ID G1NNA0_MELGA Unreviewed; 1020 AA.
AC G1NNA0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Glycogen synthase kinase-3 beta {ECO:0000256|ARBA:ARBA00015835};
DE EC=2.7.11.26 {ECO:0000256|ARBA:ARBA00012407};
GN Name=GSK3B {ECO:0000313|Ensembl:ENSMGAP00000015110.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000015110.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000015110.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000015110.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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 AlphaFoldDB; G1NNA0; -.
DR Ensembl; ENSMGAT00000016059.3; ENSMGAP00000015110.3; ENSMGAG00000014288.3.
DR GeneTree; ENSGT00520000055635; -.
DR HOGENOM; CLU_350195_0_0_1; -.
DR TreeFam; TF313965; -.
DR Proteomes; UP000001645; Chromosome 1.
DR Bgee; ENSMGAG00000014288; Expressed in pectoralis major and 17 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProt.
DR CDD; cd15292; 7tmC_GPR156; 1.
DR CDD; cd14137; STKc_GSK3; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR041946; GPR156_7TM.
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:SF8; GLYCOGEN SYNTHASE KINASE-3 BETA; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01176; GABABRECEPTR.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 615..912
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 570..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 328..362
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 957..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1020 AA; 113217 MW; 9DBC98AC8EDE87F5 CRC64;
MELGFNCSDL CNGQPGFSDQ EQQQRMLQEF CTVTITSSDR SGKSSPSFSA ALLGVVWTFL
TGGVLLALFF LAFTIRFRKN RIVKMSSPNL NIVTLLGSGL TYTSAYLFGI QEQSLSSRKS
VEMLIQLRLC LLCVGTSLVF GPILGKSWRL YKVFTQRVPD KRVIIKDLQL LAMVAVLVLA
DAVLLFTWVF SDPVQCFRSR SVSLRSVLLL YGTYLAGLTD SVSSPPVNQS LTLIVGVNLI
FLVAGTVVLI HRFFRAWHNL LFGFTSGGIF VCTTTINCFI FVPQLRQWKA FEEENQTLSH
MAKYFSSPSR SYHSVYSEEQ LYQLIGEKNS MKQLLTEKNA MIESLQEQVN NAKEKLMRLM
SAEGGCSPAV PNPCTQSTGQ HCEKCSSTGD VPREHWPLDT EKDGQQTSSV LHALPHSPMP
LSSDAQDLWK HVSHVHELLE EPECSPTLLF DTRNSLERSP EHAQEYGMLA GKHPLEQDAS
AGVAGEHPPK VSYVSSEKLQ EVLQELSLDS RTCSPAFPTH TGGMCGAQGG HPAARSSLSP
YLTRRRRRVL LPPTSIDLPA SPCAWCTAGS RPGTRSHGEP PCLGPGREGD KDGSKVTTVV
ATPGQGPDRP QEVSYTDTKV IGNGSFGVVY QAKLCDSGEL VAIKKVLQDK RFKNRELQIM
RKLDHCNIVR LRYFFYSSGE KKDEVYLNLV LDYVPETVYR VARHYSRAKQ TLPMIYVKLY
MYQLFRSLAY IHSFGICHRD IKPQNLLLDP DTAVLKLCDF GSAKQLVRGE PNVSYICSRY
YRAPELIFGA TDYTSSIDVW SAGCVLAELL LGQPIFPGDS GVDQLVEIIK VLGTPTREQI
REMNPNYTEF KFPQIKAHPW TKDSSGTGHF TSGVRVFRPR TPPEAIALCS RLLEYTPTAR
LTPLEACAHS FFDELRDPNV KLPNGREKPA LFNFTTQELS SNPSLASILI PAHARNQAAA
STPTNATAAS GENTRPPASP APWHHPLWRP RVSRKERTGF SRPAFCSVSA HGHLDASCGR
//