ID KPBB_RABIT Reviewed; 1093 AA.
AC P12798;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 148.
DE RecName: Full=Phosphorylase b kinase regulatory subunit beta;
DE Short=Phosphorylase kinase subunit beta;
GN Name=PHKB;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT ALA-2, AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Skeletal muscle;
RX PubMed=3200826; DOI=10.1073/pnas.85.24.9381;
RA Kilimann M.W., Zander N.F., Kuhn C.C., Crabb J.W., Meyer H.E.,
RA Heilmeyer L.M.G. Jr.;
RT "The alpha and beta subunits of phosphorylase kinase are homologous: cDNA
RT cloning and primary structure of the beta subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:9381-9385(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=1874721; DOI=10.1016/s0021-9258(18)98453-x;
RA Harmann B., Zander N.F., Kilimann M.W.;
RT "Isoform diversity of phosphorylase kinase alpha and beta subunits
RT generated by alternative RNA splicing.";
RL J. Biol. Chem. 266:15631-15637(1991).
RN [3]
RP PROTEIN SEQUENCE OF 2-18; 25-33; 688-709 AND 1072-1093, AND PHOSPHORYLATION
RP AT SER-12; SER-27 AND SER-701.
RX PubMed=2108025; DOI=10.1111/j.1432-1033.1990.tb15413.x;
RA Meyer H.E., Meyer G.F., Dirks H., Heilmeyer L.M.G. Jr.;
RT "Localization of phosphoserine residues in the alpha subunit of rabbit
RT skeletal muscle phosphorylase kinase.";
RL Eur. J. Biochem. 188:367-376(1990).
RN [4]
RP PROTEIN SEQUENCE OF 34-1081.
RX PubMed=2338067; DOI=10.1002/elps.1150110206;
RA Crabb J.W., Harris W.R., Johnson C.M., Sotiroudis T.G., Kuhn C.C.,
RA Heilmeyer L.M. Jr.;
RT "Electrophoretic purification of the alpha and beta subunits of
RT phosphorylase kinase and evidence in support of the deduced amino acid
RT sequences.";
RL Electrophoresis 11:133-140(1990).
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Skeletal muscle;
RX PubMed=164350; DOI=10.1111/j.1432-1033.1975.tb03909.x;
RA Cohen P., Watson D.C., Dixon G.H.;
RT "The hormonal control of activity of skeletal muscle phosphorylase kinase.
RT Amino-acid sequences at the two sites of action of adenosine-3':5'-
RT monophosphate-dependent protein kinase.";
RL Eur. J. Biochem. 51:79-92(1975).
RN [6]
RP PROTEIN SEQUENCE OF 1073-1093, ISOPRENYLATION AT CYS-1090, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=1409665; DOI=10.1073/pnas.89.20.9554;
RA Heilmeyer L.M. Jr., Serwe M., Weber C., Metzger J., Hoffmann-Posorske E.,
RA Meyer H.E.;
RT "Farnesylcysteine, a constituent of the alpha and beta subunits of rabbit
RT skeletal muscle phosphorylase kinase: localization by conversion to S-
RT ethylcysteine and by tandem mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9554-9558(1992).
CC -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC serine in certain substrates, including troponin I. The beta chain acts
CC as a regulatory unit and modulates the activity of the holoenzyme in
CC response to phosphorylation.
CC -!- ACTIVITY REGULATION: By phosphorylation of various serine residues.
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=4;
CC Name=1;
CC IsoId=P12798-1; Sequence=Displayed;
CC Name=2; Synonyms=Brain;
CC IsoId=P12798-2; Sequence=VSP_004702;
CC Name=3;
CC IsoId=P12798-3; Sequence=VSP_004703;
CC Name=4;
CC IsoId=P12798-4; Sequence=VSP_004702, VSP_004703;
CC -!- PTM: Cys-1090 is farnesylated, but the C-terminal tripeptide is not
CC removed and the cysteine carboxyl is not methylated.
CC {ECO:0000269|PubMed:1409665}.
CC -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J04120; AAA31447.1; -; mRNA.
DR EMBL; M64657; AAA31450.1; -; mRNA.
DR EMBL; M64658; AAA31448.1; -; mRNA.
DR PIR; A31758; A31758.
DR PIR; B40793; B40793.
DR RefSeq; NP_001075770.1; NM_001082301.1. [P12798-4]
DR RefSeq; XP_008246591.1; XM_008248369.2. [P12798-1]
DR RefSeq; XP_008246593.1; XM_008248371.2. [P12798-3]
DR AlphaFoldDB; P12798; -.
DR DIP; DIP-48333N; -.
DR IntAct; P12798; 2.
DR MINT; P12798; -.
DR STRING; 9986.ENSOCUP00000037032; -.
DR iPTMnet; P12798; -.
DR PaxDb; 9986-ENSOCUP00000025922; -.
DR GeneID; 100009137; -.
DR KEGG; ocu:100009137; -.
DR CTD; 5257; -.
DR eggNOG; KOG3635; Eukaryota.
DR InParanoid; P12798; -.
DR OrthoDB; 3640971at2759; -.
DR BRENDA; 2.7.11.19; 1749.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000001811; Unplaced.
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 InterPro; IPR008928; 6-hairpin_glycosidase_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:SF8; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT BETA; 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 Acetylation; Alternative splicing; Calmodulin-binding;
KW Carbohydrate metabolism; Cell membrane; Direct protein sequencing;
KW Glycogen metabolism; Lipoprotein; Membrane; Phosphoprotein; Prenylation;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2108025"
FT CHAIN 2..1093
FT /note="Phosphorylase b kinase regulatory subunit beta"
FT /id="PRO_0000057738"
FT REGION 7..29
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 688..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..795
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 920..951
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 697..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1090
FT /note="Not methylated"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:3200826"
FT MOD_RES 12
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:2108025,
FT ECO:0000269|PubMed:3200826"
FT MOD_RES 27
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:2108025,
FT ECO:0000269|PubMed:3200826"
FT MOD_RES 701
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:2108025,
FT ECO:0000269|PubMed:3200826"
FT LIPID 1090
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:1409665"
FT VAR_SEQ 1..23
FT /note="MAGATGLMAEVSWKVLERRARTK -> MASSADAVVSSPPAFL (in
FT isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_004702"
FT VAR_SEQ 780..806
FT /note="LAVRYGAAFTQKFSSSIAPHITTFLVH -> SVVRRAASLLNKVVDSLAPSI
FT TNVLVQ (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_004703"
FT VARIANT 28
FT /note="V -> I"
FT CONFLICT 24
FT /note="R -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1093 AA; 125295 MW; 5954A72A50CD6F3C CRC64;
MAGATGLMAE VSWKVLERRA RTKRSGSVYE PLKSINLPRP DNETLWDKLD YYYKIVKSTL
LLYQSPTTGL FPTKTCGGDQ TAKIHDSLYC AAGAWALALA YRRIDDDKGR THELEHSAIK
CMRGILYCYM RQADKVQQFK QDPRPTTCLH SLFNVHTGDE LLSYEEYGHL QINAVSLYLL
YLVEMISSGL QIIYNTDEVS FIQNLVFCVE RVYRVPDFGV WERGSKYNNG STELHSSSVG
LAKAALEAIN GFNLFGNQGC SWSVIFVDLD AHNRNRQTLC SLLPRESRSH NTDAALLPCI
SYPAFALDDD VLYNQTLDKV IRKLKGKYGF KRFLRDGYRT SLEDPKRRYY KPAEIKLFDG
IECEFPIFFL YMMIDGVFRG NPKQVKEYQD LLTPVLHQTT EGYPVVPKYY YVPADFVEYE
KRNPGSQKRF PSNCGRDGKL FLWGQALYII AKLLADELIS PKDIDPVQRY VPLQNQRNVS
MRYSNQGPLE NDLVVHVALV AESQRLQVFL NTYGIQTQTP QQVEPIQIWP QQELVKAYFH
LGINEKLGLS GRPDRPIGCL GTSKIYRILG KTVVCYPIIF DLSDFYMSQD VLLLIDDIKN
ALQFIKQYWK MHGRPLFLVL IREDNIRGSR FNPMLDMLAA LKNGMIGGVK VHVDRLQTLI
SGAVVEQLDF LRISDTEELP EFKSFEELEP PKHSKVKRQS STSNAPELEQ QPEVSVTEWR
NKPTHEILQK LNDCSCLASQ TILLGILLKR EGPNFITQEG TVSDHIERLY RRAGSKKLWL
AVRYGAAFTQ KFSSSIAPHI TTFLVHGKQV TLGAFGHEEE VISNPLSPRV IKNIIYYKCN
THDEREAVIQ QELVIHIGWI ISNNPELFSG MLKIRIGWII HAMEYELQIR SGDKPAKDLY
QLSPSEVKQL LLDILQPQQN GRCWLNKRQI DGSLNRTPTG FYDRVWQILE RTPNGIIVAG
KHLPQQPTLS DMTMYEMNFS LLVEDMLGNI DQPKYRQIVV ELLMVVSIVL ERNPELEFQD
KVDLDKLVKE AFHEFQKDES RLKEIEKQDD MTSFYNTPPL GKRGTCSYLT KVVMNLLLEG
EVKPSNEDSC LVS
//
