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Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase 1) (Glutamine:fructose-6-phosphate amidotransferase 1) (GFAT 1) (GFAT1) (Hexosephosphate aminotransferase 1)

 GFPT1_HUMAN             Reviewed;         699 AA.
Q06210; Q53QE6; Q9BXF8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 175.
RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1;
EC=2.6.1.16 {ECO:0000250|UniProtKB:P82808};
AltName: Full=D-fructose-6-phosphate amidotransferase 1;
AltName: Full=Glutamine:fructose-6-phosphate amidotransferase 1;
Short=GFAT 1;
Short=GFAT1;
AltName: Full=Hexosephosphate aminotransferase 1;
Name=GFPT1; Synonyms=GFAT, GFPT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1460020;
McKnight G.L., Mudri S.L., Mathewes S.L., Traxinger R.R., Marshall S.,
Sheppard P.O., O'Hara P.J.;
"Molecular cloning, cDNA sequence, and bacterial expression of human
glutamine:fructose-6-phosphate amidotransferase.";
J. Biol. Chem. 267:25208-25212(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 124-275 (ISOFORM 1), AND TISSUE
SPECIFICITY.
PubMed=11679416; DOI=10.2337/diabetes.50.11.2419;
DeHaven J.E., Robinson K.A., Nelson B.A., Buse M.G.;
"A novel variant of glutamine:fructose-6-phosphate amidotransferase-1
(GFAT1) mRNA is selectively expressed in striated muscle.";
Diabetes 50:2419-2424(2001).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-261, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17] {ECO:0000244|PDB:2ZJ3, ECO:0000244|PDB:2ZJ4}
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 332-699, SUBUNIT, AND
SUBSTRATE-BINDING SITES.
PubMed=19059404; DOI=10.1016/j.febslet.2008.11.041;
Nakaishi Y., Bando M., Shimizu H., Watanabe K., Goto F., Tsuge H.,
Kondo K., Komatsu M.;
"Structural analysis of human glutamine:fructose-6-phosphate
amidotransferase, a key regulator in type 2 diabetes.";
FEBS Lett. 583:163-167(2009).
[18]
VARIANTS CMS12 ALA-15; MET-15; VAL-43; CYS-111; THR-121; PHE-199;
TYR-366; HIS-403; HIS-452; THR-509; THR-510; TRP-514 AND TRP-530.
PubMed=21310273; DOI=10.1016/j.ajhg.2011.01.008;
Senderek J., Muller J.S., Dusl M., Strom T.M., Guergueltcheva V.,
Diepolder I., Laval S.H., Maxwell S., Cossins J., Krause S.,
Muelas N., Vilchez J.J., Colomer J., Mallebrera C.J., Nascimento A.,
Nafissi S., Kariminejad A., Nilipour Y., Bozorgmehr B., Najmabadi H.,
Rodolico C., Sieb J.P., Steinlein O.K., Schlotter B., Schoser B.,
Kirschner J., Herrmann R., Voit T., Oldfors A., Lindbergh C.,
Urtizberea A., von der Hagen M., Hubner A., Palace J., Bushby K.,
Straub V., Beeson D., Abicht A., Lochmuller H.;
"Hexosamine biosynthetic pathway mutations cause neuromuscular
transmission defect.";
Am. J. Hum. Genet. 88:162-172(2011).
-!- FUNCTION: Controls the flux of glucose into the hexosamine
pathway. Most likely involved in regulating the availability of
precursors for N- and O-linked glycosylation of proteins.
Regulates the circadian expression of clock genes ARNTL/BMAL1 and
CRY1.
-!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L-
glutamate + D-glucosamine 6-phosphate.
{ECO:0000250|UniProtKB:P82808}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
fructose 6-phosphate: step 1/1. {ECO:0000250|UniProtKB:P82808}.
-!- SUBUNIT: Homotetramer (Probable), may also exist as homodimers.
{ECO:0000269|PubMed:19059404}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=GFAT1m;
IsoId=Q06210-1; Sequence=Displayed;
Name=2;
IsoId=Q06210-2; Sequence=VSP_007497;
-!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in
skeletal muscle. Not expressed in brain. Seems to be selectively
expressed in striated muscle. {ECO:0000269|PubMed:11679416}.
-!- DISEASE: Myasthenic syndrome, congenital, 12 (CMS12) [MIM:610542]:
A form of congenital myasthenic syndrome, a group of disorders
characterized by failure of neuromuscular transmission, including
pre-synaptic, synaptic, and post-synaptic disorders that are not
of autoimmune origin. Clinical features are easy fatigability and
muscle weakness. CMS12 is characterized by onset of proximal
muscle weakness in the first decade. Individuals with this
condition have a recognizable pattern of weakness of shoulder and
pelvic girdle muscles, and sparing of ocular or facial muscles.
EMG classically shows a decremental response to repeated nerve
stimulation, a sign of neuromuscular junction dysfunction.
Affected individuals show a favorable response to
acetylcholinesterase (AChE) inhibitors.
{ECO:0000269|PubMed:21310273}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
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EMBL; M90516; AAA58502.1; -; mRNA.
EMBL; AC114772; AAY14827.1; -; Genomic_DNA.
EMBL; BC045641; AAH45641.1; -; mRNA.
EMBL; AF334737; AAK15342.1; -; mRNA.
CCDS; CCDS33216.1; -. [Q06210-2]
CCDS; CCDS58713.1; -. [Q06210-1]
PIR; A45055; A45055.
RefSeq; NP_001231639.1; NM_001244710.1. [Q06210-1]
RefSeq; NP_002047.2; NM_002056.3. [Q06210-2]
UniGene; Hs.580300; -.
PDB; 2V4M; X-ray; 2.29 A; A/B/C/D=332-699.
PDB; 2ZJ3; X-ray; 1.90 A; A=332-699.
PDB; 2ZJ4; X-ray; 2.20 A; A=332-699.
PDBsum; 2V4M; -.
PDBsum; 2ZJ3; -.
PDBsum; 2ZJ4; -.
ProteinModelPortal; Q06210; -.
SMR; Q06210; -.
BioGrid; 108941; 58.
IntAct; Q06210; 13.
MINT; MINT-5001216; -.
STRING; 9606.ENSP00000354347; -.
BindingDB; Q06210; -.
ChEMBL; CHEMBL1909481; -.
MEROPS; C44.970; -.
iPTMnet; Q06210; -.
PhosphoSitePlus; Q06210; -.
SwissPalm; Q06210; -.
BioMuta; GFPT1; -.
DMDM; 30923274; -.
EPD; Q06210; -.
MaxQB; Q06210; -.
PaxDb; Q06210; -.
PeptideAtlas; Q06210; -.
PRIDE; Q06210; -.
Ensembl; ENST00000357308; ENSP00000349860; ENSG00000198380. [Q06210-1]
Ensembl; ENST00000361060; ENSP00000354347; ENSG00000198380. [Q06210-2]
GeneID; 2673; -.
KEGG; hsa:2673; -.
UCSC; uc002sfh.4; human. [Q06210-1]
CTD; 2673; -.
DisGeNET; 2673; -.
EuPathDB; HostDB:ENSG00000198380.12; -.
GeneCards; GFPT1; -.
GeneReviews; GFPT1; -.
HGNC; HGNC:4241; GFPT1.
HPA; HPA047240; -.
MalaCards; GFPT1; -.
MIM; 138292; gene.
MIM; 610542; phenotype.
neXtProt; NX_Q06210; -.
OpenTargets; ENSG00000198380; -.
Orphanet; 353327; Congenital myasthenic syndromes with glycosylation defect.
PharmGKB; PA28651; -.
eggNOG; KOG1268; Eukaryota.
eggNOG; COG0449; LUCA.
GeneTree; ENSGT00390000010049; -.
HOGENOM; HOG000258898; -.
HOVERGEN; HBG051724; -.
InParanoid; Q06210; -.
KO; K00820; -.
OMA; ASEYRYA; -.
OrthoDB; EOG091G02N5; -.
PhylomeDB; Q06210; -.
TreeFam; TF300864; -.
BioCyc; MetaCyc:HS09974-MONOMER; -.
BRENDA; 2.6.1.16; 2681.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
Reactome; R-HSA-446210; Synthesis of UDP-N-acetyl-glucosamine.
SIGNOR; Q06210; -.
UniPathway; UPA00113; UER00528.
ChiTaRS; GFPT1; human.
EvolutionaryTrace; Q06210; -.
GeneWiki; GFPT1; -.
GenomeRNAi; 2673; -.
PRO; PR:Q06210; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000198380; -.
CleanEx; HS_GFPT1; -.
Genevisible; Q06210; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0006112; P:energy reserve metabolic process; TAS:ProtInc.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; TAS:ProtInc.
GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; TAS:Reactome.
GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
CDD; cd05008; SIS_GlmS_GlmD_1; 1.
CDD; cd05009; SIS_GlmS_GlmD_2; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR017932; GATase_2_dom.
InterPro; IPR035466; GlmS/AgaS_SIS.
InterPro; IPR035490; GlmS/FrlB_SIS.
InterPro; IPR005855; GlmS_trans.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR001347; SIS.
Pfam; PF01380; SIS; 2.
SUPFAM; SSF56235; SSF56235; 2.
TIGRFAMs; TIGR01135; glmS; 1.
PROSITE; PS51278; GATASE_TYPE_2; 1.
PROSITE; PS51464; SIS; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Aminotransferase;
Biological rhythms; Complete proteome; Congenital myasthenic syndrome;
Disease mutation; Glutamine amidotransferase; Phosphoprotein;
Reference proteome; Repeat; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 699 Glutamine--fructose-6-phosphate
aminotransferase [isomerizing] 1.
/FTId=PRO_0000135280.
DOMAIN 2 305 Glutamine amidotransferase type-2.
{ECO:0000255|PROSITE-ProRule:PRU00609}.
DOMAIN 377 516 SIS 1. {ECO:0000255|PROSITE-
ProRule:PRU00797}.
DOMAIN 548 689 SIS 2. {ECO:0000255|PROSITE-
ProRule:PRU00797}.
REGION 313 680 Isomerase.
REGION 394 395 Substrate-binding. {ECO:0000244|PDB:2V4M,
ECO:0000244|PDB:2ZJ3,
ECO:0000244|PDB:2ZJ4,
ECO:0000269|PubMed:19059404}.
REGION 439 441 Substrate-binding. {ECO:0000244|PDB:2V4M,
ECO:0000244|PDB:2ZJ3,
ECO:0000244|PDB:2ZJ4,
ECO:0000269|PubMed:19059404}.
ACT_SITE 2 2 For GATase activity.
{ECO:0000250|UniProtKB:P14742}.
BINDING 444 444 Substrate. {ECO:0000244|PDB:2V4M,
ECO:0000244|PDB:2ZJ3,
ECO:0000244|PDB:2ZJ4,
ECO:0000269|PubMed:19059404}.
BINDING 595 595 Substrate. {ECO:0000244|PDB:2V4M,
ECO:0000244|PDB:2ZJ3,
ECO:0000244|PDB:2ZJ4,
ECO:0000269|PubMed:19059404}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 229 246 Missing (in isoform 2).
{ECO:0000303|PubMed:1460020,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007497.
VARIANT 15 15 T -> A (in CMS12; dbSNP:rs387906638).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065339.
VARIANT 15 15 T -> M (in CMS12; dbSNP:rs751097758).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065340.
VARIANT 43 43 D -> V (in CMS12).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065341.
VARIANT 111 111 R -> C (in CMS12; dbSNP:rs201322234).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065342.
VARIANT 121 121 I -> T (in CMS12; dbSNP:rs753866967).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065343.
VARIANT 199 199 V -> F (in CMS12).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065344.
VARIANT 366 366 D -> Y (in CMS12).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065345.
VARIANT 403 403 R -> H (in CMS12).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065346.
VARIANT 452 452 R -> H (in CMS12).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065347.
VARIANT 509 509 M -> T (in CMS12).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065348.
VARIANT 510 510 M -> T (in CMS12).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065349.
VARIANT 514 514 R -> W (in CMS12).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065350.
VARIANT 530 530 R -> W (in CMS12).
{ECO:0000269|PubMed:21310273}.
/FTId=VAR_065351.
STRAND 339 341 {ECO:0000244|PDB:2ZJ3}.
HELIX 342 348 {ECO:0000244|PDB:2ZJ3}.
HELIX 350 358 {ECO:0000244|PDB:2ZJ3}.
TURN 359 361 {ECO:0000244|PDB:2ZJ3}.
TURN 364 367 {ECO:0000244|PDB:2ZJ3}.
HELIX 372 374 {ECO:0000244|PDB:2ZJ3}.
TURN 375 377 {ECO:0000244|PDB:2ZJ3}.
HELIX 378 383 {ECO:0000244|PDB:2ZJ3}.
STRAND 385 391 {ECO:0000244|PDB:2ZJ3}.
HELIX 393 410 {ECO:0000244|PDB:2ZJ3}.
STRAND 414 418 {ECO:0000244|PDB:2ZJ3}.
HELIX 419 424 {ECO:0000244|PDB:2ZJ3}.
STRAND 433 442 {ECO:0000244|PDB:2ZJ3}.
HELIX 445 456 {ECO:0000244|PDB:2ZJ3}.
STRAND 460 466 {ECO:0000244|PDB:2ZJ3}.
HELIX 471 475 {ECO:0000244|PDB:2ZJ3}.
STRAND 476 481 {ECO:0000244|PDB:2ZJ3}.
STRAND 489 491 {ECO:0000244|PDB:2ZJ4}.
HELIX 494 510 {ECO:0000244|PDB:2ZJ3}.
TURN 511 513 {ECO:0000244|PDB:2ZJ3}.
HELIX 515 517 {ECO:0000244|PDB:2ZJ3}.
HELIX 518 539 {ECO:0000244|PDB:2ZJ3}.
HELIX 542 552 {ECO:0000244|PDB:2ZJ3}.
STRAND 556 562 {ECO:0000244|PDB:2ZJ3}.
HELIX 564 566 {ECO:0000244|PDB:2ZJ3}.
HELIX 567 581 {ECO:0000244|PDB:2ZJ3}.
STRAND 584 589 {ECO:0000244|PDB:2ZJ3}.
HELIX 590 595 {ECO:0000244|PDB:2ZJ3}.
HELIX 597 600 {ECO:0000244|PDB:2ZJ3}.
STRAND 602 605 {ECO:0000244|PDB:2V4M}.
STRAND 607 611 {ECO:0000244|PDB:2ZJ3}.
HELIX 617 629 {ECO:0000244|PDB:2ZJ3}.
STRAND 635 639 {ECO:0000244|PDB:2ZJ3}.
HELIX 643 648 {ECO:0000244|PDB:2ZJ3}.
STRAND 650 655 {ECO:0000244|PDB:2ZJ3}.
TURN 660 662 {ECO:0000244|PDB:2ZJ3}.
HELIX 663 667 {ECO:0000244|PDB:2ZJ3}.
HELIX 669 681 {ECO:0000244|PDB:2ZJ3}.
STRAND 686 688 {ECO:0000244|PDB:2ZJ3}.
SEQUENCE 699 AA; 78806 MW; F0533A7B762C7B98 CRC64;
MCGIFAYLNY HVPRTRREIL ETLIKGLQRL EYRGYDSAGV GFDGGNDKDW EANACKIQLI
KKKGKVKALD EEVHKQQDMD LDIEFDVHLG IAHTRWATHG EPSPVNSHPQ RSDKNNEFIV
IHNGIITNYK DLKKFLESKG YDFESETDTE TIAKLVKYMY DNRESQDTSF TTLVERVIQQ
LEGAFALVFK SVHFPGQAVG TRRGSPLLIG VRSEHKLSTD HIPILYRTAR TQIGSKFTRW
GSQGERGKDK KGSCNLSRVD STTCLFPVEE KAVEYYFASD ASAVIEHTNR VIFLEDDDVA
AVVDGRLSIH RIKRTAGDHP GRAVQTLQME LQQIMKGNFS SFMQKEIFEQ PESVVNTMRG
RVNFDDYTVN LGGLKDHIKE IQRCRRLILI ACGTSYHAGV ATRQVLEELT ELPVMVELAS
DFLDRNTPVF RDDVCFFLSQ SGETADTLMG LRYCKERGAL TVGITNTVGS SISRETDCGV
HINAGPEIGV ASTKAYTSQF VSLVMFALMM CDDRISMQER RKEIMLGLKR LPDLIKEVLS
MDDEIQKLAT ELYHQKSVLI MGRGYHYATC LEGALKIKEI TYMHSEGILA GELKHGPLAL
VDKLMPVIMI IMRDHTYAKC QNALQQVVAR QGRPVVICDK EDTETIKNTK RTIKVPHSVD
CLQGILSVIP LQLLAFHLAV LRGYDVDFPR NLAKSVTVE


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