PYGB_HUMAN
ID PYGB_HUMAN Reviewed; 843 AA.
AC P11216; Q96AK1; Q9NPX8;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=Glycogen phosphorylase, brain form {ECO:0000303|PubMed:3346228};
DE EC=2.4.1.1 {ECO:0000269|PubMed:27402852};
GN Name=PYGB {ECO:0000303|PubMed:3346228};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3346228; DOI=10.1016/s0021-9258(18)69003-9;
RA Newgard C.B., Littman D.R., van Genderen C., Smith M., Fletterick R.J.;
RT "Human brain glycogen phosphorylase. Cloning, sequence analysis,
RT chromosomal mapping, tissue expression, and comparison with the human liver
RT and muscle isozymes.";
RL J. Biol. Chem. 263:3850-3857(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2615594; DOI=10.1016/0169-328x(89)90052-1;
RA Gelinas R.P., Froman B.E., McElroy F., Tait R.C., Gorin F.A.;
RT "Human brain glycogen phosphorylase: characterization of fetal cDNA and
RT genomic sequences.";
RL Brain Res. Mol. Brain Res. 6:177-185(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP PROTEIN SEQUENCE OF 2-11; 18-30; 51-61; 71-78; 193-206; 271-278; 353-359;
RP 388-395; 400-425; 508-520; 522-533; 546-552; 558-569; 577-590; 623-640;
RP 657-681; 731-754 AND 817-823, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon adenocarcinoma;
RA Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-843 IN COMPLEX WITH AMP,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND
RP PHOSPHORYLATION.
RX PubMed=27402852; DOI=10.1074/jbc.m116.738898;
RA Mathieu C., de la Sierra-Gallay I.L., Duval R., Xu X., Cocaign A.,
RA Leger T., Woffendin G., Camadro J.M., Etchebest C., Haouz A., Dupret J.M.,
RA Rodrigues-Lima F.;
RT "Insights into Brain Glycogen Metabolism: THE STRUCTURE OF HUMAN BRAIN
RT GLYCOGEN PHOSPHORYLASE.";
RL J. Biol. Chem. 291:18072-18083(2016).
CC -!- FUNCTION: Glycogen phosphorylase that regulates glycogen mobilization
CC (PubMed:27402852). Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism (PubMed:3346228). Enzymes from different
CC sources differ in their regulatory mechanisms and in their natural
CC substrates (PubMed:3346228). However, all known phosphorylases share
CC catalytic and structural properties (PubMed:3346228).
CC {ECO:0000269|PubMed:27402852, ECO:0000303|PubMed:3346228}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000269|PubMed:27402852};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Activity of phosphorylase is controlled both by
CC allosteric means (through the non-covalent binding of metabolites) and
CC by covalent modification. Thus AMP allosterically activates, whereas
CC ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase
CC B. Activated upon phosphorylation. {ECO:0000269|PubMed:27402852}.
CC -!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
CC enzymatically active phosphorylase A. {ECO:0000269|PubMed:27402852}.
CC -!- INTERACTION:
CC P11216; Q86XI6: PPP1R3B; NbExp=3; IntAct=EBI-1047231, EBI-3918864;
CC P11216; P06737: PYGL; NbExp=9; IntAct=EBI-1047231, EBI-2511865;
CC P11216; P11217: PYGM; NbExp=3; IntAct=EBI-1047231, EBI-357469;
CC P11216; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-1047231, EBI-747107;
CC -!- PTM: Phosphorylated (PubMed:27402852). Phosphorylation of Ser-15
CC converts phosphorylase B (unphosphorylated) to phosphorylase A (By
CC similarity). {ECO:0000250|UniProtKB:P11217,
CC ECO:0000269|PubMed:27402852}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; J03544; AAA59597.1; -; mRNA.
DR EMBL; U47025; AAB60395.1; -; mRNA.
DR EMBL; AL121772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017045; AAH17045.1; -; mRNA.
DR EMBL; BC030795; AAH30795.1; -; mRNA.
DR CCDS; CCDS13171.1; -.
DR PIR; A40138; A40138.
DR RefSeq; NP_002853.2; NM_002862.3.
DR PDB; 5IKO; X-ray; 2.50 A; A=1-843.
DR PDB; 5IKP; X-ray; 3.40 A; A=1-843.
DR PDBsum; 5IKO; -.
DR PDBsum; 5IKP; -.
DR AlphaFoldDB; P11216; -.
DR SMR; P11216; -.
DR BioGRID; 111792; 82.
DR IntAct; P11216; 31.
DR MINT; P11216; -.
DR STRING; 9606.ENSP00000216962; -.
DR BindingDB; P11216; -.
DR ChEMBL; CHEMBL3856; -.
DR DrugBank; DB03496; Alvocidib.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR GlyGen; P11216; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P11216; -.
DR MetOSite; P11216; -.
DR PhosphoSitePlus; P11216; -.
DR SwissPalm; P11216; -.
DR BioMuta; PYGB; -.
DR DMDM; 20178317; -.
DR EPD; P11216; -.
DR jPOST; P11216; -.
DR MassIVE; P11216; -.
DR MaxQB; P11216; -.
DR PaxDb; P11216; -.
DR PeptideAtlas; P11216; -.
DR PRIDE; P11216; -.
DR ProteomicsDB; 52720; -.
DR Antibodypedia; 10014; 633 antibodies from 35 providers.
DR DNASU; 5834; -.
DR Ensembl; ENST00000216962.9; ENSP00000216962.3; ENSG00000100994.12.
DR GeneID; 5834; -.
DR KEGG; hsa:5834; -.
DR MANE-Select; ENST00000216962.9; ENSP00000216962.3; NM_002862.4; NP_002853.2.
DR UCSC; uc002wup.4; human.
DR CTD; 5834; -.
DR DisGeNET; 5834; -.
DR GeneCards; PYGB; -.
DR HGNC; HGNC:9723; PYGB.
DR HPA; ENSG00000100994; Low tissue specificity.
DR MIM; 138550; gene.
DR neXtProt; NX_P11216; -.
DR OpenTargets; ENSG00000100994; -.
DR PharmGKB; PA34066; -.
DR VEuPathDB; HostDB:ENSG00000100994; -.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_1_1_1; -.
DR InParanoid; P11216; -.
DR OMA; HCACSVA; -.
DR OrthoDB; 240595at2759; -.
DR PhylomeDB; P11216; -.
DR TreeFam; TF300309; -.
DR BioCyc; MetaCyc:HS02178-MON; -.
DR PathwayCommons; P11216; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; P11216; -.
DR SIGNOR; P11216; -.
DR BioGRID-ORCS; 5834; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; PYGB; human.
DR GenomeRNAi; 5834; -.
DR Pharos; P11216; Tchem.
DR PRO; PR:P11216; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P11216; protein.
DR Bgee; ENSG00000100994; Expressed in lower esophagus muscularis layer and 176 other tissues.
DR ExpressionAtlas; P11216; baseline and differential.
DR Genevisible; P11216; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism;
KW Direct protein sequencing; Glycogen metabolism; Glycosyltransferase;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378"
FT CHAIN 2..843
FT /note="Glycogen phosphorylase, brain form"
FT /id="PRO_0000188535"
FT REGION 677..678
FT /note="Pyridoxal 5'-phosphate"
FT /evidence="ECO:0000269|PubMed:27402852"
FT BINDING 43
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:27402852"
FT BINDING 197
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:27402852"
FT BINDING 310
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:27402852"
FT BINDING 569
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:27402852"
FT SITE 76
FT /note="Participates in a stacking interaction with the
FT adenine ring of AMP"
FT /evidence="ECO:0000269|PubMed:27402852"
FT SITE 109
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250"
FT SITE 143
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250"
FT SITE 156
FT /note="May be involved in allosteric control"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 15
FT /note="Phosphoserine; by PHK; in form phosphorylase A"
FT /evidence="ECO:0000250|UniProtKB:P53534"
FT MOD_RES 197
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI94"
FT MOD_RES 473
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI94"
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:27402852"
FT VARIANT 303
FT /note="A -> S (in dbSNP:rs2228976)"
FT /id="VAR_034428"
FT VARIANT 502
FT /note="D -> N (in dbSNP:rs2227891)"
FT /id="VAR_020212"
FT CONFLICT 2..3
FT /note="AK -> GE (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="K -> R (in Ref. 1; AAA59597)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="A -> G (in Ref. 1; AAA59597)"
FT /evidence="ECO:0000305"
FT CONFLICT 835..843
FT /note="IPPPNIPRD -> LQHLPHPEWESGGATCWAPPELCTHLAMY (in Ref.
FT 1; AAA59597)"
FT /evidence="ECO:0000305"
FT HELIX 23..38
FT /evidence="ECO:0007829|PDB:5IKO"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 49..78
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5IKP"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:5IKO"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 199..210
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 213..232
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:5IKP"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 290..313
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 390..396
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 398..418
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 442..448
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:5IKO"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 470..475
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 490..495
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 498..508
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 516..526
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 529..554
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 562..569
FT /evidence="ECO:0007829|PDB:5IKO"
FT TURN 573..576
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 577..593
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 602..607
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 615..632
FT /evidence="ECO:0007829|PDB:5IKO"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 641..648
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 651..657
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:5IKP"
FT STRAND 662..666
FT /evidence="ECO:0007829|PDB:5IKO"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:5IKP"
FT HELIX 678..684
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 696..704
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 706..708
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 716..725
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 730..734
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 737..748
FT /evidence="ECO:0007829|PDB:5IKO"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:5IKO"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:5IKP"
FT TURN 756..759
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 760..768
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 774..792
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 795..807
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 810..812
FT /evidence="ECO:0007829|PDB:5IKO"
FT HELIX 814..824
FT /evidence="ECO:0007829|PDB:5IKO"
SQ SEQUENCE 843 AA; 96696 MW; 810BFAD3002CACB0 CRC64;
MAKPLTDSEK RKQISVRGLA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV
RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQNACD EAIYQLGLDL
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA
DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PDGVKWLDTQ VVLAMPYDTP VPGYKNNTVN
TMRLWSAKAP NDFKLQDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV
DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP
GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF
QNKTNGITPR RWLLLCNPGL ADTIVEKIGE EFLTDLSQLK KLLPLVSDEV FIRDVAKVKQ
ENKLKFSAFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKRDPAKAFV
PRTVMIGGKA APGYHMAKLI IKLVTSIGDV VNHDPVVGDR LKVIFLENYR VSLAEKVIPA
ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGAENLF IFGLRVEDVE
ALDRKGYNAR EYYDHLPELK QAVDQISSGF FSPKEPDCFK DIVNMLMHHD RFKVFADYEA
YMQCQAQVDQ LYRNPKEWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNI
PRD
