PHKG1_RAT
ID PHKG1_RAT Reviewed; 388 AA.
AC P13286;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform;
DE EC=2.7.11.19;
DE AltName: Full=Phosphorylase kinase subunit gamma-1;
DE AltName: Full=Serine/threonine-protein kinase PHKG1;
DE EC=2.7.11.1;
DE EC=2.7.11.26;
GN Name=Phkg1; Synonyms=Phkg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3357797; DOI=10.1093/nar/16.5.2355;
RA Cawley K.C., Ramachandran C., Gorin F.A., Walsh D.A.;
RT "Nucleotide sequence of cDNA encoding the catalytic subunit of
RT phosphorylase kinase from rat soleus muscle.";
RL Nucleic Acids Res. 16:2355-2356(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=8419323; DOI=10.1016/s0021-9258(18)54059-x;
RA Cawley K.C., Akita C.G., Angelos K.L., Walsh D.A.;
RT "Characterization of the gene for rat phosphorylase kinase catalytic
RT subunit.";
RL J. Biol. Chem. 268:1194-1200(1993).
CC -!- FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which
CC mediates the neural and hormonal regulation of glycogen breakdown
CC (glycogenolysis) by phosphorylating and thereby activating glycogen
CC phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43
CC and NRGN/RC3 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + phosphorylase b = 2 ADP + phosphorylase a.;
CC EC=2.7.11.19;
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 -!- 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;
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 -!- SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha,
CC beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB)
CC are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic
CC subunit, and delta is calmodulin.
CC -!- DOMAIN: The two calmodulin-binding domains appear to act in concert to
CC bind a single molecule of calmodulin and are
CC pseudosubstrate/autoinhibitory domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; X07320; CAA30280.1; -; mRNA.
DR PIR; S00731; S00731.
DR RefSeq; NP_113761.1; NM_031573.1.
DR AlphaFoldDB; P13286; -.
DR SMR; P13286; -.
DR BioGRID; 248008; 1.
DR STRING; 10116.ENSRNOP00000001222; -.
DR iPTMnet; P13286; -.
DR PhosphoSitePlus; P13286; -.
DR PaxDb; P13286; -.
DR PRIDE; P13286; -.
DR Ensembl; ENSRNOT00000001222; ENSRNOP00000001222; ENSRNOG00000000920.
DR GeneID; 29353; -.
DR KEGG; rno:29353; -.
DR CTD; 5260; -.
DR RGD; 3325; Phkg1.
DR eggNOG; KOG0599; Eukaryota.
DR GeneTree; ENSGT00940000158139; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; P13286; -.
DR OMA; YQYRRAK; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; P13286; -.
DR TreeFam; TF320349; -.
DR BRENDA; 2.7.11.19; 5301.
DR Reactome; R-RNO-70221; Glycogen breakdown (glycogenolysis).
DR PRO; PR:P13286; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000920; Expressed in skeletal muscle tissue and 16 other tissues.
DR Genevisible; P13286; RN.
DR GO; GO:0005964; C:phosphorylase kinase complex; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:0004689; F:phosphorylase kinase activity; IDA:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0005977; P:glycogen metabolic process; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002291; Phosph_kin_gamma.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01049; PHOSPHBKNASE.
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; Calmodulin-binding; Carbohydrate metabolism;
KW Glycogen metabolism; Kinase; Muscle protein; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..388
FT /note="Phosphorylase b kinase gamma catalytic chain,
FT skeletal muscle/heart isoform"
FT /id="PRO_0000086511"
FT DOMAIN 20..288
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 303..327
FT /note="Calmodulin-binding (domain-N)"
FT REGION 343..367
FT /note="Calmodulin-binding (domain-C)"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 388 AA; 45015 MW; 6ABA8A51D527C149 CRC64;
MTRDEALPDS HSAQNFYENY EPKEILGRGV SSVVRRCIHK PTCQEYAVKI IDITGGGSFS
SEEVQELREA TLKEVDILQK VSGHPNIIQL KDTYETNTFF FLVFDLMKRG ELFDYLTEKV
TLTEKETRKI MRALLEVVCT LHKLNIVHRD LKPENILLDD NMNIKLTDFG FSCQLQPGEK
LREVCGTPSY LAPEIIQCSM DEGHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR
MIMDGKYQFG SPEWDDYSDT VKDLVSRFLV VQPQDRCSAE EALAHPFFQE YVVEEVRHFS
PRGKFKVICL TVLASVRIYY QYRRVKPVTR EIVIRDPYAL RPLRRLIDAY AFRIYGHWVK
KGQQQNRAAL FENTPKAVLL SLAEEEDF
