KPB1_RAT
ID KPB1_RAT Reviewed; 1242 AA.
AC Q64649; Q64650; Q64651; Q9QZ77;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform;
DE Short=Phosphorylase kinase alpha M subunit;
GN Name=Phka1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Brushia R.J., Hoye E.R., Walsh D.A.;
RT "Fundamental physicochemical characterization of the phosphorylase b kinase
RT holoenzyme and alpha-gamma-delta and gamma-delta subunit subcomplexes
RT reconstituted in baculovirus-infected insect cells.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-267; 547-658 AND 908-1136.
RC TISSUE=Skeletal muscle;
RX PubMed=1512265; DOI=10.1016/s0021-9258(18)41924-2;
RA Cawley K.C., Akita C.G., Wineinger M.A., Carlsen R.C., Gorin F.A.,
RA Walsh D.A.;
RT "Coordinated expression of phosphorylase kinase subunits in regenerating
RT skeletal muscle.";
RL J. Biol. Chem. 267:17287-17295(1992).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630; SER-737; SER-740;
RP SER-760; SER-813; SER-974; SER-987 AND SER-1132, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- 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}.
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DR EMBL; AF197561; AAF06673.1; -; mRNA.
DR EMBL; M92917; AAA41858.1; -; mRNA.
DR EMBL; M92918; AAA41859.1; -; mRNA.
DR EMBL; M92919; AAA41860.1; -; mRNA.
DR PIR; B43431; B43431.
DR PIR; C43431; C43431.
DR AlphaFoldDB; Q64649; -.
DR STRING; 10116.ENSRNOP00000068112; -.
DR iPTMnet; Q64649; -.
DR PhosphoSitePlus; Q64649; -.
DR jPOST; Q64649; -.
DR PaxDb; Q64649; -.
DR PRIDE; Q64649; -.
DR UCSC; RGD:621522; rat.
DR RGD; 621522; Phka1.
DR eggNOG; KOG3635; Eukaryota.
DR InParanoid; Q64649; -.
DR PhylomeDB; Q64649; -.
DR BRENDA; 2.7.11.19; 5301.
DR Reactome; R-RNO-70221; Glycogen breakdown (glycogenolysis).
DR UniPathway; UPA00163; -.
DR PRO; PR:Q64649; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005964; C:phosphorylase kinase complex; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; TAS:RGD.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
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; Muscle protein; Phosphoprotein;
KW Prenylation; Reference proteome.
FT CHAIN 1..1242
FT /note="Phosphorylase b kinase regulatory subunit alpha,
FT skeletal muscle isoform"
FT /id="PRO_0000057728"
FT REGION 812..842
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 1065..1105
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46020"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46020"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1009
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1020
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 1239
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P18688"
FT CONFLICT 245
FT /note="T -> S (in Ref. 2; AAA41858)"
FT /evidence="ECO:0000305"
FT CONFLICT 264..265
FT /note="IS -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 926
FT /note="I -> L (in Ref. 2; AAA41860)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="R -> K (in Ref. 2; AAA41860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1242 AA; 139155 MW; 15E61F40D4D2E82C CRC64;
MRSRSNSGVR LDSYARLVQQ HTILCHQNPV TGLLPASYDQ KDAWVRDNVY SILAVWGLGL
AYRKNADRDE DKAKAYELEQ SVVKLMRGLL HCMIRQVDKV ESFKYSQSTK DSLHAKYNTK
TCATVVGDDQ WGHLQLDATS VYLLFLAQMT ASGLHIIHSL DEVNFIQNLV FYIEAAYKTA
DFGIWERGDK TNQGISELNA CSVGMAKAAL EALDELDLFG VKGGPQSVIH VLADEVQHCQ
SILNTLLPRA STSKEVDASL LSVISFPAFA VEDSKLVEIT KQEIITKLQG RYGCCRFLRD
GYKTPKEDPN RLYYEPAELK LFENIECEWP LFWTYFILDG IFSGNTEQVQ EYREALDAVL
IKGKNGVPLL PELYSVPPDR VDEEYQNPHT VDRVPMGKLP HMWGQSLYIL GNLMAEGFLA
PGEIDPLNRR FSTVPKPDVV VQVSILAETE EIKAILKDKG IDVETIAEVY PIRVQPARIL
SHIYSSLGCN SRMKLSGRPY RLMGVLGTSK LYDIRKTIYT FTPQFIDQQQ FYLALDNQMI
VEMLRTDLSY LCSRWRMTGQ PTITFPISHT MLDEDGASLN SSILAALRKM QDGYFGGARI
QTGKLSEFLT TSCCTHLSFM DPGPEGKLYS EDYDEDYDDE LDSGNWMDSY DSTRNARCGD
EVARYLDHLL AHTGPHPKLT PTSRKGGLDR FRAAVQTTCD LMSLVAKAKE LHIQNVHMYL
PTKLFQPSRP SLNLLDSPES PQDSQVPSVR VEVHLPRDQS GEVDFQSLVS QLKETSSLQE
QADILYMLYT MKGPDWNTEL YEEGGSTVRE LLSELYVKVG EIRHWGLIRY ISGILRKKVE
ALDEACTDLL SYQKHLTVGL PPEPREKTIS APLPYEALTK LIDEASEGDM NISTLTQEIM
VYLAMYMRTQ PGLFAEMFRL RIGLIIQVMA TELAHSLRCS AEEATEGLMN LSPSAMRNLL
HHILSGKEFG VERSVRPTDS NVSPAISIHE IGAVGATKTE RTGIMQLKSE IKQVEFRRLS
VSPESQTSGG HPSSIDLMSP TFLSPAACIS ASSGSFPTVC EPQTSKDSRQ GQWQRRRRLD
GALNRVPIGF YQKVWKILQK CHGLSVEGFV LPSSSTREMT PGEIKFSVHV ESVLNRVPQP
EYRQLLVEAI LVLTMLADIE IHSIGSIIAV EKIVHIANDL FLQEKKTLGA DDIMLAKDPA
SGICTLLYDS APSGRFGTMT YLSKAAATYV QEFLPHSLCA VQ
