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   27-MAR-2024, entry version 160.
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.ENSMUSP00000113533; -.
DR   iPTMnet; Q9DB30; -.
DR   PhosphoSitePlus; Q9DB30; -.
DR   EPD; Q9DB30; -.
DR   MaxQB; Q9DB30; -.
DR   PaxDb; 10090-ENSMUSP00000033086; -.
DR   PeptideAtlas; Q9DB30; -.
DR   ProteomicsDB; 287709; -.
DR   Antibodypedia; 13792; 440 antibodies from 30 providers.
DR   DNASU; 68961; -.
DR   Ensembl; ENSMUST00000033086.8; ENSMUSP00000033086.2; ENSMUSG00000030815.12.
DR   Ensembl; ENSMUST00000121004.3; ENSMUSP00000113533.2; ENSMUSG00000030815.12.
DR   GeneID; 68961; -.
DR   KEGG; mmu:68961; -.
DR   UCSC; uc009jwc.2; mouse.
DR   AGR; MGI:1916211; -.
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; 1121238at2759; -.
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 79 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 256 other cell types or tissues.
DR   ExpressionAtlas; Q9DB30; baseline and differential.
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: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:SF390; PHOSPHORYLASE B KINASE GAMMA CATALYTIC CHAIN, LIVER_TESTIS ISOFORM; 1.
DR   PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN 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; Q9DB30; MM.
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
//