ID   KPB2_TAKRU              Reviewed;        1229 AA.
AC   Q9W6R1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Phosphorylase b kinase regulatory subunit alpha, liver isoform;
DE            Short=Phosphorylase kinase alpha L subunit;
GN   Name=phka2;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10330123;
RA   Brunner B., Todt T., Lenzner S., Stout K., Schulz U., Ropers H.-H.,
RA   Kalscheuer V.M.;
RT   "Genomic structure and comparative analysis of nine Fugu genes:
RT   conservation of synteny with human chromosome Xp22.2-p22.1.";
RL   Genome Res. 9:437-448(1999).
CC   -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC       serine in certain substrates, including troponin I. The alpha chain may
CC       bind calmodulin (By similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: By phosphorylation of various serine residues and
CC       by calcium. {ECO:0000250}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC   -!- SUBUNIT: Polymer of 16 chains, four each of alpha, beta, gamma, and
CC       delta. Alpha and beta are regulatory chains, gamma is the catalytic
CC       chain, 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}.
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DR   EMBL; AF146687; AAD28794.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9W6R1; -.
DR   STRING; 31033.ENSTRUP00000043730; -.
DR   eggNOG; KOG3635; Eukaryota.
DR   InParanoid; Q9W6R1; -.
DR   BRENDA; 2.7.11.19; 6209.
DR   UniPathway; UPA00163; -.
DR   Proteomes; UP000005226; 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   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; 2.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   Pfam; PF19292; KPBB_C; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   3: Inferred from homology;
KW   Calmodulin-binding; Carbohydrate metabolism; Cell membrane;
KW   Glycogen metabolism; Lipoprotein; Membrane; Phosphoprotein; Prenylation;
KW   Reference proteome.
FT   CHAIN           1..1229
FT                   /note="Phosphorylase b kinase regulatory subunit alpha,
FT                   liver isoform"
FT                   /id="PRO_0000057733"
FT   REGION          625..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..855
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          1024..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1052..1092
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        625..644
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           1226
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P18688"
SQ   SEQUENCE   1229 AA;  137924 MW;  98316E76C20B3D3F CRC64;
     MRSRSNSGVR LDGYARLVHE TILGFQNPVT GLLPASVQKK DAWVRDNVYS ILAVWGLGMA
     YRKNADRDED KAKAYELEQS VVKLMQGLLH CMMRQVAKVE KFKHTQSTTD CLHAKYDTST
     CATVVGDDQW GHLQVDATSI YLLMLAQMTA SGLRIISNLD EVAFVQNLVF YIEAAYKVAD
     YGMWERGDKT NQGLPELNGS SVGMAKAALE AIDELDLFGA HGGPKSVIHV LPDEVEHCQS
     ILCSMLPRAS PSKEIDAGLL SVISFPAFAV EDADLVTITK SEIINKLQGR YGCCRFIRDG
     YHCPKEDPTR LHYDPAELKL FENIECEWPV FWTYLILDGI FAEDQVQVQE YREALEGVLI
     RGKNGIKLLP ELYTVPFDKV EEEYRNPHSV DREATGQLPH MWEQSLYILG CLLAEGFLAP
     GEIDPLNRRF STSFKPDVVV QVCVLAESQE IKALLSEQGM VVQTVAEVLP IRVMSARVLS
     QIYVRLGNCK KLSLSGRPYR HIGVLGTSKF YEIRNHTYTF TPQFLDQHHF YLALDNQMIV
     EMLRTELAYL SSCWRMTGRP TLTFPVTRSM LVEDGDAVDP CILSTLRKLQ DGYFAGARVQ
     MSDLSTFQTT SFHTRLSFLD EEHDDSLLED DEEQEEEEED KFEDDYNNYG PSGNNQVCYV
     SKDKFDQYLT QLLHSTTQKC HLPPIQRGQH HVFSAEHTTR DILSFMAQVQ GLNVPKSSMY
     LPVTPLKSKH RRSLNLLDVP HPQHGPHLKQ NKVGTFNSVL AADLHLPRDP QGKTDFATLV
     KQLKECPTLQ DQADILYILN TSKGADWLVE LSGPGQGGVS VHTLLEELYI QAGACKEWGL
     IRYISGILRK RVEVLAEACT DLISHHKQLT VGLPPEPRER VITVPLPPEE LNTLIYEASG
     QDISVAVLTQ EIMVYLAMYI RSQPALFGDM LRLRIGLIMQ VMATELARSL HCSGEEASES
     LMSLSPFDMK NLLHHILSGK EFGVERSMRP IQSTATSPAI SIHEIGHTGA TKTERTGIRK
     LKSEIKQRCS SPSTPSGILS PVGPGPADGQ LHWVERQGQW LRRRRLDGAI NRVPVGFYQK
     VWKILQKCHG LSIDGYVLPS STTREMTAGE IKFAVQVESV LNHVPQPEYR QLLVESVMVL
     GLVADVDVES IGSIIYVDRI LHLANDLFLT DQKSYSAGDY FLEKDPETGI CNFFYDSAPS
     GIYGTMTYLS KAAVTYIQDF LPSSSCIMQ