PHKG1_MOUSE
ID PHKG1_MOUSE Reviewed; 388 AA.
AC P07934;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3472241; DOI=10.1073/pnas.84.9.2886;
RA Chamberlain J.S., Vantuinen P., Reeves A.A., Philip B.A., Caskey C.T.;
RT "Isolation of cDNA clones for the catalytic gamma subunit of mouse muscle
RT phosphorylase kinase: expression of mRNA in normal and mutant Phk mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2886-2890(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3597394; DOI=10.1016/s0021-9258(18)47485-6;
RA Bender P.K., Emerson C.P. Jr.;
RT "Skeletal muscle phosphorylase kinase catalytic subunit mRNAs are expressed
RT in heart tissue but not in liver.";
RL J. Biol. Chem. 262:8799-8805(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Muscle;
RX PubMed=8486349; DOI=10.1006/geno.1993.1151;
RA Maichele A.J., Farwell N.J., Chamberlain J.S.;
RT "A B2 repeat insertion generates alternate structures of the mouse muscle
RT gamma-phosphorylase kinase gene.";
RL Genomics 16:139-149(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; L08059; AAB59721.1; -; Genomic_DNA.
DR EMBL; L08057; AAB59721.1; JOINED; Genomic_DNA.
DR EMBL; L08058; AAB59721.1; JOINED; Genomic_DNA.
DR EMBL; M16216; AAA39926.1; -; mRNA.
DR EMBL; J03293; AAA39925.1; -; mRNA.
DR EMBL; S60494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S60492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S60493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055102; AAH55102.1; -; mRNA.
DR CCDS; CCDS19701.1; -.
DR PIR; A29872; A29872.
DR RefSeq; NP_035209.1; NM_011079.3.
DR AlphaFoldDB; P07934; -.
DR SMR; P07934; -.
DR BioGRID; 202146; 4.
DR IntAct; P07934; 2.
DR MINT; P07934; -.
DR STRING; 10090.ENSMUSP00000026617; -.
DR PhosphoSitePlus; P07934; -.
DR MaxQB; P07934; -.
DR PaxDb; P07934; -.
DR PeptideAtlas; P07934; -.
DR PRIDE; P07934; -.
DR ProteomicsDB; 287930; -.
DR Antibodypedia; 2094; 313 antibodies from 32 providers.
DR DNASU; 18682; -.
DR Ensembl; ENSMUST00000026617; ENSMUSP00000026617; ENSMUSG00000025537.
DR GeneID; 18682; -.
DR KEGG; mmu:18682; -.
DR UCSC; uc008ztm.1; mouse.
DR CTD; 5260; -.
DR MGI; MGI:97579; Phkg1.
DR VEuPathDB; HostDB:ENSMUSG00000025537; -.
DR eggNOG; KOG0599; Eukaryota.
DR GeneTree; ENSGT00940000158139; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; P07934; -.
DR OMA; CHYRRAK; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; P07934; -.
DR TreeFam; TF320349; -.
DR BRENDA; 2.7.11.19; 3474.
DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR BioGRID-ORCS; 18682; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Phkg1; mouse.
DR PRO; PR:P07934; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P07934; protein.
DR Bgee; ENSMUSG00000025537; Expressed in hindlimb stylopod muscle and 113 other tissues.
DR ExpressionAtlas; P07934; baseline and differential.
DR Genevisible; P07934; MM.
DR GO; GO:0005964; C:phosphorylase kinase complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004689; F:phosphorylase kinase activity; IMP:MGI.
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:0005980; P:glycogen catabolic process; ISO:MGI.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
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 1: Evidence at protein 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_0000086509"
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"
FT CONFLICT 313
FT /note="L -> V (in Ref. 1; AAA39926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 44960 MW; 96E1256891E43718 CRC64;
MTRDDALPDS HSAQTFYENY EPKEILGRGV SSVVRRCIHK PTCQEYAVKI IDITGGGSFS
SEEVQELREA TLKEVDILQK VSGHPNIIQL KDTYETNTFF FLVFDLMKRG ELFDYLTEKV
TLTEKETRKI MRALLEVICT LHKLNIVHRD LKPENILLDD NMNIKLTDFG FSCQLQPGEK
LREVCGTPSY LAPEIIQCSM DDGHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR
MIMDGKYQFG SPEWDDYSDT VKDLVSRFLV VQPQDRCSAE EALAHPFFQE YVVEEVRHFS
PRGKFKVICL TVLASVKIYY QYRRVKPVTR EIVIRDPYAL RPLRRLIDAY AFRIYGHWVK
KGQQQNRAAL FENTPKAVLL SLAEEEDF
