ID KPB1_MOUSE Reviewed; 1241 AA.
AC P18826; A2AI90;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 27-MAR-2024, entry version 191.
DE RecName: Full=Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform;
DE Short=Phosphorylase kinase alpha M subunit;
GN Name=Phka1;
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 [MRNA] (ISOFORMS 1 AND 2), AND INVOLVEMENT IN
RP PHOSPHORYLASE KINASE DEFICIENCY.
RC STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RX PubMed=8298647; DOI=10.1038/ng1293-381;
RA Schneider A., Davidson J.J., Wuellrich A., Kilimann M.W.;
RT "Phosphorylase kinase deficiency in I-strain mice is associated with a
RT frameshift mutation in the alpha subunit muscle isoform.";
RL Nat. Genet. 5:381-385(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 243-579.
RX PubMed=2602386; DOI=10.1073/pnas.86.24.9996;
RA Bender P.K., Lalley P.A.;
RT "I/Lyn mouse phosphorylase kinase deficiency: mutation disrupts expression
RT of the alpha/alpha'-subunit mRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9996-10000(1989).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759; SER-973 AND SER-986, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
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.
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.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ABC;
CC IsoId=P18826-1; Sequence=Displayed;
CC Name=2; Synonyms=AC;
CC IsoId=P18826-2; Sequence=VSP_004698;
CC -!- TISSUE SPECIFICITY: Both isoforms are expressed in muscle.
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 -!- DISEASE: Note=Defects in Phka1 are the cause of phosphorylase kinase
CC deficiency in I-strain mice. {ECO:0000269|PubMed:8298647}.
CC -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; X74616; CAA52687.1; -; mRNA.
DR EMBL; X73877; CAA52085.1; -; Transcribed_RNA.
DR EMBL; AL732405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL805925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M28867; AAA39927.1; -; mRNA.
DR CCDS; CCDS30323.1; -. [P18826-1]
DR PIR; S40528; S40528.
DR RefSeq; NP_032858.2; NM_008832.2. [P18826-1]
DR AlphaFoldDB; P18826; -.
DR SMR; P18826; -.
DR BioGRID; 202145; 1.
DR IntAct; P18826; 2.
DR MINT; P18826; -.
DR STRING; 10090.ENSMUSP00000061991; -.
DR iPTMnet; P18826; -.
DR PhosphoSitePlus; P18826; -.
DR SwissPalm; P18826; -.
DR jPOST; P18826; -.
DR MaxQB; P18826; -.
DR PaxDb; 10090-ENSMUSP00000061991; -.
DR ProteomicsDB; 263643; -. [P18826-1]
DR ProteomicsDB; 263644; -. [P18826-2]
DR Pumba; P18826; -.
DR Antibodypedia; 339; 120 antibodies from 27 providers.
DR DNASU; 18679; -.
DR Ensembl; ENSMUST00000052012.14; ENSMUSP00000061991.8; ENSMUSG00000034055.17. [P18826-1]
DR Ensembl; ENSMUST00000113611.3; ENSMUSP00000109241.3; ENSMUSG00000034055.17. [P18826-2]
DR GeneID; 18679; -.
DR KEGG; mmu:18679; -.
DR UCSC; uc009tyr.1; mouse. [P18826-1]
DR AGR; MGI:97576; -.
DR CTD; 5255; -.
DR MGI; MGI:97576; Phka1.
DR VEuPathDB; HostDB:ENSMUSG00000034055; -.
DR eggNOG; KOG3635; Eukaryota.
DR GeneTree; ENSGT00950000183118; -.
DR InParanoid; P18826; -.
DR OMA; CFLMLDA; -.
DR OrthoDB; 3640971at2759; -.
DR PhylomeDB; P18826; -.
DR TreeFam; TF313970; -.
DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR UniPathway; UPA00163; -.
DR BioGRID-ORCS; 18679; 2 hits in 81 CRISPR screens.
DR PRO; PR:P18826; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P18826; Protein.
DR Bgee; ENSMUSG00000034055; Expressed in triceps brachii and 235 other cell types or tissues.
DR ExpressionAtlas; P18826; baseline and differential.
DR Genevisible; P18826; MM.
DR GO; GO:0005964; C:phosphorylase kinase complex; ISO:MGI.
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; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10749:SF4; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT ALPHA, SKELETAL MUSCLE ISOFORM; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR Pfam; PF19292; KPBB_C; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Carbohydrate metabolism;
KW Cell membrane; Glycogen metabolism; Lipoprotein; Membrane; Muscle protein;
KW Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..1241
FT /note="Phosphorylase b kinase regulatory subunit alpha,
FT skeletal muscle isoform"
FT /id="PRO_0000057727"
FT REGION 811..841
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 1064..1104
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64649"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46020"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46020"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64649"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64649"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46020"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1008
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1019
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1024
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64649"
FT LIPID 1238
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT VAR_SEQ 1026..1042
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8298647"
FT /id="VSP_004698"
FT CONFLICT 109
FT /note="K -> P (in Ref. 1; CAA52687)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="N -> Q (in Ref. 1; CAA52687 and 3; AAA39927)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="E -> N (in Ref. 1; CAA52687 and 3; AAA39927)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="L -> I (in Ref. 1; CAA52687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1241 AA; 138825 MW; 954FFF4155CF1F3A CRC64;
MRSRSNSGVR LDGYARLVHQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA
YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE SFKYSQSTKD SLHAKYNTKT
CATVVGDDQW GHLQLDATSV YLLFLAQMTA SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD
FGIWERGDKT NQGISELNAS SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS
ILNSLLPRAS TSKEVDASLL SVVSFPAFAV EDSHLVELTK QEIITKLQGR YGCCRFLRDG
YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGI FSGNVEQVQE YREALDAVLI
KGKNGVPLLP ELYSVPPDRV DEEYQNPHTV DRVPMGKLPH MWGQSLYILG SLMAEGFLAP
GEIDPLNRRF STVPKPDVVV QVSILAETEE IKAILKDKGI DVETIAEVYP IRVQPARILS
HIYSSLGCNS RMKLSGRPYR LMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNQMIV
EMLRTDLSYL CSRWRMTGQP TITFPISHTM LDEDGTSLNS SILAALRKMQ DGYFGGARIQ
TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDEDYEDDL DSGNWMDSYD STSNARCGDE
VARYLDRLLA HTVPHPKLAP TSRKGGLDRF RAAVQTTCDL MSLVAKAKEL HIQNVHMYLP
TKLFQPSRPS LNLLDSPESP QDSQVPSVHV EVHLPRDQSG EVDFQSLVSQ LKETSSLQEQ
ADILYMLYSM KGPDWNTELY EEGGATVREL LSELYVKVGE IRHWGLIRYI SGILRKKVEA
LDEACTDLLS YQKHLTVGLP PEPREKTISA PLPYEALTKL IDEASEGDMS ISTLTQEIMV
YLAMYMRTQP GLFAEMFRLR IGLIIQVMAT ELAHSLRCSA EEATEGLMNL SPSAMKNLLH
HILSGKEFGV ERSVRPTDSN VSPAISIHEI GAVGATKTER TGIMQLKSEI KQVEFRRLSV
SMESQTSGGH PSGVDLMSPS FLSPAACIAA SSGSFPTVCD HQTSKDSRQG QWQRRRRLDG
ALNRVPIGFY QKVWKILQKC HGLSVEGFVL PSSTTREMTP GEIKFSVHVE SVLNRVPQPE
YRQLLVEAIL VLTMLADIEI HSIGSIIAVE KIVHIANDLF LQEQKTLGAD DTMLAKDPAS
GICTLLYDSA PSGRFGTMTY LSKAAATYVQ EFLPHSLCAM Q
//
