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Glycine betaine transporter BetP (Glycine betaine permease)

 BETP_CORGL              Reviewed;         595 AA.
P54582;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
23-MAY-2018, entry version 119.
RecName: Full=Glycine betaine transporter BetP {ECO:0000305};
AltName: Full=Glycine betaine permease {ECO:0000303|PubMed:8752342};
Name=betP {ECO:0000303|PubMed:8752342};
OrderedLocusNames=Cgl0892, cg1016;
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
LMG 3730 / NCIMB 10025).
Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
Corynebacterium.
NCBI_TaxID=196627;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=8752342;
Peter H., Burkovski A., Kraemer R.;
"Isolation, characterization, and expression of the Corynebacterium
glutamicum betP gene, encoding the transport system for the compatible
solute glycine betaine.";
J. Bacteriol. 178:5229-5234(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
Ikeda M., Nakagawa S.;
"The Corynebacterium glutamicum genome: features and impacts on
biotechnological processes.";
Appl. Microbiol. Biotechnol. 62:99-109(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
Tauch A.;
"The complete Corynebacterium glutamicum ATCC 13032 genome sequence
and its impact on the production of L-aspartate-derived amino acids
and vitamins.";
J. Biotechnol. 104:5-25(2003).
[4]
FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
INDUCTION.
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=7642496;
Farwick M., Siewe R.M., Kraemer R.;
"Glycine betaine uptake after hyperosmotic shift in Corynebacterium
glutamicum.";
J. Bacteriol. 177:4690-4695(1995).
[5]
FUNCTION, ENZYME REGULATION, AND DOMAIN.
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=9446558;
Peter H., Burkovski A., Kraemer R.;
"Osmo-sensing by N- and C-terminal extensions of the glycine betaine
uptake system BetP of Corynebacterium glutamicum.";
J. Biol. Chem. 273:2567-2574(1998).
[6]
FUNCTION, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10625602;
Ruebenhagen R., Roensch H., Jung H., Kraemer R., Morbach S.;
"Osmosensor and osmoregulator properties of the betaine carrier BetP
from Corynebacterium glutamicum in proteoliposomes.";
J. Biol. Chem. 275:735-741(2000).
[7]
FUNCTION, AND ENZYME REGULATION.
PubMed=11574473; DOI=10.1093/emboj/20.19.5412;
Ruebenhagen R., Morbach S., Kraemer R.;
"The osmoreactive betaine carrier BetP from Corynebacterium glutamicum
is a sensor for cytoplasmic K+.";
EMBO J. 20:5412-5420(2001).
[8]
FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
DOMAIN.
PubMed=15134432; DOI=10.1021/bi0359628;
Schiller D., Ruebenhagen R., Kraemer R., Morbach S.;
"The C-terminal domain of the betaine carrier BetP of Corynebacterium
glutamicum is directly involved in sensing K+ as an osmotic
stimulus.";
Biochemistry 43:5583-5591(2004).
[9]
ENZYME REGULATION.
PubMed=15063732; DOI=10.1016/S0014-5793(04)00279-0;
Schiller D., Kraemer R., Morbach S.;
"Cation specificity of osmosensing by the betaine carrier BetP of
Corynebacterium glutamicum.";
FEBS Lett. 563:108-112(2004).
[10]
SUBUNIT.
PubMed=15046983; DOI=10.1016/j.jmb.2004.02.026;
Ziegler C., Morbach S., Schiller D., Kraemer R., Tziatzios C.,
Schubert D., Kuehlbrandt W.;
"Projection structure and oligomeric state of the osmoregulated
sodium/glycine betaine symporter BetP of Corynebacterium glutamicum.";
J. Mol. Biol. 337:1137-1147(2004).
[11]
ENZYME REGULATION.
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=15995189; DOI=10.1128/JB.187.14.4752-4759.2005;
Ozcan N., Kraemer R., Morbach S.;
"Chill activation of compatible solute transporters in Corynebacterium
glutamicum at the level of transport activity.";
J. Bacteriol. 187:4752-4759(2005).
[12]
INDUCTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=17390131; DOI=10.1007/s00253-007-0938-4;
Weinand M., Kraemer R., Morbach S.;
"Characterization of compatible solute transporter multiplicity in
Corynebacterium glutamicum.";
Appl. Microbiol. Biotechnol. 76:701-708(2007).
[13]
ENZYME REGULATION.
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=17693504; DOI=10.1128/JB.00986-07;
Ozcan N., Ejsing C.S., Shevchenko A., Lipski A., Morbach S.,
Kraemer R.;
"Osmolality, temperature, and membrane lipid composition modulate the
activity of betaine transporter BetP in Corynebacterium glutamicum.";
J. Bacteriol. 189:7485-7496(2007).
[14]
SUBUNIT, AND MUTAGENESIS OF TRP-101 AND THR-351.
PubMed=21681199; DOI=10.1038/embor.2011.102;
Perez C., Khafizov K., Forrest L.R., Kraemer R., Ziegler C.;
"The role of trimerization in the osmoregulated betaine transporter
BetP.";
EMBO Rep. 12:804-810(2011).
[15] {ECO:0000244|PDB:2WIT}
X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 30-595 IN COMPLEX WITH
GLYCINE BETAINE, FUNCTION, ENZYME REGULATION, SUBUNIT, SUBCELLULAR
LOCATION, TOPOLOGY, AND MUTAGENESIS OF GLU-135; TRP-189; TRP-194;
TYR-197; ARG-210; GLY-301; TRP-362; TRP-366; TRP-371; TRP-374;
TRP-377; ARG-387 AND ARG-392.
PubMed=19262666; DOI=10.1038/NATURE07819;
Ressl S., Terwisscha van Scheltinga A.C., Vonrhein C., Ott V.,
Ziegler C.;
"Molecular basis of transport and regulation in the Na(+)/betaine
symporter BetP.";
Nature 458:47-52(2009).
[16] {ECO:0000244|PDB:3P03}
X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 30-595 OF MUTANT ASP-153 IN
COMPLEX WITH CHOLINE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, SUBUNIT, TOPOLOGY, AND MUTAGENESIS OF GLY-149; GLY-151 AND
GLY-153.
PubMed=21364531; DOI=10.1038/emboj.2011.46;
Perez C., Koshy C., Ressl S., Nicklisch S., Kramer R., Ziegler C.;
"Substrate specificity and ion coupling in the Na+/betaine symporter
BetP.";
EMBO J. 30:1221-1229(2011).
[17] {ECO:0000244|PDB:4AIN, ECO:0000244|PDB:4DOJ}
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 41-579 IN COMPLEXES WITH
GLYCINE BETAINE AND CHOLINE, FUNCTION, SUBUNIT, TOPOLOGY, AND
MUTAGENESIS OF PHE-156; PHE-369; TRP-373; TRP-374; TRP-377; PHE-380
AND PHE-384.
PubMed=22940865; DOI=10.1038/nature11403;
Perez C., Koshy C., Yildiz O., Ziegler C.;
"Alternating-access mechanism in conformationally asymmetric trimers
of the betaine transporter BetP.";
Nature 490:126-130(2012).
[18] {ECO:0000244|PDB:4C7R}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 30-595, FUNCTION, ENZYME
REGULATION, SUBUNIT, TOPOLOGY, AND MUTAGENESIS OF GLY-149; MET-150;
ILE-152 AND GLY-153.
PubMed=24141878; DOI=10.1038/EMBOJ.2013.226;
Koshy C., Schweikhard E.S., Gartner R.M., Perez C., Yildiz O.,
Ziegler C.;
"Structural evidence for functional lipid interactions in the betaine
transporter BetP.";
EMBO J. 32:3096-3105(2013).
[19] {ECO:0000244|PDB:4LLH}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 30-595, SUBUNIT, TOPOLOGY,
AND MUTAGENESIS OF GLY-153 AND ASN-309.
PubMed=25023443; DOI=10.1038/ncomms5231;
Perez C., Faust B., Mehdipour A.R., Francesconi K.A., Forrest L.R.,
Ziegler C.;
"Substrate-bound outward-open state of the betaine transporter BetP
provides insights into Na+ coupling.";
Nat. Commun. 5:4231-4231(2014).
-!- FUNCTION: Involved in response to osmotic stress (PubMed:7642496,
PubMed:9446558, PubMed:10625602, PubMed:19262666, PubMed:21364531,
PubMed:24141878). High-affinity glycine betaine-specific uptake
system, which couples the uptake of glycine betaine to the symport
of two Na(+) ions (PubMed:7642496, PubMed:10625602,
PubMed:15134432, PubMed:19262666, PubMed:21364531,
PubMed:22940865, PubMed:24141878). Transport is driven both by the
Na(+) gradient and by the electrical potential (PubMed:7642496,
PubMed:10625602). In addition, functions both as an osmosensor and
as an osmoregulator that transduces signal to the catalytic part
of the carrier protein, which adapts its activity to the extent of
osmotic stress (PubMed:9446558, PubMed:10625602, PubMed:11574473).
{ECO:0000269|PubMed:10625602, ECO:0000269|PubMed:11574473,
ECO:0000269|PubMed:15134432, ECO:0000269|PubMed:19262666,
ECO:0000269|PubMed:21364531, ECO:0000269|PubMed:22940865,
ECO:0000269|PubMed:24141878, ECO:0000269|PubMed:7642496,
ECO:0000269|PubMed:9446558}.
-!- ENZYME REGULATION: Uptake is activated by hyperosmotic stress
(PubMed:7642496, PubMed:9446558, PubMed:10625602, PubMed:15134432,
PubMed:19262666, PubMed:21364531, PubMed:24141878). Osmoresponsive
activation is triggered by a change in the internal K(+)
concentration (PubMed:11574473, PubMed:15063732). In addition,
shows a pronounced chill stimulation, at temperatures around 10
degrees Celsius (PubMed:15995189, PubMed:17693504). Chill
activation may be influenced by the membrane lipid composition
(PubMed:17693504). Uptake is completely abolished by the uncoupler
CCCP, and to a different extent by the ionophores valinomycin and
nigericin (PubMed:7642496). {ECO:0000269|PubMed:10625602,
ECO:0000269|PubMed:11574473, ECO:0000269|PubMed:15063732,
ECO:0000269|PubMed:15134432, ECO:0000269|PubMed:15995189,
ECO:0000269|PubMed:17693504, ECO:0000269|PubMed:19262666,
ECO:0000269|PubMed:21364531, ECO:0000269|PubMed:24141878,
ECO:0000269|PubMed:7642496, ECO:0000269|PubMed:9446558}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8.6 uM for glycine betaine {ECO:0000269|PubMed:7642496};
KM=3.6 uM for glycine betaine {ECO:0000269|PubMed:10625602};
KM=3.5 uM for glycine betaine {ECO:0000269|PubMed:21364531};
KM=3 uM for glycine betaine {ECO:0000269|PubMed:15134432};
KM=4.1 mM for Na(+) {ECO:0000269|PubMed:7642496};
KM=15 mM for Na(+) {ECO:0000269|PubMed:10625602};
KM=38.1 mM for Na(+) {ECO:0000269|PubMed:15134432};
Vmax=110 nmol/min/mg enzyme {ECO:0000269|PubMed:7642496};
Vmax=2.3 mmol/min/mg enzyme {ECO:0000269|PubMed:10625602};
Vmax=2264 nmol/min/mg enzyme {ECO:0000269|PubMed:21364531};
Vmax=1693 nmol/min/mg enzyme {ECO:0000269|PubMed:15134432};
pH dependence:
Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:7642496};
-!- SUBUNIT: Homotrimer (PubMed:15046983, PubMed:21681199,
PubMed:19262666, PubMed:21364531, PubMed:22940865,
PubMed:24141878, PubMed:25023443). The monomer can accumulate
glycine betaine, but trimerization is required to properly respond
to osmotic stress (PubMed:21681199). {ECO:0000269|PubMed:15046983,
ECO:0000269|PubMed:19262666, ECO:0000269|PubMed:21364531,
ECO:0000269|PubMed:21681199, ECO:0000269|PubMed:22940865,
ECO:0000269|PubMed:24141878, ECO:0000269|PubMed:25023443}.
-!- INTERACTION:
Self; NbExp=14; IntAct=EBI-6985171, EBI-6985171;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:17390131, ECO:0000269|PubMed:19262666}; Multi-
pass membrane protein {ECO:0000269|PubMed:19262666,
ECO:0000269|PubMed:21364531, ECO:0000269|PubMed:22940865,
ECO:0000269|PubMed:24141878, ECO:0000269|PubMed:25023443}.
-!- INDUCTION: Constitutively expressed at a basal level of activity
(PubMed:7642496). Induced upon hyperosmotic conditions, resulting
in an increase of its transport activity (PubMed:7642496,
PubMed:17390131). {ECO:0000269|PubMed:17390131,
ECO:0000269|PubMed:7642496}.
-!- DOMAIN: Contains a negatively charged N-terminus and a positively
charged C-terminus, which are both involved in sensing and/or
transducing osmotic changes to the domain responsible for the
translocation of the substrate glycine betaine (PubMed:9446558).
The C-terminal domain is directly involved in K(+) sensing or
K(+)-dependent activation of BetP (PubMed:15134432).
{ECO:0000269|PubMed:15134432, ECO:0000269|PubMed:9446558}.
-!- DISRUPTION PHENOTYPE: Mutant shows strongly decreased glycine
betaine uptake. {ECO:0000269|PubMed:8752342}.
-!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
{ECO:0000305}.
-!- CAUTION: Binds 2 Na(+), but the precise binding sites are still
uncertain and may change during the transport cycle.
{ECO:0000305|PubMed:19262666, ECO:0000305|PubMed:22940865,
ECO:0000305|PubMed:25023443}.
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EMBL; X93514; CAA63771.1; -; Genomic_DNA.
EMBL; BA000036; BAB98285.1; -; Genomic_DNA.
EMBL; BX927150; CAF19598.1; -; Genomic_DNA.
RefSeq; NP_600119.1; NC_003450.3.
PDB; 2WIT; X-ray; 3.35 A; A/B/C=30-595.
PDB; 3P03; X-ray; 3.35 A; A/B/C=30-595.
PDB; 4AIN; X-ray; 3.10 A; A/B/C=41-579.
PDB; 4C7R; X-ray; 2.70 A; A/B/C=30-595.
PDB; 4DOJ; X-ray; 3.25 A; A/B/C=30-595.
PDB; 4LLH; X-ray; 2.80 A; A/B/C=30-595.
PDBsum; 2WIT; -.
PDBsum; 3P03; -.
PDBsum; 4AIN; -.
PDBsum; 4C7R; -.
PDBsum; 4DOJ; -.
PDBsum; 4LLH; -.
ProteinModelPortal; P54582; -.
SMR; P54582; -.
DIP; DIP-59738N; -.
MINT; P54582; -.
STRING; 196627.cg1016; -.
TCDB; 2.A.15.1.10; the betaine/carnitine/choline transporter (bcct) family.
PRIDE; P54582; -.
EnsemblBacteria; BAB98285; BAB98285; BAB98285.
EnsemblBacteria; CAF19598; CAF19598; cg1016.
GeneID; 1018885; -.
KEGG; cgb:cg1016; -.
KEGG; cgl:NCgl0856; -.
PATRIC; fig|196627.13.peg.875; -.
eggNOG; ENOG4105C94; Bacteria.
eggNOG; COG1292; LUCA.
HOGENOM; HOG000053240; -.
OMA; VHAWAIY; -.
BioCyc; CORYNE:G18NG-10462-MONOMER; -.
EvolutionaryTrace; P54582; -.
Proteomes; UP000000582; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
GO; GO:0071705; P:nitrogen compound transport; IEA:InterPro.
InterPro; IPR018093; BCCT_CS.
InterPro; IPR000060; BCCT_transptr.
PANTHER; PTHR30047; PTHR30047; 1.
Pfam; PF02028; BCCT; 1.
TIGRFAMs; TIGR00842; bcct; 1.
PROSITE; PS01303; BCCT; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Membrane; Metal-binding; Reference proteome; Sodium; Stress response;
Symport; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 595 Glycine betaine transporter BetP.
/FTId=PRO_0000201483.
TOPO_DOM 1 59 Cytoplasmic.
{ECO:0000305|PubMed:9446558}.
TRANSMEM 60 80 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 81 98 Periplasmic. {ECO:0000305}.
TRANSMEM 99 119 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 120 137 Cytoplasmic. {ECO:0000305}.
TRANSMEM 138 158 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 159 185 Periplasmic. {ECO:0000305}.
TRANSMEM 186 206 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 207 236 Cytoplasmic. {ECO:0000305}.
TRANSMEM 237 257 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 258 276 Periplasmic. {ECO:0000305}.
TRANSMEM 277 296 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 297 299 Cytoplasmic. {ECO:0000305}.
TRANSMEM 300 323 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 324 365 Periplasmic. {ECO:0000305}.
TRANSMEM 366 386 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 387 396 Cytoplasmic. {ECO:0000305}.
TRANSMEM 397 417 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 418 451 Periplasmic. {ECO:0000305}.
TRANSMEM 452 476 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 477 489 Cytoplasmic. {ECO:0000305}.
TRANSMEM 490 510 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 511 520 Periplasmic. {ECO:0000305}.
TRANSMEM 521 541 Helical. {ECO:0000269|PubMed:24141878}.
TOPO_DOM 542 595 Cytoplasmic.
{ECO:0000305|PubMed:9446558}.
REGION 152 153 Glycine betaine binding.
{ECO:0000244|PDB:4AIN,
ECO:0000269|PubMed:22940865}.
REGION 373 377 Glycine betaine binding.
{ECO:0000244|PDB:4AIN,
ECO:0000269|PubMed:19262666,
ECO:0000269|PubMed:22940865}.
METAL 147 147 Sodium 1; via carbonyl oxygen.
{ECO:0000305|PubMed:19262666,
ECO:0000305|PubMed:22940865,
ECO:0000305|PubMed:25023443}.
METAL 148 148 Sodium 2; via carbonyl oxygen.
{ECO:0000305|PubMed:19262666}.
METAL 150 150 Sodium 2; via carbonyl oxygen.
{ECO:0000305|PubMed:19262666,
ECO:0000305|PubMed:22940865,
ECO:0000305|PubMed:25023443}.
METAL 306 306 Sodium 1. {ECO:0000305|PubMed:19262666}.
METAL 310 310 Sodium 1. {ECO:0000305|PubMed:19262666}.
BINDING 253 253 Glycine betaine. {ECO:0000244|PDB:4AIN,
ECO:0000269|PubMed:22940865}.
MUTAGEN 101 101 W->A: Mainly monomeric, shows a decrease
in activity and cannot be activated in
response to increased osmolality; when
associated with A-351.
{ECO:0000269|PubMed:21681199}.
MUTAGEN 135 135 E->A: Strongly decreased betaine
transport. {ECO:0000269|PubMed:19262666}.
MUTAGEN 149 149 G->A: Decreases betaine transport. No
effect on activation by increased
osmolality. {ECO:0000269|PubMed:21364531,
ECO:0000269|PubMed:24141878}.
MUTAGEN 150 150 M->F: No effect on activation by
increased osmolality; when associated
with A-152.
{ECO:0000269|PubMed:24141878}.
MUTAGEN 151 151 G->A: Nearly abolishes betaine transport.
{ECO:0000269|PubMed:21364531}.
MUTAGEN 152 152 I->A: No effect on activation by
increased osmolality; when associated
with F-150.
{ECO:0000269|PubMed:24141878}.
MUTAGEN 153 153 G->A: Decreases betaine transport and
alters activation at higher osmolality.
{ECO:0000269|PubMed:21364531,
ECO:0000269|PubMed:24141878}.
MUTAGEN 153 153 G->D: Changes substrate specificity,
giving rise to proton-coupled choline
transport. Decreases sodium-dependent
betaine transport.
{ECO:0000269|PubMed:21364531,
ECO:0000269|PubMed:25023443}.
MUTAGEN 156 156 F->A: Decreases betaine transport, but
has no major effect on affinity for
glycine betaine.
{ECO:0000269|PubMed:22940865}.
MUTAGEN 189 189 W->C: Mildly decreased betaine transport.
{ECO:0000269|PubMed:19262666}.
MUTAGEN 194 194 W->L: Strongly decreased betaine
transport. {ECO:0000269|PubMed:19262666}.
MUTAGEN 197 197 Y->L: Nearly abolishes betaine transport.
{ECO:0000269|PubMed:19262666}.
MUTAGEN 210 210 R->A: Nearly abolishes betaine transport.
{ECO:0000269|PubMed:19262666}.
MUTAGEN 301 301 G->L: Strongly decreased betaine
transport. {ECO:0000269|PubMed:19262666}.
MUTAGEN 309 309 N->A: Decreases affinity for sodium ions.
{ECO:0000269|PubMed:25023443}.
MUTAGEN 351 351 T->A: Mainly trimeric, but shows reduced
activity at high osmolalities. Mainly
monomeric, shows a decrease in activity
and cannot be activated in response to
increased osmolality; when associated
with A-101.
{ECO:0000269|PubMed:21681199}.
MUTAGEN 362 362 W->C: Strongly decreased betaine
transport. {ECO:0000269|PubMed:19262666}.
MUTAGEN 366 366 W->C: No effect on betaine transport.
{ECO:0000269|PubMed:19262666}.
MUTAGEN 369 369 F->G: Decreases affinity for glycine
betaine. Decreases betaine transport.
{ECO:0000269|PubMed:22940865}.
MUTAGEN 371 371 W->L: No effect on betaine transport.
{ECO:0000269|PubMed:19262666}.
MUTAGEN 373 373 W->A: Strongly decreases affinity for
glycine betaine and betaine transport.
{ECO:0000269|PubMed:22940865}.
MUTAGEN 374 374 W->A: Strongly decreases betaine
transport, but has no major effect on
affinity for glycine betaine.
{ECO:0000269|PubMed:22940865}.
MUTAGEN 374 374 W->L: No effect on betaine transport.
{ECO:0000269|PubMed:19262666}.
MUTAGEN 377 377 W->A: Abolishes betaine transport.
{ECO:0000269|PubMed:22940865}.
MUTAGEN 377 377 W->L: Nearly abolishes betaine transport.
{ECO:0000269|PubMed:19262666}.
MUTAGEN 380 380 F->A: Decreases betaine transport, but
has no effect on affinity for glycine
betaine. {ECO:0000269|PubMed:22940865}.
MUTAGEN 384 384 F->A: Decreases betaine transport, but
has no effect on affinity for glycine
betaine. {ECO:0000269|PubMed:22940865}.
MUTAGEN 387 387 R->A: Mildly decreased betaine transport.
{ECO:0000269|PubMed:19262666}.
MUTAGEN 392 392 R->K: Moderately decreased betaine
transport. {ECO:0000269|PubMed:19262666}.
HELIX 42 54 {ECO:0000244|PDB:4AIN}.
HELIX 60 79 {ECO:0000244|PDB:4C7R}.
HELIX 81 98 {ECO:0000244|PDB:4C7R}.
HELIX 100 119 {ECO:0000244|PDB:4C7R}.
HELIX 121 124 {ECO:0000244|PDB:4C7R}.
STRAND 126 129 {ECO:0000244|PDB:4C7R}.
HELIX 138 149 {ECO:0000244|PDB:4C7R}.
HELIX 152 168 {ECO:0000244|PDB:4C7R}.
HELIX 178 189 {ECO:0000244|PDB:4C7R}.
HELIX 191 209 {ECO:0000244|PDB:4C7R}.
HELIX 217 220 {ECO:0000244|PDB:4C7R}.
HELIX 222 225 {ECO:0000244|PDB:4C7R}.
HELIX 227 231 {ECO:0000244|PDB:4C7R}.
HELIX 233 265 {ECO:0000244|PDB:4C7R}.
TURN 266 269 {ECO:0000244|PDB:4C7R}.
HELIX 276 291 {ECO:0000244|PDB:4C7R}.
TURN 292 296 {ECO:0000244|PDB:4C7R}.
HELIX 298 323 {ECO:0000244|PDB:4C7R}.
HELIX 326 348 {ECO:0000244|PDB:4C7R}.
HELIX 354 357 {ECO:0000244|PDB:4C7R}.
HELIX 360 363 {ECO:0000244|PDB:4C7R}.
TURN 364 366 {ECO:0000244|PDB:4C7R}.
HELIX 367 376 {ECO:0000244|PDB:4C7R}.
HELIX 378 389 {ECO:0000244|PDB:4C7R}.
HELIX 394 425 {ECO:0000244|PDB:4C7R}.
TURN 432 434 {ECO:0000244|PDB:4C7R}.
HELIX 436 445 {ECO:0000244|PDB:4C7R}.
TURN 448 452 {ECO:0000244|PDB:4C7R}.
HELIX 453 478 {ECO:0000244|PDB:4C7R}.
TURN 479 483 {ECO:0000244|PDB:4C7R}.
HELIX 489 510 {ECO:0000244|PDB:4C7R}.
HELIX 511 513 {ECO:0000244|PDB:4C7R}.
HELIX 514 524 {ECO:0000244|PDB:4C7R}.
HELIX 527 545 {ECO:0000244|PDB:4C7R}.
HELIX 548 582 {ECO:0000244|PDB:4C7R}.
TURN 583 585 {ECO:0000244|PDB:4C7R}.
SEQUENCE 595 AA; 64209 MW; 8354B41C834CEFE2 CRC64;
MTTSDPNPKP IVEDAQPEQI TATEELAGLL ENPTNLEGKL ADAEEEIILE GEDTQASLNW
SVIVPALVIV LATVVWGIGF KDSFTNFASS ALSAVVDNLG WAFILFGTVF VFFIVVIAAS
KFGTIRLGRI DEAPEFRTVS WISMMFAAGM GIGLMFYGTT EPLTFYRNGV PGHDEHNVGV
AMSTTMFHWT LHPWAIYAIV GLAIAYSTFR VGRKQLLSSA FVPLIGEKGA EGWLGKLIDI
LAIIATVFGT ACSLGLGALQ IGAGLSAANI IEDPSDWTIV GIVSVLTLAF IFSAISGVGK
GIQYLSNANM VLAALLAIFV FVVGPTVSIL NLLPGSIGNY LSNFFQMAGR TAMSADGTAG
EWLGSWTIFY WAWWISWSPF VGMFLARISR GRSIREFILG VLLVPAGVST VWFSIFGGTA
IVFEQNGESI WGDGAAEEQL FGLLHALPGG QIMGIIAMIL LGTFFITSAD SASTVMGTMS
QHGQLEANKW VTAAWGVATA AIGLTLLLSG GDNALSNLQN VTIVAATPFL FVVIGLMFAL
VKDLSNDVIY LEYREQQRFN ARLARERRVH NEHRKRELAA KRRRERKASG AGKRR


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