PGLHLLQPPH LLCPL
//