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Database: UniProt
Entry: G1NNA0_MELGA
LinkDB: G1NNA0_MELGA
Original site: G1NNA0_MELGA 
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
//
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