PGM1_HUMAN
ID PGM1_HUMAN Reviewed; 562 AA.
AC P36871; B2R5N9; B4DPV0; Q16105; Q16106; Q5BKZ9; Q6NW22; Q86U74; Q96J40;
AC Q9NTY4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Phosphoglucomutase-1;
DE Short=PGM 1;
DE EC=5.4.2.2 {ECO:0000269|PubMed:15378030, ECO:0000269|PubMed:25288802};
DE AltName: Full=Glucose phosphomutase 1;
GN Name=PGM1;
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] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS CYS-221
RP AND HIS-420.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP HIS-420.
RC TISSUE=Astrocyte, and Mesangial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS CYS-221
RP AND HIS-420.
RC TISSUE=Cervix, Hypothalamus, Placenta, 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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82 (ISOFORMS 1 AND 2), AND
RP ALTERNATIVE SPLICING.
RX PubMed=8257433; DOI=10.1042/bj2960417;
RA Putt W., Ives J.H., Hollyoake M., Hopkinson D.A., Whitehouse D.B.,
RA Edwards Y.H.;
RT "Phosphoglucomutase 1: a gene with two promoters and a duplicated first
RT exon.";
RL Biochem. J. 296:417-422(1993).
RN [7]
RP PHOSPHORYLATION AT THR-467, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15378030; DOI=10.1038/sj.onc.1207969;
RA Gururaj A., Barnes C.J., Vadlamudi R.K., Kumar R.;
RT "Regulation of phosphoglucomutase 1 phosphorylation and activity by a
RT signaling kinase.";
RL Oncogene 23:8118-8127(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185; SER-201; SER-206;
RP SER-378; SER-505 AND SER-509, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [19] {ECO:0007744|PDB:5EPC, ECO:0007744|PDB:5F9C, ECO:0007744|PDB:5HSH}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF WILD-TYPE; VARIANT CDG1T ARG-121
RP AND VARIANT ARG-291 IN COMPLEX WITH MAGNESIUM, AND COFACTOR.
RX PubMed=26972339; DOI=10.1016/j.jmb.2016.02.032;
RA Stiers K.M., Kain B.N., Graham A.C., Beamer L.J.;
RT "Induced structural disorder as a molecular mechanism for enzyme
RT dysfunction in phosphoglucomutase 1 deficiency.";
RL J. Mol. Biol. 428:1493-1505(2016).
RN [20]
RP VARIANTS MET-68; CYS-221 AND HIS-420.
RX PubMed=7902567; DOI=10.1073/pnas.90.22.10725;
RA Takahashi N., Neels J.V.;
RT "Intragenic recombination at the human phosphoglucomutase 1 locus:
RT predictions fulfilled.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10725-10729(1993).
RN [21]
RP VARIANTS CYS-221 AND HIS-420.
RX PubMed=7902568; DOI=10.1073/pnas.90.22.10730;
RA March R.E., Putt W., Hollyoake M., Ives J.H., Lovegrove J.U.,
RA Hopkinson D.A., Edwards Y.H., Whitehouse D.B.;
RT "The classical human phosphoglucomutase (PGM1) isozyme polymorphism is
RT generated by intragenic recombination.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10730-10733(1993).
RN [22]
RP INVOLVEMENT IN CDG1T, AND VARIANT CDG1T ALA-115.
RX PubMed=19625727; DOI=10.1056/nejmc0901158;
RA Stojkovic T., Vissing J., Petit F., Piraud M., Orngreen M.C., Andersen G.,
RA Claeys K.G., Wary C., Hogrel J.Y., Laforet P.;
RT "Muscle glycogenosis due to phosphoglucomutase 1 deficiency.";
RL N. Engl. J. Med. 361:425-427(2009).
RN [23]
RP VARIANT CDG1T ARG-121.
RX PubMed=22492991; DOI=10.1093/hmg/dds123;
RA Timal S., Hoischen A., Lehle L., Adamowicz M., Huijben K.,
RA Sykut-Cegielska J., Paprocka J., Jamroz E., van Spronsen F.J., Korner C.,
RA Gilissen C., Rodenburg R.J., Eidhof I., Van den Heuvel L., Thiel C.,
RA Wevers R.A., Morava E., Veltman J., Lefeber D.J.;
RT "Gene identification in the congenital disorders of glycosylation type I by
RT whole-exome sequencing.";
RL Hum. Mol. Genet. 21:4151-4161(2012).
RN [24]
RP VARIANT CDG1T ARG-291.
RX PubMed=22976764; DOI=10.1007/s10545-012-9525-7;
RA Perez B., Medrano C., Ecay M.J., Ruiz-Sala P., Martinez-Pardo M.,
RA Ugarte M., Perez-Cerda C.;
RT "A novel congenital disorder of glycosylation type without central nervous
RT system involvement caused by mutations in the phosphoglucomutase 1 gene.";
RL J. Inherit. Metab. Dis. 36:535-542(2013).
RN [25]
RP VARIANTS CDG1T ALA-19; TYR-38; ARG-41; HIS-62; ALA-115; ARG-121; TYR-263;
RP GLY-263; ARG-291; ARG-330; LYS-377; LYS-388 AND PRO-516.
RX PubMed=24499211; DOI=10.1056/nejmoa1206605;
RA Tegtmeyer L.C., Rust S., van Scherpenzeel M., Ng B.G., Losfeld M.E.,
RA Timal S., Raymond K., He P., Ichikawa M., Veltman J., Huijben K.,
RA Shin Y.S., Sharma V., Adamowicz M., Lammens M., Reunert J., Witten A.,
RA Schrapers E., Matthijs G., Jaeken J., Rymen D., Stojkovic T., Laforet P.,
RA Petit F., Aumaitre O., Czarnowska E., Piraud M., Podskarbi T.,
RA Stanley C.A., Matalon R., Burda P., Seyyedi S., Debus V., Socha P.,
RA Sykut-Cegielska J., van Spronsen F., de Meirleir L., Vajro P., DeClue T.,
RA Ficicioglu C., Wada Y., Wevers R.A., Vanderschaeghe D., Callewaert N.,
RA Fingerhut R., van Schaftingen E., Freeze H.H., Morava E., Lefeber D.J.,
RA Marquardt T.;
RT "Multiple phenotypes in phosphoglucomutase 1 deficiency.";
RL N. Engl. J. Med. 370:533-542(2014).
RN [26]
RP CHARACTERIZATION OF VARIANTS CDG1T ALA-19; TYR-38; ARG-41; HIS-62; ALA-115;
RP ARG-121; GLY-263; TYR-263; ARG-291; ARG-330; LYS-377; LYS-388 AND PRO-516,
RP VARIANTS MET-68; CYS-221 AND HIS-420, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, PHOSPHORYLATION AT SER-117, AND
RP ACTIVITY REGULATION.
RX PubMed=25288802; DOI=10.1074/jbc.m114.597914;
RA Lee Y., Stiers K.M., Kain B.N., Beamer L.J.;
RT "Compromised catalysis and potential folding defects in in vitro studies of
RT missense mutants associated with hereditary phosphoglucomutase 1
RT deficiency.";
RL J. Biol. Chem. 289:32010-32019(2014).
CC -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC of glucose. {ECO:0000269|PubMed:17924679, ECO:0000269|PubMed:25288802}.
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:15378030,
CC ECO:0000269|PubMed:25288802};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:26972339};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:26972339};
CC -!- ACTIVITY REGULATION: Glucose-1,6-bisphosphate enhances phosphorylation
CC of the active site Ser-117, and thereby increases enzyme activity.
CC {ECO:0000269|PubMed:25288802}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 uM for alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:25288802};
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P36871; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-2861475, EBI-717399;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P36871-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36871-2; Sequence=VSP_004686;
CC Name=3;
CC IsoId=P36871-3; Sequence=VSP_045204;
CC -!- PTM: Phosphorylation at Thr-467 by PAK1 significantly enhances
CC enzymatic activity. {ECO:0000269|PubMed:15378030}.
CC -!- POLYMORPHISM: Many polymorphic variants of PGM1 exist. 8 different
CC alleles are known: PGM1*1+, PGM1*1-, PGM1*2+, PGM1*2-, PGM1*3+,
CC PGM1*3-, PGM1*7+ and PGM1*7-. The sequence of PGM1*1+ is shown here.
CC -!- DISEASE: Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. {ECO:0000269|PubMed:19625727,
CC ECO:0000269|PubMed:22492991, ECO:0000269|PubMed:22976764,
CC ECO:0000269|PubMed:24499211, ECO:0000269|PubMed:25288802,
CC ECO:0000269|PubMed:26972339}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH90856.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; M83088; AAA60080.1; -; mRNA.
DR EMBL; BT006961; AAP35607.1; -; mRNA.
DR EMBL; AK298505; BAG60712.1; -; mRNA.
DR EMBL; AK312254; BAG35186.1; -; mRNA.
DR EMBL; AL109925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001756; AAH01756.3; -; mRNA.
DR EMBL; BC019920; AAH19920.1; -; mRNA.
DR EMBL; BC067763; AAH67763.2; -; mRNA.
DR EMBL; BC090856; AAH90856.1; ALT_INIT; mRNA.
DR EMBL; S67989; AAB29177.2; -; Genomic_DNA.
DR EMBL; S67998; AAB29178.1; -; Genomic_DNA.
DR CCDS; CCDS53323.1; -. [P36871-2]
DR CCDS; CCDS53324.1; -. [P36871-3]
DR CCDS; CCDS625.1; -. [P36871-1]
DR PIR; A41801; A41801.
DR PIR; S39397; S39397.
DR RefSeq; NP_001166289.1; NM_001172818.1. [P36871-2]
DR RefSeq; NP_001166290.1; NM_001172819.1. [P36871-3]
DR RefSeq; NP_002624.2; NM_002633.2. [P36871-1]
DR PDB; 5EPC; X-ray; 1.85 A; A/B=1-562.
DR PDB; 5F9C; X-ray; 2.50 A; A/B=1-562.
DR PDB; 5HSH; X-ray; 2.65 A; A/B=1-562.
DR PDB; 5JN5; X-ray; 1.75 A; A/B=1-562.
DR PDB; 5TR2; X-ray; 2.50 A; A/B=1-562.
DR PDB; 5VBI; X-ray; 1.75 A; A/B=1-562.
DR PDB; 5VEC; X-ray; 2.20 A; A/B=1-562.
DR PDB; 5VG7; X-ray; 1.95 A; A/B=1-562.
DR PDB; 5VIN; X-ray; 2.60 A; A/B=1-562.
DR PDB; 6SNO; X-ray; 2.70 A; A=2-562.
DR PDB; 6SNP; X-ray; 2.75 A; A=2-562.
DR PDB; 6SNQ; X-ray; 2.70 A; A=2-562.
DR PDB; 6UIQ; X-ray; 2.30 A; A/B=1-562.
DR PDB; 6UO6; X-ray; 2.15 A; A/B=1-562.
DR PDBsum; 5EPC; -.
DR PDBsum; 5F9C; -.
DR PDBsum; 5HSH; -.
DR PDBsum; 5JN5; -.
DR PDBsum; 5TR2; -.
DR PDBsum; 5VBI; -.
DR PDBsum; 5VEC; -.
DR PDBsum; 5VG7; -.
DR PDBsum; 5VIN; -.
DR PDBsum; 6SNO; -.
DR PDBsum; 6SNP; -.
DR PDBsum; 6SNQ; -.
DR PDBsum; 6UIQ; -.
DR PDBsum; 6UO6; -.
DR AlphaFoldDB; P36871; -.
DR SMR; P36871; -.
DR BioGRID; 111256; 81.
DR DIP; DIP-60903N; -.
DR IntAct; P36871; 34.
DR STRING; 9606.ENSP00000360124; -.
DR DrugBank; DB02835; Alpha-D-Glucose 1,6-Bisphosphate.
DR DrugBank; DB04397; Alpha-D-Glucose-1-Phosphate-6-Vanadate.
DR DrugBank; DB06773; Human calcitonin.
DR GlyGen; P36871; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P36871; -.
DR MetOSite; P36871; -.
DR PhosphoSitePlus; P36871; -.
DR SwissPalm; P36871; -.
DR BioMuta; PGM1; -.
DR DMDM; 585670; -.
DR REPRODUCTION-2DPAGE; P36871; -.
DR CPTAC; CPTAC-255; -.
DR CPTAC; CPTAC-256; -.
DR CPTAC; CPTAC-988; -.
DR EPD; P36871; -.
DR jPOST; P36871; -.
DR MassIVE; P36871; -.
DR MaxQB; P36871; -.
DR PeptideAtlas; P36871; -.
DR PRIDE; P36871; -.
DR ProteomicsDB; 4816; -.
DR ProteomicsDB; 55222; -. [P36871-1]
DR ProteomicsDB; 55223; -. [P36871-2]
DR TopDownProteomics; P36871-1; -. [P36871-1]
DR Antibodypedia; 3314; 245 antibodies from 26 providers.
DR DNASU; 5236; -.
DR Ensembl; ENST00000371083.4; ENSP00000360124.4; ENSG00000079739.17. [P36871-2]
DR Ensembl; ENST00000371084.8; ENSP00000360125.3; ENSG00000079739.17. [P36871-1]
DR Ensembl; ENST00000540265.5; ENSP00000443449.1; ENSG00000079739.17. [P36871-3]
DR GeneID; 5236; -.
DR KEGG; hsa:5236; -.
DR MANE-Select; ENST00000371084.8; ENSP00000360125.3; NM_002633.3; NP_002624.2.
DR UCSC; uc001dbh.5; human. [P36871-1]
DR CTD; 5236; -.
DR DisGeNET; 5236; -.
DR GeneCards; PGM1; -.
DR GeneReviews; PGM1; -.
DR HGNC; HGNC:8905; PGM1.
DR HPA; ENSG00000079739; Group enriched (skeletal muscle, tongue).
DR MalaCards; PGM1; -.
DR MIM; 171900; gene.
DR MIM; 614921; phenotype.
DR neXtProt; NX_P36871; -.
DR OpenTargets; ENSG00000079739; -.
DR Orphanet; 319646; PGM1-CDG.
DR PharmGKB; PA33242; -.
DR VEuPathDB; HostDB:ENSG00000079739; -.
DR eggNOG; KOG0625; Eukaryota.
DR GeneTree; ENSGT00940000155542; -.
DR HOGENOM; CLU_009330_0_1_1; -.
DR InParanoid; P36871; -.
DR OMA; DTRFMSE; -.
DR OrthoDB; 446752at2759; -.
DR PhylomeDB; P36871; -.
DR TreeFam; TF300350; -.
DR BioCyc; MetaCyc:HS01335-MON; -.
DR BRENDA; 5.4.2.2; 2681.
DR PathwayCommons; P36871; -.
DR Reactome; R-HSA-3322077; Glycogen synthesis.
DR Reactome; R-HSA-5609974; Defective PGM1 causes PGM1-CDG.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SABIO-RK; P36871; -.
DR SignaLink; P36871; -.
DR SIGNOR; P36871; -.
DR BioGRID-ORCS; 5236; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; PGM1; human.
DR GeneWiki; PGM1; -.
DR GenomeRNAi; 5236; -.
DR Pharos; P36871; Tbio.
DR PRO; PR:P36871; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P36871; protein.
DR Bgee; ENSG00000079739; Expressed in skeletal muscle tissue of rectus abdominis and 211 other tissues.
DR ExpressionAtlas; P36871; baseline and differential.
DR Genevisible; P36871; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004614; F:phosphoglucomutase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; TAS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; TAS:UniProtKB.
DR DisProt; DP02748; -.
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 PANTHER; PTHR22573; PTHR22573; 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; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism;
KW Congenital disorder of glycosylation; Cytoplasm; Disease variant;
KW Glucose metabolism; Glycogen storage disease; Isomerase; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..562
FT /note="Phosphoglucomutase-1"
FT /id="PRO_0000147776"
FT ACT_SITE 117
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000269|PubMed:25288802"
FT BINDING 23
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 117
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate groupe"
FT /evidence="ECO:0000269|PubMed:25288802"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:26972339,
FT ECO:0007744|PDB:5EPC, ECO:0007744|PDB:5F9C"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:26972339,
FT ECO:0007744|PDB:5EPC, ECO:0007744|PDB:5F9C"
FT BINDING 292
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:26972339,
FT ECO:0007744|PDB:5EPC, ECO:0007744|PDB:5F9C"
FT BINDING 293
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 357
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 376
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 378
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 389
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
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:25288802,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38652"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
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:0007744|PubMed:24275569"
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:0000269|PubMed:15378030"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38652"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38652"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 507
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0F9"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38652"
FT VAR_SEQ 1..197
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045204"
FT VAR_SEQ 1..77
FT /note="MVKIVTVKTQAYQDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVEPAQR
FT QEATLVVGGDGRFYMKEAIQLIARI -> MSDFEEWISGTYRKMEEGPLPLLTFATAPY
FT HDQKPGTSGLRKKTYYFEEKPCYLENFIQSIFFSIDLKDRQGSSLVVGGDGRYFNKSAI
FT ETIVQM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004686"
FT VARIANT 19
FT /note="T -> A (in CDG1T; reduces strongly
FT phosphoglucomutase activity; dbSNP:rs1320810473)"
FT /evidence="ECO:0000269|PubMed:24499211,
FT ECO:0000269|PubMed:25288802"
FT /id="VAR_071635"
FT VARIANT 38
FT /note="N -> Y (in CDG1T; reduces strongly solubility;
FT increases aggregation; dbSNP:rs587777402)"
FT /evidence="ECO:0000269|PubMed:24499211,
FT ECO:0000269|PubMed:25288802"
FT /id="VAR_071636"
FT VARIANT 41
FT /note="Q -> R (in CDG1T; reduces solubility; increases
FT aggregation; dbSNP:rs1300651770)"
FT /evidence="ECO:0000269|PubMed:24499211,
FT ECO:0000269|PubMed:25288802"
FT /id="VAR_071637"
FT VARIANT 62
FT /note="D -> H (in CDG1T; reduces solubility; reduces
FT strongly phosphoglucomutase activity; dbSNP:rs587777403)"
FT /evidence="ECO:0000269|PubMed:24499211,
FT ECO:0000269|PubMed:25288802"
FT /id="VAR_071638"
FT VARIANT 68
FT /note="K -> M (in allele PGM1*7+, allele PGM1*7-, allele
FT PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is
FT similar to wild-type; dbSNP:rs200390982)"
FT /evidence="ECO:0000269|PubMed:25288802,
FT ECO:0000269|PubMed:7902567"
FT /id="VAR_006090"
FT VARIANT 88
FT /note="I -> V (in dbSNP:rs855314)"
FT /id="VAR_050496"
FT VARIANT 115
FT /note="T -> A (in CDG1T; reduces mildly phosphoglucomutase
FT activity; dbSNP:rs121918371)"
FT /evidence="ECO:0000269|PubMed:19625727,
FT ECO:0000269|PubMed:24499211, ECO:0000269|PubMed:25288802"
FT /id="VAR_062280"
FT VARIANT 121
FT /note="G -> R (in CDG1T; there is 7% enzyme residual
FT phosphoglucomutase activity; dbSNP:rs398122912)"
FT /evidence="ECO:0000269|PubMed:22492991,
FT ECO:0000269|PubMed:24499211, ECO:0000269|PubMed:25288802"
FT /id="VAR_069219"
FT VARIANT 221
FT /note="R -> C (in allele PGM1*2+, allele PGM1*2-, allele
FT PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is
FT similar to wild-type; dbSNP:rs1126728)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:25288802, ECO:0000269|PubMed:7902567,
FT ECO:0000269|PubMed:7902568, ECO:0000269|Ref.2"
FT /id="VAR_006091"
FT VARIANT 263
FT /note="D -> G (in CDG1T; reduces strongly
FT phosphoglucomutase activity; dbSNP:rs1465877146)"
FT /evidence="ECO:0000269|PubMed:24499211,
FT ECO:0000269|PubMed:25288802"
FT /id="VAR_071639"
FT VARIANT 263
FT /note="D -> Y (in CDG1T; reduces strongly
FT phosphoglucomutase activity; dbSNP:rs587777404)"
FT /evidence="ECO:0000269|PubMed:24499211,
FT ECO:0000269|PubMed:25288802"
FT /id="VAR_071640"
FT VARIANT 291
FT /note="G -> R (in CDG1T; reduces strongly
FT phosphoglucomutase activity; dbSNP:rs772768778)"
FT /evidence="ECO:0000269|PubMed:22976764,
FT ECO:0000269|PubMed:24499211, ECO:0000269|PubMed:25288802"
FT /id="VAR_071641"
FT VARIANT 330
FT /note="G -> R (in CDG1T; decreases mildly solubility;
FT dbSNP:rs777164338)"
FT /evidence="ECO:0000269|PubMed:24499211,
FT ECO:0000269|PubMed:25288802"
FT /id="VAR_071642"
FT VARIANT 377
FT /note="E -> K (in CDG1T; decreases strongly solubility)"
FT /evidence="ECO:0000269|PubMed:24499211,
FT ECO:0000269|PubMed:25288802"
FT /id="VAR_071643"
FT VARIANT 388
FT /note="E -> K (in CDG1T; decreases strongly solubility;
FT dbSNP:rs1301021797)"
FT /evidence="ECO:0000269|PubMed:24499211,
FT ECO:0000269|PubMed:25288802"
FT /id="VAR_071644"
FT VARIANT 420
FT /note="Y -> H (in allele PGM1*1-, allele PGM1*2-, allele
FT PGM1*3- and allele PGM1*7-; phosphoglucomutase activity is
FT similar to wild-type; dbSNP:rs11208257)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:25288802,
FT ECO:0000269|PubMed:7902567, ECO:0000269|PubMed:7902568,
FT ECO:0000269|Ref.2"
FT /id="VAR_006092"
FT VARIANT 501
FT /note="V -> I (in dbSNP:rs6676290)"
FT /id="VAR_034380"
FT VARIANT 516
FT /note="L -> P (in CDG1T; decreases strongly solubility;
FT dbSNP:rs587777401)"
FT /evidence="ECO:0000269|PubMed:24499211,
FT ECO:0000269|PubMed:25288802"
FT /id="VAR_071645"
FT CONFLICT 134
FT /note="S -> C (in Ref. 5; AAH67763)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:5JN5"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5HSH"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5JN5"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6UIQ"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5F9C"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:5JN5"
FT TURN 237..241
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:5JN5"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:5HSH"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:5JN5"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 391..405
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 422..433
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 435..450
FT /evidence="ECO:0007829|PDB:5JN5"
FT TURN 452..456
FT /evidence="ECO:0007829|PDB:6SNO"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 465..473
FT /evidence="ECO:0007829|PDB:5JN5"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:5JN5"
FT TURN 506..509
FT /evidence="ECO:0007829|PDB:5VIN"
FT STRAND 512..522
FT /evidence="ECO:0007829|PDB:5JN5"
FT TURN 525..529
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 532..547
FT /evidence="ECO:0007829|PDB:5JN5"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:5JN5"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:5JN5"
FT MOD_RES P36871-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:21406692"
SQ SEQUENCE 562 AA; 61449 MW; 61A26C19107D467A CRC64;
MVKIVTVKTQ AYQDQKPGTS GLRKRVKVFQ SSANYAENFI QSIISTVEPA QRQEATLVVG
GDGRFYMKEA IQLIARIAAA NGIGRLVIGQ NGILSTPAVS CIIRKIKAIG GIILTASHNP
GGPNGDFGIK FNISNGGPAP EAITDKIFQI SKTIEEYAVC PDLKVDLGVL GKQQFDLENK
FKPFTVEIVD SVEAYATMLR SIFDFSALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE
LGAPANSAVN CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH
GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVASATKI ALYETPTGWK
FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS ILATRKQSVE DILKDHWQKY
GRNFFTRYDY EEVEAEGANK MMKDLEALMF DRSFVGKQFS ANDKVYTVEK ADNFEYSDPV
DGSISRNQGL RLIFTDGSRI VFRLSGTGSA GATIRLYIDS YEKDVAKINQ DPQVMLAPLI
SIALKVSQLQ ERTGRTAPTV IT
