PHKG2_BOVIN
ID PHKG2_BOVIN Reviewed; 406 AA.
AC Q2KJ16; A7E3T5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 (By similarity). {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; BT030706; ABS45022.1; -; mRNA.
DR EMBL; BC105568; AAI05569.1; -; mRNA.
DR RefSeq; NP_001039593.1; NM_001046128.1.
DR AlphaFoldDB; Q2KJ16; -.
DR SMR; Q2KJ16; -.
DR STRING; 9913.ENSBTAP00000004433; -.
DR PaxDb; Q2KJ16; -.
DR PRIDE; Q2KJ16; -.
DR Ensembl; ENSBTAT00000004433; ENSBTAP00000004433; ENSBTAG00000003417.
DR GeneID; 512670; -.
DR KEGG; bta:512670; -.
DR CTD; 5261; -.
DR VEuPathDB; HostDB:ENSBTAG00000003417; -.
DR VGNC; VGNC:32834; PHKG2.
DR eggNOG; KOG0599; Eukaryota.
DR GeneTree; ENSGT00940000160435; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q2KJ16; -.
DR OMA; QFRSPEW; -.
DR OrthoDB; 330091at2759; -.
DR TreeFam; TF320349; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000003417; Expressed in spermatid and 106 other tissues.
DR ExpressionAtlas; Q2KJ16; baseline.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005964; C:phosphorylase kinase complex; IEA:InterPro.
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:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:Ensembl.
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 2: Evidence at transcript 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_0000244591"
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; 46542 MW; E0B8F8494DF8A58E CRC64;
MTLDVGPEDE LPDWAAAKEF YQKYDPKDVI GRGVSSVVRR CVHRATGQEF AVKIMEVTAE
RLSPEQLEEV REATRRETHI LRQVAGHPHI ITLIDSYESS SFMFLVFDLM RKGELFDYLT
EKVALSEKET RSIMRSLLEA VSFLHNNNIV HRDLKPENIL LDDNMQIRLS DFGFSCHLEP
GEKLRELCGT PGYLAPEILK CSMDETHPGY GKEVDLWACG VILFTLLAGS PPFWHRRQIL
MLRMIMEGQY QFSSPEWDDR SDTVKDLISR LLQVDPVERL TAEQALQHPF FERCEGSQAW
NLTPRQRFRV AVWTVLAAGR VALSAHRIRP LTKSALLRDP YALRPVRRLI DNCAFRLYGH
WVKKGEQQNR AALFQHRPPG PFPMMGPEEE GDSATIAEDE AMLVLG
