KPB2_RABIT
ID KPB2_RABIT Reviewed; 1235 AA.
AC P46018;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Phosphorylase b kinase regulatory subunit alpha, liver isoform;
DE Short=Phosphorylase kinase alpha L subunit;
GN Name=PHKA2;
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].
RC TISSUE=Liver;
RX PubMed=1372435; DOI=10.1073/pnas.89.6.2096;
RA Davidson J.J., Oezelik T., Hamacher C., Willems P.J., Francke U.,
RA Kilimann M.W.;
RT "cDNA cloning of a liver isoform of the phosphorylase kinase alpha subunit
RT and mapping of the gene to Xp22.2-p22.1, the region of human X-linked liver
RT glycogenosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2096-2100(1992).
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 -!- TISSUE SPECIFICITY: Predominantly expressed in liver and other non-
CC muscle tissues.
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; X60421; CAA42952.1; -; mRNA.
DR PIR; S24109; S24109.
DR RefSeq; NP_001129153.1; NM_001135681.1.
DR AlphaFoldDB; P46018; -.
DR STRING; 9986.ENSOCUP00000022300; -.
DR PRIDE; P46018; -.
DR GeneID; 100190898; -.
DR KEGG; ocu:100190898; -.
DR CTD; 5256; -.
DR eggNOG; KOG3635; Eukaryota.
DR InParanoid; P46018; -.
DR OrthoDB; 55049at2759; -.
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 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 2: Evidence at transcript level;
KW Calmodulin-binding; Carbohydrate metabolism; Cell membrane;
KW Glycogen metabolism; Lipoprotein; Membrane; Phosphoprotein; Prenylation;
KW Reference proteome.
FT CHAIN 1..1235
FT /note="Phosphorylase b kinase regulatory subunit alpha,
FT liver isoform"
FT /id="PRO_0000057732"
FT REGION 808..838
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 976..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1099
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1032..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46019"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46019"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46019"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46019"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46019"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46019"
FT LIPID 1232
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P18688"
SQ SEQUENCE 1235 AA; 138770 MW; B8E218C1D8C6F376 CRC64;
MRSRSNSGVR LDGYARLVQQ TILCYQNPVT GLLSASHEQK DAWVRDNIYS ILAVWGLGMA
YRKNADRDED KAKAYELEQN VVKLMRGLLQ CMMRQVDKVE KFKYTQSTKD SLHAKYNTAT
CSTVVGDDQW GHLQVDATSL FLLFLAQMTA SGLRIIFTLD EVAFIQNLVF YIEAAYKVAD
YGMWERGDKT NQGIPELNAS SVGMAKAALE AIDELDLFGA HGGRKSVIHV LPDEVEHCQS
ILFSMLPRAS TSKEIDAGLL SIISFPAFAV EDANLVNVTK SEIISKLQGR YGCCRFLRDG
YKTPREDPNR LHYDPAELKL FENIECEWPV FWTYFIIDGI FNGDALQVQE YQEALEGILI
RGKDGIRLVP ELYAIPPNKV DEEYKNPHTV DRVPLGKLPH LWGQSLYILS SLLAEGFLAT
GEIDPLNRRF STSVKPDVVV QVTVLAENSH IKELLRKHGV DVQSIADIYP IRVQPGRILS
HIYAKLGRNK NMKLSGRPYR HIGVLGTSKL YVIRNQIFTF TPQFTDQHHF YLALDNEMIV
EMLRIELAYL CTCWRMTGRP TLTFPITHTM LTNDGSDIHS AVLSTIRKLE DGYFGGARVQ
LGNLSEFLTT SFYTYLTFLD PDCDEKLFDD ASEGSFSPDS DSDLGGYLEE TYNQVTESQD
ELDKYINHLL QSTYSKCHLP PLCKKMEDHN VFSAIHSTRD ILSMMAKAKG LEVPFAPMTL
PTKALSVHRK SLNLVDSPQP LLKRILKRLH WPKDERGDVD CEKLVEQLKD CCTLQDQADI
LYILYVLKGP SWDTALSGQH GVTVHNLLSE LYGKAGLNQE WGLIRYISGL LRKKVEVLAE
ACADLLSHQK QLTVGLPPEP REKTISAPLP PEELTELIYE ASGEDISIAV LTQEIVVYLA
MYVRAQPALF VEMLRLRIGL IIQVMATELA RSLNCSGEEA SESLMNLSPF DMKNLLHHIL
SGKEFGVERS MRPIHSSASS PAISIHEVGH TGVTKTERSG INRLRSEMKQ MTRRFSADEQ
FFPVSQTVSS SAYSKSVRSS TPSSPTGTSS SDSGGHHISW GERQGQWLRR RRLDGAINRV
PVGFYQRVWK ILQKCHGLSI DGYVLPSSTT REMTPQEIKF AVHVESVLNR VSQPEYRQLL
VEAIMVLTLL SDTEMESIGG IIHVDQIVQM ANQLFLQEQI STGAMDTLEK DQATGICHFF
YDSAPSGAYG TMTYLTRAVA SHLQELLPSS GCQTQ
