(data stored in ACNUC31886 zone)

HOGENOM: RABITX_5_PE6

ID   RABITX_5_PE6                         STANDARD;      PRT;   1236 AA.
AC   RABITX_5_PE6; P46018;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Phosphorylase b kinase regulatory subunit alpha, liver
DE   isoform; Short=Phosphorylase kinase alpha L subunit; (RABITX_5.PE6).
GN   Name=PHKA2;
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABITX_5.PE6.
CC       Oryctolagus cuniculus chromosome X oryCun2 partial sequence
CC       3829307..4829306 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:KPB2_RABIT
CC   -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC       serine in certain substrates, including troponin I. The alpha
CC       chain may bind calmodulin.
CC   -!- ENZYME REGULATION: By phosphorylation of various serine residues
CC       and by calcium.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC   -!- SUBUNIT: Polymer of 16 chains, four each of alpha, beta, gamma,
CC       and delta. Alpha and beta are regulatory chains, gamma is the
CC       catalytic chain, and delta is calmodulin.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in liver and other
CC       non-muscle tissues.
CC   -!- PTM: Although the final Cys is probably farnesylated, the terminal
CC       tripeptide is probably not removed, and the C-terminus is not
CC       methylated (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC       family.
CC   -!- GENE_FAMILY: HOG000231478 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Oryctolagus_cuniculus;ENSOCUG00000013782;ENSOCUT00000031800;ENSOCUP00000022300.
DR   EMBL; X60421; - ;
DR   UniProtKB/Swiss-Prot; P46018; -.
DR   EMBL; X60421; CAA42952.1; -; mRNA.
DR   PIR; S24109; S24109.
DR   RefSeq; NP_001129153.1; NM_001135681.1.
DR   UniGene; Ocu.2085; -.
DR   ProteinModelPortal; P46018; -.
DR   STRING; P46018; -.
DR   Ensembl; ENSOCUT00000031800; ENSOCUP00000022300; ENSOCUG00000013782.
DR   GeneID; 100190898; -.
DR   CTD; 5256; -.
DR   GeneTree; ENSGT00520000055553; -.
DR   OrthoDB; EOG4ZPDTH; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:InterPro.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR012341; 6hp_glycosidase.
DR   InterPro; IPR011613; Glyco_hydro_15-rel.
DR   InterPro; IPR008734; PHK_AB.
DR   Gene3D; G3DSA:1.50.10.10; CelA/Cel48F_cat; 1.
DR   PANTHER; PTHR10749; PHK_AB; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   SUPFAM; SSF48208; Glyco_trans_6hp; 1.
DR   HOGENOMDNA; RABITX_5.PE6; -.
KW   ENSOCUG00000013782820036002503210000011;
KW   KPB2_RABIT; X60421;
KW   Calmodulin-binding; Carbohydrate metabolism; Cell membrane;
KW   Glycogen metabolism; Lipoprotein; Membrane; Phosphoprotein;
KW   Prenylation.
SQ   SEQUENCE   1236 AA;  UNKNOWN MW;  UNKNOWN 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 LLKKDPEGDC HWPKDERGDV DCEKLVEQLK DCCTLQDQAD
     ILYILYVLKG PSWDTALSGQ HGVTVHNLLS ELYGKAGLNQ EWGLIRYISG LLRKKVEVLA
     EACADLLSHQ KQLTVGLPPE PREKTISAPL PPEELTQLIY EASGEDISIA VLTQEIVVYL
     AMYVRAQPSL FVEMLRLRIG LIIQVMATEL ARSLNCSGEE ASESLMNLSP FDMKNLLHHI
     LSGKEFGVER SMRPIHSSAS SPAISIHEVG HTGVTKTERS GINRLRSEMK QMTRRFSADE
     QFFPVSQTVS SSAYSKSVRS STPSSPTGTS SSDSGGHHIS WGERQGQWLR RRRLDGAINR
     VPVGFYQRVW KILQKCHGLS IDGYVLPSST TREMTPQEIK FAVHVESVLN RVSQPEYRQL
     LVEAIMVLTL LSDTEMESIG GIIHVDQIVQ MANQLFLQEQ ISTGAMDTLE KDQATGICHF
     FYDSAPSGAY GTMTYLTRAV ASHLQELLPS SGCQTQ
//

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