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KPB2_MOUSE
ID   KPB2_MOUSE              Reviewed;        1235 AA.
AC   Q8BWJ3; Q3TN65; Q810J6;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Phosphorylase b kinase regulatory subunit alpha, liver isoform;
DE            Short=Phosphorylase kinase alpha L subunit;
GN   Name=Phka2;
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=Heart, and Kidney;
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 MRNA].
RC   TISSUE=Pancreas;
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).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-1015, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-1015, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC       serine in certain substrates, including troponin I. The alpha chain may
CC       bind calmodulin.
CC   -!- ACTIVITY REGULATION: By phosphorylation of various serine residues and
CC       by calcium. {ECO:0000250}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- PTM: Although the final Cys may be farnesylated, the terminal
CC       tripeptide is probably not removed, and the C-terminus is not
CC       methylated. {ECO:0000250|UniProtKB:P18688}.
CC   -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH50040.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK052346; BAC34948.1; -; mRNA.
DR   EMBL; AK165506; BAE38224.1; -; mRNA.
DR   EMBL; BC050040; AAH50040.1; ALT_INIT; mRNA.
DR   CCDS; CCDS30504.1; -.
DR   RefSeq; NP_001171350.1; NM_001177879.1.
DR   RefSeq; NP_766371.1; NM_172783.3.
DR   RefSeq; XP_006528742.1; XM_006528679.3.
DR   AlphaFoldDB; Q8BWJ3; -.
DR   BioGRID; 225291; 2.
DR   STRING; 10090.ENSMUSP00000033652; -.
DR   iPTMnet; Q8BWJ3; -.
DR   PhosphoSitePlus; Q8BWJ3; -.
DR   EPD; Q8BWJ3; -.
DR   jPOST; Q8BWJ3; -.
DR   MaxQB; Q8BWJ3; -.
DR   PaxDb; Q8BWJ3; -.
DR   PRIDE; Q8BWJ3; -.
DR   ProteomicsDB; 265017; -.
DR   Antibodypedia; 24169; 97 antibodies from 25 providers.
DR   DNASU; 110094; -.
DR   Ensembl; ENSMUST00000033652; ENSMUSP00000033652; ENSMUSG00000031295.
DR   Ensembl; ENSMUST00000112377; ENSMUSP00000107996; ENSMUSG00000031295.
DR   GeneID; 110094; -.
DR   KEGG; mmu:110094; -.
DR   UCSC; uc009utk.1; mouse.
DR   CTD; 5256; -.
DR   MGI; MGI:97577; Phka2.
DR   VEuPathDB; HostDB:ENSMUSG00000031295; -.
DR   eggNOG; KOG3635; Eukaryota.
DR   GeneTree; ENSGT00950000183118; -.
DR   HOGENOM; CLU_004177_1_0_1; -.
DR   InParanoid; Q8BWJ3; -.
DR   OMA; QFEHIEC; -.
DR   OrthoDB; 55049at2759; -.
DR   PhylomeDB; Q8BWJ3; -.
DR   TreeFam; TF313970; -.
DR   Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR   UniPathway; UPA00163; -.
DR   BioGRID-ORCS; 110094; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Phka2; mouse.
DR   PRO; PR:Q8BWJ3; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q8BWJ3; protein.
DR   Bgee; ENSMUSG00000031295; Expressed in brown adipose tissue and 251 other tissues.
DR   ExpressionAtlas; Q8BWJ3; baseline and differential.
DR   Genevisible; Q8BWJ3; MM.
DR   GO; GO:0005964; C:phosphorylase kinase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR045583; KPBA/B_C.
DR   InterPro; IPR008734; PHK_A/B_su.
DR   PANTHER; PTHR10749; PTHR10749; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   Pfam; PF19292; KPBB_C; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Carbohydrate metabolism; Cell membrane;
KW   Glycogen metabolism; Lipoprotein; Membrane; Phosphoprotein; Prenylation;
KW   Reference proteome.
FT   CHAIN           1..1235
FT                   /note="Phosphorylase b kinase regulatory subunit alpha,
FT                   liver isoform"
FT                   /id="PRO_0000057731"
FT   REGION          636..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..837
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          1033..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1059..1099
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         695
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46019"
FT   MOD_RES         729
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46019"
FT   MOD_RES         983
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46019"
FT   MOD_RES         1015
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1044
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46019"
FT   LIPID           1232
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P18688"
SQ   SEQUENCE   1235 AA;  138492 MW;  81B6EC538B0228CC CRC64;
     MRSRSNSGVR LDGYARLVQQ TILCYQNPVT GLLSASHDQK DAWVRDNIYS ILAVWGLGMA
     YRKNADRDED KAKAYELEQN VVKLMRGLLQ CMMRQVDKVE KFKHTQSTKD SLHAKYNTAT
     CSTVVGDDQW GHLQVDATSL FLLFLAQMTA SGLRIIFTLD EVAFIQNLVF YIEAAYKVAD
     YGMWERGDKT NQGIPELNAS SVGVAKAALE AIDELDLFGA HGGRKSVIHV LPDEVEHCQS
     ILFSMLPRAS TSKEIDAGLL SIISFPAFAV EDVNLVNVTK NEIISKLQGR YGCCRFLRDG
     YKTPREDPHR LHYDPAELKL FENIECEWPV FWTYLIIDGI FNGDAVQVQE YREALEGILI
     RGKDGIHLVP ELYAIPPDKV DEEYKNPHTV DRVPLGKLPH LWGQSLYILS SLLAEGFLAT
     GEIDPLNRRF STSVKPDVVV QVAVLAENSH IKGLLKEHGM TVQSIADVHP IRVQPGRILS
     HIYAKLGRNK NMKLSGRPYR HIGVLGTSKL YVIRNHIFTF TPQFTDQHHF YLALDNEMIV
     EMLRIELAYL CTCWRMTGRP TLTFPVTHTM LTNDGSDIHP AVLSTIRKLE DGYFGGARVK
     LGNLAEFLTT SFYTHLTFLD PDCDEKLFGD ITDRSFSPDS EPDLGGYLED SSPQESQDEL
     DQYISHLLQS TSLKCYLPPL CKKSEDSHFF SAIHSTRDIL SVMAKAKGLE TTFFPMILPT
     KVLSGHRKSL NLVDSPQPLL KTTPEYDYQW PRDDHDEVDC EKLVGQLKDC SNLQDQADIL
     YILYVMKGPR WDTNLFGQHG VTVHSLLSEL YGKAGLNQEW SLIRYISGLL RKKVEVLAEA
     CADLLSHQKQ LTVGLPPEPR EKTISTPLPP EELTELIYEA SGQDISIAVL TQEIVVYLAM
     YVRAQPSLFA EMLRLRIGLI IQVMATELAR SLNCSGKEAS ESLMNLSPFD MKSLLHHILS
     GKEFGVERSV RPIHSSMSSP AISIHEVGHT GATKTERSGI TRLRSEMKQM NRRASADEQF
     FPLGQTMSNS LHSIKSVRSS TPSSPTGTSS TDSGGQHLGW GEQQGQWLRR RRLDGAINRV
     PVGFYQKVWK ILQKCHGLSI DGYVLPSSTT QEMTPCEIKF AVHVESVLNR VSQPEYRQLL
     VEAIMVLTLL SDTEMDSIGG IIHVDQIVQL ANQLFLQDQV SFGTTDILEK DQATGICHLF
     YDSAPSGAYG TMTYLTKAVA SHLQELLPSS GCQMQ
 
 
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