PHKG1_RABIT
ID PHKG1_RABIT Reviewed; 387 AA.
AC P00518;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white;
RX PubMed=3609320; DOI=10.1016/0014-5793(87)80871-2;
RA da Cruz e Silva E.F., Cohen P.T.W.;
RT "Isolation and sequence analysis of a cDNA clone encoding the entire
RT catalytic subunit of phosphorylase kinase.";
RL FEBS Lett. 220:36-42(1987).
RN [2]
RP PROTEIN SEQUENCE OF 2-387.
RX PubMed=6541504; DOI=10.1021/bi00313a027;
RA Reimann E.M., Titani K., Ericsson L.H., Wade R.D., Fischer E.H.,
RA Walsh K.A.;
RT "Homology of the gamma subunit of phosphorylase b kinase with cAMP-
RT dependent protein kinase.";
RL Biochemistry 23:4185-4192(1984).
RN [3]
RP CALMODULIN-BINDING DOMAINS.
RX PubMed=2507540; DOI=10.1016/s0021-9258(18)71472-5;
RA Dasgupta M., Honeycutt T., Blumenthal D.K.;
RT "The gamma-subunit of skeletal muscle phosphorylase kinase contains two
RT noncontiguous domains that act in concert to bind calmodulin.";
RL J. Biol. Chem. 264:17156-17163(1989).
RN [4]
RP FUNCTION IN PHOSPHORYLATION OF GAP43 AND NRGN/RC3.
RX PubMed=8454596; DOI=10.1016/s0021-9258(18)53240-3;
RA Paudel H.K., Zwiers H., Wang J.H.;
RT "Phosphorylase kinase phosphorylates the calmodulin-binding regulatory
RT regions of neuronal tissue-specific proteins B-50 (GAP-43) and
RT neurogranin.";
RL J. Biol. Chem. 268:6207-6213(1993).
RN [5]
RP CALMODULIN-BINDING DOMAINS.
RX PubMed=7673209; DOI=10.1074/jbc.270.38.22283;
RA Dasgupta M., Blumenthal D.K.;
RT "Characterization of the regulatory domain of the gamma-subunit of
RT phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains
RT are also autoinhibitory.";
RL J. Biol. Chem. 270:22283-22289(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 16-292.
RX PubMed=7663944; DOI=10.1016/s0969-2126(01)00180-0;
RA Owen D.J., Noble M.E.M., Garman E.F., Papageorgiou A.C., Johnson L.N.;
RT "Two structures of the catalytic domain of phosphorylase kinase: an active
RT protein kinase complexed with substrate analogue and product.";
RL Structure 3:467-482(1995).
RN [7]
RP FUNCTION IN PHOSPHORYLATION OF MAPT.
RX PubMed=8999860; DOI=10.1016/s0021-9258(19)67481-8;
RA Paudel H.K.;
RT "The regulatory Ser262 of microtubule-associated protein tau is
RT phosphorylated by phosphorylase kinase.";
RL J. Biol. Chem. 272:1777-1785(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-299.
RX PubMed=9362479; DOI=10.1093/emboj/16.22.6646;
RA Lowe E.D., Noble M.E.M., Skamnaki V.T., Oikonomakos N.G., Owen D.J.,
RA Johnson L.N.;
RT "The crystal structure of a phosphorylase kinase peptide substrate complex:
RT kinase substrate recognition.";
RL EMBO J. 16:6646-6658(1997).
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. {ECO:0000269|PubMed:8454596, ECO:0000269|PubMed:8999860}.
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.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; Y00684; CAA68682.1; -; mRNA.
DR PIR; S00075; KIRBFG.
DR RefSeq; NP_001095175.1; NM_001101705.1.
DR RefSeq; XP_008247862.1; XM_008249640.2.
DR PDB; 1PHK; X-ray; 2.20 A; A=2-299.
DR PDB; 1QL6; X-ray; 2.40 A; A=2-299.
DR PDB; 2PHK; X-ray; 2.60 A; A=15-291.
DR PDBsum; 1PHK; -.
DR PDBsum; 1QL6; -.
DR PDBsum; 2PHK; -.
DR AlphaFoldDB; P00518; -.
DR SMR; P00518; -.
DR DIP; DIP-48334N; -.
DR IntAct; P00518; 2.
DR STRING; 9986.ENSOCUP00000011717; -.
DR iPTMnet; P00518; -.
DR Ensembl; ENSOCUT00000013615; ENSOCUP00000011717; ENSOCUG00000013618.
DR GeneID; 100009297; -.
DR KEGG; ocu:100009297; -.
DR CTD; 5260; -.
DR eggNOG; KOG0599; Eukaryota.
DR GeneTree; ENSGT00940000158139; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; P00518; -.
DR OMA; YQYRRAK; -.
DR OrthoDB; 330091at2759; -.
DR BRENDA; 2.7.11.19; 1749.
DR EvolutionaryTrace; P00518; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000013618; Expressed in skeletal muscle tissue and 10 other tissues.
DR GO; GO:0005964; C:phosphorylase kinase complex; IEA:InterPro.
DR GO; GO:0098723; C:skeletal muscle myofibril; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004689; F:phosphorylase kinase activity; IEA:UniProtKB-EC.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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 3D-structure; ATP-binding; Calmodulin-binding; Carbohydrate metabolism;
KW Direct protein sequencing; Glycogen metabolism; Kinase; Muscle protein;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6541504"
FT CHAIN 2..387
FT /note="Phosphorylase b kinase gamma catalytic chain,
FT skeletal muscle/heart isoform"
FT /id="PRO_0000086510"
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 TURN 17..19
FT /evidence="ECO:0007829|PDB:1PHK"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:1PHK"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:1PHK"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1PHK"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:1PHK"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:1QL6"
FT HELIX 61..81
FT /evidence="ECO:0007829|PDB:1PHK"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1PHK"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 124..143
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1PHK"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1PHK"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 210..225
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:1PHK"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:1PHK"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1PHK"
SQ SEQUENCE 387 AA; 44803 MW; 0EC8710C2A4C1BE8 CRC64;
MTRDAALPGS HSTHGFYENY EPKEILGRGV SSVVRRCIHK PTCKEYAVKI IDVTGGGSFS
AEEVQELREA TLKEVDILRK VSGHPNIIQL KDTYETNTFF FLVFDLMKKG ELFDYLTEKV
TLSEKETRKI MRALLEVICA LHKLNIVHRD LKPENILLDD DMNIKLTDFG FSCQLDPGEK
LREVCGTPSY LAPEIIECSM NDNHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR
MIMSGNYQFG SPEWDDYSDT VKDLVSRFLV VQPQKRYTAE EALAHPFFQQ YVVEEVRHFS
PRGKFKVICL TVLASVRIYY QYRRVKPVTR EIVIRDPYAL RPLRRLIDAY AFRIYGHWVK
KGQQQNRAAL FENTPKAVLF SLAEDDY
