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 27-MAR-2024, entry version 195. 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}. 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; 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; 10090-ENSMUSP00000026617; -. DR PeptideAtlas; P07934; -. DR ProteomicsDB; 287930; -. DR Antibodypedia; 2094; 337 antibodies from 32 providers. DR DNASU; 18682; -. DR Ensembl; ENSMUST00000026617.13; ENSMUSP00000026617.7; ENSMUSG00000025537.13. DR GeneID; 18682; -. DR KEGG; mmu:18682; -. DR UCSC; uc008ztm.1; mouse. DR AGR; MGI:97579; -. 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; 1121238at2759; -. 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 80 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 116 other cell types or tissues. DR ExpressionAtlas; P07934; baseline and differential. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24347:SF386; PHOSPHORYLASE B KINASE GAMMA CATALYTIC CHAIN, SKELETAL MUSCLE_HEART ISOFORM; 1. DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF12330; Haspin_kinase; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01049; PHOSPHBKNASE. 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. DR Genevisible; P07934; MM. 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 //