PHKG2_RAT
ID PHKG2_RAT Reviewed; 406 AA.
AC P31325; A1A5L8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Phosphorylase b kinase gamma catalytic chain, liver/testis isoform;
DE Short=PHK-gamma-LT;
DE Short=PHK-gamma-T;
DE EC=2.7.11.19;
DE AltName: Full=Phosphorylase kinase subunit gamma-2;
GN Name=Phkg2;
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], AND FUNCTION IN PHOSPHORYLATION OF PYGM.
RX PubMed=1370475; DOI=10.1016/s0021-9258(18)45967-4;
RA Calalb M.B., Fox D.T., Hanks S.K.;
RT "Molecular cloning and enzymatic analysis of the rat homolog of 'PhK-gamma
RT T,' an isoform of phosphorylase kinase catalytic subunit.";
RL J. Biol. Chem. 267:1455-1463(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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. May regulate glycogeneolysis in the testis. In vitro,
CC phosphorylates PYGM. {ECO:0000269|PubMed:1370475}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + phosphorylase b = 2 ADP + phosphorylase a.;
CC EC=2.7.11.19;
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; M73808; AAA41863.1; -; mRNA.
DR EMBL; BC128715; AAI28716.1; -; mRNA.
DR PIR; A42034; A42034.
DR RefSeq; NP_542151.1; NM_080584.4.
DR RefSeq; XP_008758077.1; XM_008759855.2.
DR AlphaFoldDB; P31325; -.
DR SMR; P31325; -.
DR BioGRID; 250831; 1.
DR STRING; 10116.ENSRNOP00000025419; -.
DR PaxDb; P31325; -.
DR Ensembl; ENSRNOT00000087142; ENSRNOP00000072734; ENSRNOG00000018725.
DR GeneID; 140671; -.
DR KEGG; rno:140671; -.
DR UCSC; RGD:620024; rat.
DR CTD; 5261; -.
DR RGD; 620024; Phkg2.
DR eggNOG; KOG0599; Eukaryota.
DR GeneTree; ENSGT00940000160435; -.
DR InParanoid; P31325; -.
DR OMA; QFRSPEW; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; P31325; -.
DR TreeFam; TF320349; -.
DR BRENDA; 2.7.11.19; 5301.
DR Reactome; R-RNO-70221; Glycogen breakdown (glycogenolysis).
DR PRO; PR:P31325; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018725; Expressed in testis and 20 other tissues.
DR Genevisible; P31325; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:0004689; F:phosphorylase kinase activity; IDA:RGD.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:Ensembl.
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 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; Carbohydrate metabolism;
KW Glycogen metabolism; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..406
FT /note="Phosphorylase b kinase gamma catalytic chain,
FT liver/testis isoform"
FT /id="PRO_0000086514"
FT DOMAIN 24..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 306..330
FT /note="Calmodulin-binding (domain-N)"
FT /evidence="ECO:0000250"
FT REGION 346..370
FT /note="Calmodulin-binding (domain-C)"
FT /evidence="ECO:0000250"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 406 AA; 46678 MW; 7D5DB86B8E8D5BDA CRC64;
MTLDVGPEDE LPDWAAAKEF YQKYDPKDII GRGVSSVVRR CVHRATGDEF AVKIMEVSAE
RLSLEQLEEV RDATRREMHI LRQVAGHPHI ITLIDSYESS SFMFLVFDLM RKGELFDYLT
EKVALSEKET RSIMRSLLEA VNFLHVNNIV HRDLKPENIL LDDNMQIRLS DFGFSCHLEP
GEKLRELCGT PGYLAPEILK CSMDETHPGY GKEVDLWACG VILFTLLAGS PPFWHRRQIL
MLRMIMEGQY QFSSPEWDDR SNTVKDLIAK LLQVDPNARL TAEQALQHPF FERCKGSQPW
NLTPRQRFRV AVWTILAAGR VALSSHRLRP LTKNALLRDP YALRPVRRLI DNCAFRLYGH
WVKKGEQQNR AALFQHQPPR PFPIIATDLE GDSSAITEDE VTLVRS
