LOCUS       NP_037320                843 aa            linear   ROD 04-JUN-2024
DEFINITION  glycogen phosphorylase, brain form [Rattus norvegicus].
ACCESSION   NP_037320 XP_001057365 XP_342543
VERSION     NP_037320.1
DBSOURCE    REFSEQ: accession NM_013188.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Dienel,G.A., Ball,K.K. and Cruz,N.F.
  TITLE     A glycogen phosphorylase inhibitor selectively enhances local rates
            of glucose utilization in brain during sensory stimulation of
            conscious rats: implications for glycogen turnover
  JOURNAL   J Neurochem 102 (2), 466-478 (2007)
   PUBMED   17442042
  REMARK    GeneRIF: Thus, glycogen is an active fuel for specific structures
            in normal activated brain, not simply an emergency fuel depot and
            flux-generated pyruvate greatly exceeded net accumulation of
            lactate or net consumption of glycogen during activation. T
REFERENCE   3  (residues 1 to 843)
  AUTHORS   Pfeiffer-Guglielmi,B., Francke,M., Reichenbach,A. and Hamprecht,B.
  TITLE     Glycogen phosphorylase isozymes and energy metabolism in the rat
            peripheral nervous system--an immunocytochemical study
  JOURNAL   Brain Res 1136 (1), 20-27 (2007)
   PUBMED   17239832
REFERENCE   4  (residues 1 to 843)
  AUTHORS   Birch,A.M., Kenny,P.W., Oikonomakos,N.G., Otterbein,L.,
            Schofield,P., Whittamore,P.R. and Whalley,D.P.
  TITLE     Development of potent, orally active
            1-substituted-3,4-dihydro-2-quinolone glycogen phosphorylase
            inhibitors
  JOURNAL   Bioorg Med Chem Lett 17 (2), 394-399 (2007)
   PUBMED   17095214
REFERENCE   5  (residues 1 to 843)
  AUTHORS   Pfeiffer-Guglielmi,B., Coles,J.A., Francke,M., Reichenbach,A.,
            Fleckenstein,B., Jung,G., Nicaise,G. and Hamprecht,B.
  TITLE     Immunocytochemical analysis of rat vagus nerve by antibodies
            against glycogen phosphorylase isozymes
  JOURNAL   Brain Res 1110 (1), 23-29 (2006)
   PUBMED   16879805
  REMARK    GeneRIF: We have demonstrated immunocytochemically the presence of
            glycogen phosphorylase, brain form in large and small axons of the
            rat vagus nerve, but not in Schwann cells.
REFERENCE   6  (residues 1 to 843)
  AUTHORS   Lomako,J., Lomako,W.M., Whelan,W.J., Dombro,R.S., Neary,J.T. and
            Norenberg,M.D.
  TITLE     Glycogen synthesis in the astrocyte: from glycogenin to proglycogen
            to glycogen
  JOURNAL   FASEB J 7 (14), 1386-1393 (1993)
   PUBMED   8224611
REFERENCE   7  (residues 1 to 843)
  AUTHORS   Hudson,J.W., Hefferon,K.L. and Crerar,M.M.
  TITLE     Comparative analysis of species-independent, isozyme-specific
            amino-acid substitutions in mammalian muscle, brain and liver
            glycogen phosphorylases
  JOURNAL   Biochim Biophys Acta 1164 (2), 197-208 (1993)
   PUBMED   7916624
REFERENCE   8  (residues 1 to 843)
  AUTHORS   Mayer,D., Seelmann-Eggebert,G. and Letsch,I.
  TITLE     Glycogen phosphorylase isoenzymes from hepatoma 3924A and from a
            non-tumorigenic liver cell line. Comparison with the liver and
            brain enzymes
  JOURNAL   Biochem J 282 (Pt 3) (Pt 3), 665-673 (1992)
   PUBMED   1554349
REFERENCE   9  (residues 1 to 843)
  AUTHORS   Johnson,L.N.
  TITLE     Glycogen phosphorylase: control by phosphorylation and allosteric
            effectors
  JOURNAL   FASEB J 6 (6), 2274-2282 (1992)
   PUBMED   1544539
  REMARK    Review article
REFERENCE   10 (residues 1 to 843)
  AUTHORS   Crerar,M.M., Hudson,J.W., Matthews,K.E., David,E.S. and
            Golding,G.B.
  TITLE     Studies on the expression and evolution of the glycogen
            phosphorylase gene family in the rat
  JOURNAL   Genome 30 (4), 582-590 (1988)
   PUBMED   3209063
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB720204.1, L10668.1, CK357665.1, CO400919.1, CA504871.1 and
            AW535913.1.
            
            On or before Oct 13, 2007 this sequence version replaced
            XP_342543.1, XP_001057365.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L10668.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..843
                     /product="glycogen phosphorylase, brain form"
                     /EC_number="2.4.1.1"
                     /note="brain glycogen phosphorylase; phosphorylase,
                     glycogen; brain"
                     /calculated_mol_wt=96607
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P11216; propagated from
                     UniProtKB/Swiss-Prot (P53534.3)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P53534.3)"
     Region          29..828
                     /region_name="GT35_Glycogen_Phosphorylase"
                     /note="glycogen phosphorylase and similar proteins;
                     cd04300"
                     /db_xref="CDD:340853"
     Site            order(29,31,33..34,36..38,61..63,194,283,286)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340853"
     Site            76
                     /site_type="other"
                     /note="Participates in a stacking interaction with the
                     adenine ring of AMP.
                     /evidence=ECO:0000250|UniProtKB:P11216; propagated from
                     UniProtKB/Swiss-Prot (P53534.3)"
     Site            order(89,91,135..137,281,284,286,293,340,342,378..379,383,
                     485,492,569..570,572..575,609,614,616,650..651,673,
                     675..678,681)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:340853"
     Site            109
                     /site_type="other"
                     /note="Involved in the association of subunits.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P53534.3)"
     Site            143
                     /site_type="other"
                     /note="Involved in the association of subunits.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P53534.3)"
     Site            156
                     /site_type="other"
                     /note="May be involved in allosteric control.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P53534.3)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8CI94; propagated from
                     UniProtKB/Swiss-Prot (P53534.3)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8CI94; propagated from
                     UniProtKB/Swiss-Prot (P53534.3)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P53534.3)"
     Region          677..678
                     /region_name="Pyridoxal 5'-phosphate.
                     /evidence=ECO:0000250|UniProtKB:P11216"
                     /note="propagated from UniProtKB/Swiss-Prot (P53534.3)"
     CDS             1..843
                     /gene="Pygb"
                     /gene_synonym="GLYPHOA"
                     /coded_by="NM_013188.1:110..2641"
                     /db_xref="GeneID:25739"
                     /db_xref="RGD:3460"
ORIGIN      
        1 makpltdser qkqisvrgia glgdvaevrk sfnrhlhftl vkdrnvatpr dyffalahtv
       61 rdhlvgrwir tqqhyyerdp kriyylslef ymgrtlqntm vnlglqtacd eatyqlgldl
      121 eeleeieeda glgngglgrl aacfldsmat lglaaygygi ryefgifnqk ivngwqveea
      181 ddwlrygnpw ekarpeymlp vhfygrveht pngvlwldtq vvlampydtp vpgyknntvn
      241 tmrlwsakap ndfklkdfnv gdyieavldr nlaenisrvl ypndnffegk elrlkqeyfv
      301 vaatlqdiir rfksskfgcr dpvrtcfetf pdkvaiqlnd thpalsipel mrilvdvekv
      361 dwdkaweitk ktcaytnhtv lpealerwpv smfekllprh leiiyainqr hldhvaalfp
      421 gdvdrlrrms vieegdckri nmahlcvigs havngvarih seivkqsvfk dfyelepekf
      481 qnktngitpr rwlllcnpgl aeiiverige gfltdlsqlk kllslvddea firdvakvkq
      541 enklkfsaql ekeykvkinp asmfdvhvkr iheykrqlln clhiitlynr ikkdptktfv
      601 prtvmiggka apgyhmakmi iklvtsigdv vnhdpvvgdr lrviflenyr vslaekvipa
      661 adlsqqista gteasgtgnm kfmlngalti gtmdganvem aeeageenlf ifgmrvedve
      721 aldqkgynar efyerlpelr qavdqissgf fspkdpdcfk dvvnmlmyhd rfkvfadyea
      781 yiqcqaqvdh lyrnpkdwtk kvirniacsg kfssdrtite yareiwgvep sdlqipppnl
      841 pkd
//
