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 24-JAN-2024, entry version 102.
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 SMR; Q9W6R1; -.
DR STRING; 31033.ENSTRUP00000043732; -.
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; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10749:SF5; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT ALPHA, LIVER ISOFORM; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR Pfam; PF19292; KPBB_C; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 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
//
