PHKG2_MOUSE
ID PHKG2_MOUSE Reviewed; 406 AA.
AC Q9DB30; A6H632;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 151.
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 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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
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; AK005277; BAB23926.1; -; mRNA.
DR EMBL; CH466531; EDL17548.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL17549.1; -; Genomic_DNA.
DR EMBL; BC138913; AAI38914.1; -; mRNA.
DR EMBL; BC145734; AAI45735.1; -; mRNA.
DR CCDS; CCDS21869.1; -.
DR RefSeq; NP_081164.2; NM_026888.3.
DR RefSeq; XP_006508230.1; XM_006508167.3.
DR RefSeq; XP_011240193.1; XM_011241891.1.
DR AlphaFoldDB; Q9DB30; -.
DR SMR; Q9DB30; -.
DR BioGRID; 213142; 2.
DR STRING; 10090.ENSMUSP00000033086; -.
DR iPTMnet; Q9DB30; -.
DR PhosphoSitePlus; Q9DB30; -.
DR EPD; Q9DB30; -.
DR MaxQB; Q9DB30; -.
DR PaxDb; Q9DB30; -.
DR PeptideAtlas; Q9DB30; -.
DR PRIDE; Q9DB30; -.
DR ProteomicsDB; 287709; -.
DR Antibodypedia; 13792; 387 antibodies from 30 providers.
DR DNASU; 68961; -.
DR Ensembl; ENSMUST00000033086; ENSMUSP00000033086; ENSMUSG00000030815.
DR Ensembl; ENSMUST00000121004; ENSMUSP00000113533; ENSMUSG00000030815.
DR GeneID; 68961; -.
DR KEGG; mmu:68961; -.
DR UCSC; uc009jwc.2; mouse.
DR CTD; 5261; -.
DR MGI; MGI:1916211; Phkg2.
DR VEuPathDB; HostDB:ENSMUSG00000030815; -.
DR eggNOG; KOG0599; Eukaryota.
DR GeneTree; ENSGT00940000160435; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9DB30; -.
DR OMA; QFRSPEW; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q9DB30; -.
DR TreeFam; TF320349; -.
DR BRENDA; 2.7.11.19; 3474.
DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR BioGRID-ORCS; 68961; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9DB30; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DB30; protein.
DR Bgee; ENSMUSG00000030815; Expressed in seminiferous tubule of testis and 252 other tissues.
DR ExpressionAtlas; Q9DB30; baseline and differential.
DR Genevisible; Q9DB30; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004689; F:phosphorylase kinase activity; IMP:MGI.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; IMP: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 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_0000086513"
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"
FT CONFLICT 260
FT /note="R -> C (in Ref. 1; BAB23926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 46572 MW; 2B12C7F0F8FE054C CRC64;
MTLDVGPEDE LPDWAAAKEF YQKYDPKDII GRGVSSVVRR CVHRATGDEF AVKIMEVSAE
RLSLEQLEEV RDATRREMHI LRQVAGHPHI ITLIDSYESS SFMFLVFDLM RKGELFDYLT
EKVALSEKET RSIMRSLLEA VSFLHANNIV HRDLKPENIL LDDNMQIRLS DFGFSCHLEA
GEKLRELCGT PGYLAPEILK CSMDETHPGY GKEVDLWACG VILFTLLAGS PPFWHRRQIL
MLRMIMEGQY QFTSPEWDDR SNTVKDLISK LLQVDPEARL TAEQALQHPF FERCEGSQPW
NLTPRQRFRV AVWTILAAGR VALSSHRLRP LTKNALLRDP YALRPVRRLI DNCAFRLYGH
WVKKGEQQNR AALFQHQPPR LFPIAATELE GDSGAITEDE ATLVRS
