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 02-SEP-2026, entry version 143. DE RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027}; DE EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027}; 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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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 Evidence={ECO:0000256|PROSITE-ProRule:PRU10027}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[tau protein] + ATP = O-phospho-L-seryl-[tau protein] CC + ADP + H(+); 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:ARBA00048291}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU10027}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[tau protein] + ATP = O-phospho-L-threonyl-[tau CC protein] + ADP + H(+); 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:ARBA00048878}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. GSK-3 subfamily. CC {ECO:0000256|ARBA:ARBA00005527}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 OrthoDB; 272141at2759; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC. DR GO; GO:0051093; P:negative regulation of developmental process; IEA:UniProtKB-ARBA. DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-ARBA. DR CDD; cd14137; STKc_GSK3; 1. DR FunFam; 1.10.510.10:FF:000055; Glycogen synthase kinase-3 beta; 1. DR FunFam; 3.30.200.20:FF:000009; Glycogen synthase kinase-3 beta; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR050591; GSK-3. 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, ECO:0000256|PROSITE- KW ProRule:PRU00159}; 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|PROSITE-ProRule:PRU00159}; KW Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00159}. 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 1..15 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..82 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 450..478 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 244 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10027" 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 //