(data stored in ACNUC31886 zone)

HOGENOM: RABITX_53_PE3

ID   RABITX_53_PE3                        STANDARD;      PRT;   1241 AA.
AC   RABITX_53_PE3; P18688;
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, skeletal
DE   muscle isoform; Short=Phosphorylase kinase alpha M subunit;
DE   (RABITX_53.PE3).
GN   Name=PHKA1;
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_53.PE3.
CC       Oryctolagus cuniculus chromosome X oryCun2 partial sequence
CC       51054136..52054135 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:KPB1_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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=ABC, Alpha;
CC         IsoId=P18688-1; Sequence=Displayed;
CC       Name=2; Synonyms=BC;
CC         IsoId=P18688-2; Sequence=VSP_004701;
CC       Name=3; Synonyms=Alpha';
CC         IsoId=P18688-3; Sequence=VSP_004699, VSP_004700;
CC   -!- TISSUE SPECIFICITY: Isoform 1 predominates in muscle, heart, brain
CC       and testis. Isoforms 1 and 2 are expressed in similar quantities
CC       in the other tissues. Isoform 3 is highly expressed in slow muscle
CC       and heart.
CC   -!- PTM: Phosphorylation of Ser-1018 by PKA stimulates the
CC       dephosphorylation of the beta subunit and, thus, reverses the
CC       initial stimulation of PHK by the faster beta-subunit
CC       phosphorylation by PKA, that occurs in muscle in response to
CC       adrenaline.
CC   -!- PTM: Cys-1234 is farnesylated, but the C-terminal tripeptide is
CC       not removed and the cysteine carboxyl is not methylated.
CC   -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC       family.
CC   -!- GENE_FAMILY: HOG000231478 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Oryctolagus_cuniculus;ENSOCUG00000024271;ENSOCUT00000021035;ENSOCUP00000024040.
DR   EMBL; J03247; - ;
DR   EMBL; M64656; - ;
DR   UniProtKB/Swiss-Prot; P18688; -.
DR   EMBL; J03247; AAA31446.1; ALT_SEQ; mRNA.
DR   EMBL; M64656; AAC23909.1; -; mRNA.
DR   PIR; A31334; A31334.
DR   RefSeq; NP_001159389.1; NM_001165917.1.
DR   UniGene; Ocu.2209; -.
DR   ProteinModelPortal; P18688; -.
DR   DIP; DIP-44274N; -.
DR   MINT; MINT-5209269; -.
DR   STRING; P18688; -.
DR   Ensembl; ENSOCUT00000021035; ENSOCUP00000024040; ENSOCUG00000024271.
DR   GeneID; 100303771; -.
DR   eggNOG; maNOG06065; -.
DR   GeneTree; ENSGT00520000055553; -.
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_53.PE3; -.
KW   ENSOCUG00000024271820036002503210000011;
KW   KPB1_RABIT; J03247; M64656;
KW   Alternative splicing; Calmodulin-binding; Carbohydrate metabolism;
KW   Cell membrane; Direct protein sequencing; Glycogen metabolism;
KW   Lipoprotein; Membrane; Muscle protein; Phosphoprotein; Prenylation.
SQ   SEQUENCE   1241 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRSRSNSGVR LDSYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA
     YRKNADRDED KAKAYELEQQ SVVKLMRGLL HCMIRQVDKV ESFKYSQSTK DSLHAKYNTK
     TCATVVGDDQ WGHLQLDATS VYLLFLAQMT ASGLHIIHSL DEVNFIQNLV FYIEAAYKTA
     DFGIWERGDK TNQGISELNA SSVGMAKAAL EALDELDLFG VKGGPQSVIH VLADEVQHCQ
     SILNSLLPRA STSKEVDASL LSVISFPAFA VEDSKLVEIT KQEIITKLQH CQGRYGCCRF
     LRDGYKTPKE DPNRLYYEPA ELKLFENIEC EWPLFWTYFI LDGVFSGNAE QVQEYREALE
     AVLIKGKNGV PLLPELYSVP PDKVDEEYQN PHTVDRVPMG KLPHMWGQSL YILGSLMAEG
     FLAPGEIDPL NRRFSTVPKP DVVVQVSILA ETEEIKAILK DKGINVETIA EVYPIRVQPA
     RILSHIYSSL GCNNRMKLSG RPYRHMGVLG TSKLYDIRKT IFTFTPQFID QQQFYLALDN
     KMIVEMLRTD LSYLCSRWRM TGQPTITFPI SQTMLDEDGT SLNSSILAAL RKMQDGYFGG
     ARIQTGKLSE FLTTSCCTHL SFMDPGPEGK LYSEDYDDNY DELESGDWMD GYNSASTARC
     GDEVARYLDH LLAHTAPHPK LAPASQKGGL NRFRAAVQTT CDLMSLVTKA KELHVQNVHM
     YLPTKLFQAS RPSLNLLDSS HPSQEDQVPT VRVEVHLPRD QSGEVDFQAL VLQLKETSSL
     QEQADILYML YTMKGPDWDT ELYEEGSATV RELLTELYGK VGKIRHWGLI RYISGILRKK
     VEALDEACTD LLSHQKHLTV GLPPEPREKT ISAPLPYEAL TRLIEEACEG DMNISILTQE
     IMVYLAMYMR TQPGLFAEMF RLRIGLIIQV MATELAHSLR CSAEEATEGL MNLSPSAMKN
     LLHHILSGKE FGVERSVRPT DSNVSPAISI HEIGAVGATK TERTGIMQLK SEIKQVEFRR
     LSISTESQPN GGHSLGADLM SPSFLSPGTS VTPSSGSFPG HHTSKDSRQG QWQRRRRLDG
     ALNRVPIGFY QKVWKVLQKC HGLSVEGFVL PSSTTREMTP GEIKFSVHVE SVLNRVPQPE
     YRQLLVEAIL VLTMLADIEI HSIGSIIAVE KIVHIANDLF LQEQKTLGAD DIMLAKDPAS
     GICTLLYDSA PSGRFGTMTY LSKAAATYVQ EFLPHSICAM Q
//

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