ID PGM1_RABIT Reviewed; 562 AA. AC P00949; P38651; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 10-JUN-2026, entry version 172. DE RecName: Full=Phosphoglucomutase-1; DE Short=PGM 1; DE EC=5.4.2.2 {ECO:0000269|PubMed:1328221}; DE AltName: Full=Glucose phosphomutase 1; GN Name=PGM1; 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 PROTEIN SEQUENCE (ISOFORM 1). RC TISSUE=Muscle; RX PubMed=6223925; DOI=10.1016/s0021-9258(17)44646-1; RA Ray W.J. Jr., Hermodson M.A., Puvathingal J.M., Mahoney W.C.; RT "The complete amino acid sequence of rabbit muscle phosphoglucomutase."; RL J. Biol. Chem. 258:9166-9174(1983). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1530890; DOI=10.1073/pnas.89.1.411; RA Whitehouse D.B., Putt W., Lovegrove J.U., Morrison K.E., Hollyoake M., RA Fox M.F., Hopkinson D.A., Edwards Y.H.; RT "Phosphoglucomutase 1: complete human and rabbit mRNA sequences and direct RT mapping of this highly polymorphic marker on human chromosome 1."; RL Proc. Natl. Acad. Sci. U.S.A. 89:411-415(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND RP CATALYTIC ACTIVITY. RC TISSUE=Skeletal muscle; RX PubMed=1328221; DOI=10.1016/s0021-9258(19)36800-0; RA Lee Y.S., Marks A.R., Gureckas N., Lacro R., Nadal-Ginard B., Kim D.H.; RT "Purification, characterization, and molecular cloning of a 60-kDa RT phosphoprotein in rabbit skeletal sarcoplasmic reticulum which is an RT isoform of phosphoglucomutase."; RL J. Biol. Chem. 267:21080-21088(1992). RN [4] RP ACTIVE SITE. RX PubMed=5669853; DOI=10.1042/bj1090093; RA Milstein C.P., Milstein C.; RT "A tryptic peptide containing a unique serine phosphate residue in rabbit RT phosphoglucomutase."; RL Biochem. J. 109:93-99(1968). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS). RX PubMed=1532581; DOI=10.1016/s0021-9258(18)42699-3; RA Dai J.-B., Liu Y., Ray W.J. Jr., Konno M.; RT "The crystal structure of muscle phosphoglucomutase refined at 2.7-A RT resolution."; RL J. Biol. Chem. 267:6322-6337(1992). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS). RX PubMed=15299904; DOI=10.1107/s0907444997000887; RA Ray W.J. Jr., Baranidharan S., Liu Y.; RT "Enhanced diffractivity of phosphoglucomutase crystals. Use of an RT alternative cryocrystallographic procedure."; RL Acta Crystallogr. D 53:385-391(1997). RN [7] {ECO:0007744|PDB:1LXT, ECO:0007744|PDB:3PMG} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, SUBUNIT, RP ACTIVITY REGULATION, AND PHOSPHORYLATION AT SER-117. RX PubMed=15299905; DOI=10.1107/s0907444997000875; RA Liu Y., Ray W.J. Jr., Baranidharan S.; RT "Structure of rabbit muscle phosphoglucomutase refined at 2.4-A RT resolution."; RL Acta Crystallogr. D 53:392-405(1997). RN [8] {ECO:0007744|PDB:1C47} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ALPHA-D-GLUCOSE RP 1,6-BISPHOSPHATE. RA Baranidharan S., Ray W.J. Jr., Liu Y.; RT "Binding driven structural changes in crystaline phosphoglucomutase RT associated with chemical reaction."; RL Submitted (AUG-1999) to the PDB data bank. RN [9] {ECO:0007744|PDB:1C4G} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG. RA Baranidharan S., Ray W.J. Jr.; RT "Structural relationships at the active site of Phos in analog complexes."; RL Submitted (AUG-1999) to the PDB data bank. CC -!- FUNCTION: Catalyzes the reversible isomerization of alpha-D-glucose 1- CC phosphate to alpha-D-glucose 6-phosphate (PubMed:1328221). The CC mechanism proceeds via the intermediate compound alpha-D-glucose 1,6- CC bisphosphate (Probable). This enzyme participates in both the breakdown CC and synthesis of glucose (By similarity). CC {ECO:0000250|UniProtKB:P36871, ECO:0000269|PubMed:1328221, CC ECO:0000305|PubMed:1328221}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; CC EC=5.4.2.2; Evidence={ECO:0000269|PubMed:1328221}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-seryl-[protein] + alpha-D-glucose 1-phosphate = CC alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein]; CC Xref=Rhea:RHEA:68748, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, CC ChEBI:CHEBI:29999, ChEBI:CHEBI:58392, ChEBI:CHEBI:58601, CC ChEBI:CHEBI:83421; Evidence={ECO:0000305|PubMed:1328221}; CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein] = O- CC phospho-L-seryl-[protein] + alpha-D-glucose 6-phosphate; CC Xref=Rhea:RHEA:68752, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, CC ChEBI:CHEBI:29999, ChEBI:CHEBI:58225, ChEBI:CHEBI:58392, CC ChEBI:CHEBI:83421; Evidence={ECO:0000305|PubMed:1328221}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:15299905}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:15299905}; CC -!- ACTIVITY REGULATION: Glucose-1,6-bisphosphate enhances phosphorylation CC of the active site Ser-117, and thereby increases enzyme activity. CC {ECO:0000305|PubMed:15299905}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15299905, CC ECO:0000269|PubMed:6223925}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Sarcoplasmic reticulum CC {ECO:0000269|PubMed:1328221}. Note=Localizes to the junctional skeletal CC sarcoplasmic reticulum, probably by association with phospholipids CC and/or other proteins. {ECO:0000269|PubMed:1328221}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P00949-1; Sequence=Displayed; CC Name=2; CC IsoId=P00949-2; Sequence=VSP_004690, VSP_004691, VSP_004692, CC VSP_004693; CC -!- PTM: Isoform 2 is the major calmodulin-dependent phosphoprotein in CC junctional skeletal sarcoplasmic reticulum vesicles. CC {ECO:0000269|PubMed:1328221}. CC -!- PTM: Phosphorylation at Thr-467 by PAK1 significantly enhances CC enzymatic activity. {ECO:0000250|UniProtKB:P36871}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M97664; AAA31454.1; -; mRNA. DR EMBL; M97663; AAA31453.1; -; mRNA. DR PIR; A45077; PMRBI. DR PIR; B41801; PMRB. DR RefSeq; NP_001075785.1; NM_001082316.1. [P00949-2] DR PDB; 1C47; X-ray; 2.70 A; A/B=2-562. DR PDB; 1C4G; X-ray; 2.70 A; A/B=2-562. DR PDB; 1JDY; X-ray; 2.70 A; A/B=2-562. DR PDB; 1LXT; X-ray; 2.70 A; A/B=2-562. DR PDB; 1VKL; X-ray; 2.70 A; A/B=2-562. DR PDB; 3PMG; X-ray; 2.40 A; A/B=2-562. DR AlphaFoldDB; P00949; -. DR PCDDB; P00949; -. DR SMR; P00949; -. DR FunCoup; P00949; 603. DR STRING; 9986.ENSOCUP00000025628; -. DR iPTMnet; P00949; -. DR PaxDb; 9986-ENSOCUP00000025628; -. DR GeneID; 100009155; -. DR KEGG; ocu:100009155; -. DR CTD; 5236; -. DR eggNOG; KOG0027; Eukaryota. DR eggNOG; KOG0625; Eukaryota. DR InParanoid; P00949; -. DR OrthoDB; 2291at2759; -. DR EvolutionaryTrace; P00949; -. DR Proteomes; UP000001811; Unplaced. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0004614; F:phosphoglucomutase activity; IDA:UniProtKB. DR GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB. DR CDD; cd03085; PGM1; 1. DR FunFam; 3.30.310.50:FF:000002; Phosphoglucomutase 5; 1. DR FunFam; 3.40.120.10:FF:000004; Phosphoglucomutase 5; 1. DR FunFam; 3.40.120.10:FF:000005; Phosphoglucomutase 5; 1. DR FunFam; 3.40.120.10:FF:000007; Phosphoglucomutase 5; 1. DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3. DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1. DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I. DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III. DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II. DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III. DR InterPro; IPR036900; A-D-PHexomutase_C_sf. DR InterPro; IPR016066; A-D-PHexomutase_CS. DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF. DR InterPro; IPR045244; PGM. DR NCBIfam; NF005737; PRK07564.1-1; 1. DR PANTHER; PTHR22573:SF37; PHOSPHOGLUCOMUTASE-1; 1. DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1. DR Pfam; PF24947; PGM1_C_vert_fung; 1. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR Pfam; PF02880; PGM_PMM_III; 1. DR PRINTS; PR00509; PGMPMM. DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1. DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3. DR PROSITE; PS00710; PGM_PMM; 1. DR PDBsum; 1C47; -. DR PDBsum; 1C4G; -. DR PDBsum; 1JDY; -. DR PDBsum; 1LXT; -. DR PDBsum; 1VKL; -. DR PDBsum; 3PMG; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism; KW Cytoplasm; Direct protein sequencing; Glucose metabolism; Isomerase; KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome; KW Sarcoplasmic reticulum. FT CHAIN 1..562 FT /note="Phosphoglucomutase-1" FT /id="PRO_0000147779" FT ACT_SITE 117 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000269|PubMed:5669853" FT BINDING 23 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47" FT BINDING 117 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47" FT BINDING 117 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via phosphate group" FT /evidence="ECO:0000269|PubMed:15299905, FT ECO:0007744|PDB:3PMG" FT BINDING 288 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15299905, FT ECO:0007744|PDB:3PMG" FT BINDING 290 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15299905, FT ECO:0007744|PDB:3PMG" FT BINDING 292 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47" FT BINDING 292 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15299905, FT ECO:0007744|PDB:3PMG" FT BINDING 293 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47" FT BINDING 357 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47" FT BINDING 376 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47" FT BINDING 378 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47" FT BINDING 389 FT /ligand="alpha-D-glucose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:58392" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1C47" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 16 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 115 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9D0F9" FT MOD_RES 117 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15299905, FT ECO:0007744|PDB:3PMG" FT MOD_RES 134 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38652" FT MOD_RES 185 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 213 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38652" FT MOD_RES 349 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D0F9" FT MOD_RES 353 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9D0F9" FT MOD_RES 369 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38652" FT MOD_RES 378 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 419 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D0F9" FT MOD_RES 467 FT /note="Phosphothreonine; by PAK1" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 485 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38652" FT MOD_RES 505 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 507 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9D0F9" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P36871" FT MOD_RES 541 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P38652" FT VAR_SEQ 1..13 FT /note="MVKIVTVKTKAYP -> MEEGPLPLLTIRTAPYH (in isoform 2)" FT /evidence="ECO:0000303|PubMed:1328221" FT /id="VSP_004690" FT VAR_SEQ 25..36 FT /note="RVKVFQSSTNYA -> KTYYFEDKPCYL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:1328221" FT /id="VSP_004691" FT VAR_SEQ 44..56 FT /note="ISTVEPAQRQEAT -> FFSIDLKDRQGSS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:1328221" FT /id="VSP_004692" FT VAR_SEQ 65..77 FT /note="FYMKEAIQLIVRI -> YFNKSAIETILQM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:1328221" FT /id="VSP_004693" FT STRAND 5..8 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 21..25 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 26..31 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 35..45 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:3PMG" FT TURN 52..54 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 67..80 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 85..93 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 96..106 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 109..114 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 125..133 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 141..153 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:1JDY" FT STRAND 171..175 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 184..189 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 193..200 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 205..213 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:1C47" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 229..232 FT /evidence="ECO:0007829|PDB:1C47" FT HELIX 233..240 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:3PMG" FT TURN 266..269 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 270..277 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 282..287 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:1C47" FT STRAND 294..298 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 299..301 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 306..315 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 317..319 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 321..326 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 340..346 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 359..367 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 372..376 FT /evidence="ECO:0007829|PDB:3PMG" FT TURN 377..379 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 380..383 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 386..388 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 391..405 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 409..420 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 422..433 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 435..450 FT /evidence="ECO:0007829|PDB:3PMG" FT TURN 452..456 FT /evidence="ECO:0007829|PDB:1C47" FT STRAND 458..461 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 464..473 FT /evidence="ECO:0007829|PDB:3PMG" FT TURN 479..481 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 490..494 FT /evidence="ECO:0007829|PDB:3PMG" FT TURN 495..497 FT /evidence="ECO:0007829|PDB:1LXT" FT STRAND 499..506 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 508..510 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 512..522 FT /evidence="ECO:0007829|PDB:3PMG" FT TURN 525..529 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 532..547 FT /evidence="ECO:0007829|PDB:3PMG" FT HELIX 549..553 FT /evidence="ECO:0007829|PDB:3PMG" FT STRAND 559..561 FT /evidence="ECO:0007829|PDB:3PMG" SQ SEQUENCE 562 AA; 61558 MW; 6D9F42284EF09002 CRC64; MVKIVTVKTK AYPDQKPGTS GLRKRVKVFQ SSTNYAENFI QSIISTVEPA QRQEATLVVG GDGRFYMKEA IQLIVRIAAA NGIGRLVIGQ NGILSTPAVS CIIRKIKAIG GIILTASHNP GGPNGDFGIK FNISNGGPAP EAITDKIFQI SKTIEEYAIC PDLKVDLGVL GKQQFDLENK FKPFTVEIVD SVEAYATMLR NIFDFNALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE LGAPANSAVN CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVANATKI ALYETPTGWK FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS ILATRKQSVE DILKDHWHKF GRNFFTRYDY EEVEAEGATK MMKDLEALMF DRSFVGKQFS ANDKVYTVEK ADNFEYHDPV DGSVSKNQGL RLIFADGSRI IFRLSGTGSA GATIRLYIDS YEKDNAKINQ DPQVMLAPLI SIALKVSQLQ ERTGRTAPTV IT //